DrLLPS - Data resource of LLPS

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LLPS-Hos-3149
ABL1

▼ OVERVIEW


Status:	Reviewed
Protein Name:	Tyrosine-protein kinase ABL1; Abelson murine leukemia viral oncogene homolog 1; Abelson tyrosine-protein kinase 1; Proto-oncogene c-Abl; p150
Gene Name:	ABL1, ABL, JTK7
Ensembl Gene:	ENSG00000097007.17
Ensembl Protein:	ENSP00000323315.5
Organism:	Homo sapiens
Taxa ID:	9606
LLPS Type:	Scaffold

PDB: 1JU5 (A, B, C) More

▼ PROPERTY

——— Disorder propensity (calculated by IUPred2A)

▼ Classification

Minimum set of experiments:
Minimum set of experiments:

Experiment	Description	PMIDs
In vitro
Assembly	"...The liquid droplets disassembled almost completely by the end of the incubation period, whereas liquid droplets formed by NCK1 SH3(3) (without FUS attachment) plus ABL1 PRM(4) were not affected by DNA-PK."	28924037

Experiment	Description	PMIDs
In vitro
Assembly	"...We began by studying three independent pairs of interacting multivalent scaffolds in vitro. These systems consisted of (1) a protein with ten repeats of human SUMO3 (polySUMO) and a protein with ten repeats of the SUMO Interaction Motif (SIM) from PIASx (polySIM); (2) a protein with four repeats of the second SH3 domain from Nck (polySH3) and a protein containing four repeats of a Proline-Rich Motif (PRM) from Abl1 (polyPRM); and (3) the PTB protein (contains four RNA recognition motifs [RRMs]) and an RNA with five repeats of the RRM recognition element UCUCU (polyUCUCU). Each of these pairs phase separated when mixed together, but not when individual components were alone in solution."	27374333
In cells
Experiment	Description	PMIDs
Assembly	"...In fluorescence recovery after photobleaching (FRAP) experiments, clients diffused much more rapidly within droplets than did scaffolds (i.e., for droplets ~20 μm in diameter, RFP-SIM and polySUMO had exponential recovery constants, t, of 1.3 min and 38 min, respectively; Figure S5 and Table S3). Thus, scaffold rearrangements likely limit the rate of transitions between compositional states. Scaling recovery times to droplets of 1 μm diameter, as often observed in cells, indicates that compositions should interchange on a timescale of ~6 s in natural systems (Table S3)."	27374333

Condensates:

Condensate	Description	Tissue/Cell	PMIDs
Droplet	"...The liquid droplets disassembled almost completely by the end of the incubation period, whereas liquid droplets formed by NCK1 SH3(3) (without FUS attachment) plus ABL1 PRM(4) were not affected by DNA-PK."	In vitro	28924037
Nucleolus	Predicted from orthologs	N/A	(View)

Organism	DrLLPS ID	UniProt ID	LLPS type	Condensate	Identity	E-value	Score
Mus musculus	LLPS-Mum-2399	P00520	Client	Nucleolus	86.47	0.0	1865

▼ FUNCTION

Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (PubMed:28428613). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner. Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (By similarity).

▼ CROSS REFERENCE

Database	Nucleotide ID	Protein ID
Ensembl	ENST00000318560.5	ENSP00000323315.5
Ensembl	ENST00000372348.6	ENSP00000361423.2
Ensembl	ENST00000393293.4	ENSP00000376971.4
UniProt		P00519, ABL1_HUMAN, A3KFJ3, Q13869, Q13870, Q16133, Q17R61, Q45F09
GeneBank	DQ145721, U07563, AL161733, M14752, U07561, AL359092, BC117451, X16416, CH471090, S69223	AAB60394.1, AAZ38718.1, AAD14034.1, AAB60393.1, CAA34438.1, AAA51561.1, EAW87948.1, AAI17452.1
RefSeq	NM_005157.5, NM_007313.2	NP_005148.2, NP_009297.2
Entrez	25

▼ SEQUENCE

Protein Sequence (FASTA)
1 MGQQPGKVLG DQRRPSLPAL HFIKGAGKKE SSRHGGPHCN VFVEHEALQR PVASDFEPQG 60 61 LSEAARWNSK ENLLAGPSEN DPNLFVALYD FVASGDNTLS ITKGEKLRVL GYNHNGEWCE 120 121 AQTKNGQGWV PSNYITPVNS LEKHSWYHGP VSRNAAEYLL SSGINGSFLV RESESSPGQR 180 181 SISLRYEGRV YHYRINTASD GKLYVSSESR FNTLAELVHH HSTVADGLIT TLHYPAPKRN 240 241 KPTVYGVSPN YDKWEMERTD ITMKHKLGGG QYGEVYEGVW KKYSLTVAVK TLKEDTMEVE 300 301 EFLKEAAVMK EIKHPNLVQL LGVCTREPPF YIITEFMTYG NLLDYLRECN RQEVNAVVLL 360 361 YMATQISSAM EYLEKKNFIH RDLAARNCLV GENHLVKVAD FGLSRLMTGD TYTAHAGAKF 420 421 PIKWTAPESL AYNKFSIKSD VWAFGVLLWE IATYGMSPYP GIDLSQVYEL LEKDYRMERP 480 481 EGCPEKVYEL MRACWQWNPS DRPSFAEIHQ AFETMFQESS ISDEVEKELG KQGVRGAVST 540 541 LLQAPELPTK TRTSRRAAEH RDTTDVPEMP HSKGQGESDP LDHEPAVSPL LPRKERGPPE 600 601 GGLNEDERLL PKDKKTNLFS ALIKKKKKTA PTPPKRSSSF REMDGQPERR GAGEEEGRDI 660 661 SNGALAFTPL DTADPAKSPK PSNGAGVPNG ALRESGGSGF RSPHLWKKSS TLTSSRLATG 720 721 EEEGGGSSSK RFLRSCSASC VPHGAKDTEW RSVTLPRDLQ STGRQFDSST FGGHKSEKPA 780 781 LPRKRAGENR SDQVTRGTVT PPPRLVKKNE EAADEVFKDI MESSPGSSPP NLTPKPLRRQ 840 841 VTVAPASGLP HKEEAGKGSA LGTPAAAEPV TPTSKAGSGA PGGTSKGPAE ESRVRRHKHS 900 901 SESPGRDKGK LSRLKPAPPP PPAASAGKAG GKPSQSPSQE AAGEAVLGAK TKATSLVDAV 960 961 NSDAAKPSQP GEGLKKPVLP ATPKPQSAKP SGTPISPAPV PSTLPSASSA LAGDQPSSTA 1020 1021 FIPLISTRVS LRKTRQPPER IASGAITKGV VLDSTEALCL AISRNSEQMA SHSAVLEAGK 1080 1081 NLYTFCVSYV DSIQQMRNKF AFREAINKLE NNLRELQICP ATAGSGPAAT QDFSKLLSSV 1140 1141 KEISDIVQR 1149
Nucleotide CDS Sequence (FASTA)
1 ATGTTGGAGA TCTGCCTGAA GCTGGTGGGC TGCAAATCCA AGAAGGGGCT GTCCTCGTCC 60 61 TCCAGCTGTT ATCTGGAAGA AGCCCTTCAG CGGCCAGTAG CATCTGACTT TGAGCCTCAG 120 121 GGTCTGAGTG AAGCCGCTCG TTGGAACTCC AAGGAAAACC TTCTCGCTGG ACCCAGTGAA 180 181 AATGACCCCA ACCTTTTCGT TGCACTGTAT GATTTTGTGG CCAGTGGAGA TAACACTCTA 240 241 AGCATAACTA AAGGTGAAAA GCTCCGGGTC TTAGGCTATA ATCACAATGG GGAATGGTGT 300 301 GAAGCCCAAA CCAAAAATGG CCAAGGCTGG GTCCCAAGCA ACTACATCAC GCCAGTCAAC 360 361 AGTCTGGAGA AACACTCCTG GTACCATGGG CCTGTGTCCC GCAATGCCGC TGAGTATCTG 420 421 CTGAGCAGCG GGATCAATGG CAGCTTCTTG GTGCGTGAGA GTGAGAGCAG TCCTGGCCAG 480 481 AGGTCCATCT CGCTGAGATA CGAAGGGAGG GTGTACCATT ACAGGATCAA CACTGCTTCT 540 541 GATGGCAAGC TCTACGTCTC CTCCGAGAGC CGCTTCAACA CCCTGGCCGA GTTGGTTCAT 600 601 CATCATTCAA CGGTGGCCGA CGGGCTCATC ACCACGCTCC ATTATCCAGC CCCAAAGCGC 660 661 AACAAGCCCA CTGTCTATGG TGTGTCCCCC AACTACGACA AGTGGGAGAT GGAACGCACG 720 721 GACATCACCA TGAAGCACAA GCTGGGCGGG GGCCAGTACG GGGAGGTGTA CGAGGGCGTG 780 781 TGGAAGAAAT ACAGCCTGAC GGTGGCCGTG AAGACCTTGA AGGAGGACAC CATGGAGGTG 840 841 GAAGAGTTCT TGAAAGAAGC TGCAGTCATG AAAGAGATCA AACACCCTAA CCTGGTGCAG 900 901 CTCCTTGGGG TCTGCACCCG GGAGCCCCCG TTCTATATCA TCACTGAGTT CATGACCTAC 960 961 GGGAACCTCC TGGACTACCT GAGGGAGTGC AACCGGCAGG AGGTGAACGC CGTGGTGCTG 1020 1021 CTGTACATGG CCACTCAGAT CTCGTCAGCC ATGGAGTACC TGGAGAAGAA AAACTTCATC 1080 1081 CACAGAGATC TTGCTGCCCG AAACTGCCTG GTAGGGGAGA ACCACTTGGT GAAGGTAGCT 1140 1141 GATTTTGGCC TGAGCAGGTT GATGACAGGG GACACCTACA CAGCCCATGC TGGAGCCAAG 1200 1201 TTCCCCATCA AATGGACTGC ACCCGAGAGC CTGGCCTACA ACAAGTTCTC CATCAAGTCC 1260 1261 GACGTCTGGG CATTTGGAGT ATTGCTTTGG GAAATTGCTA CCTATGGCAT GTCCCCTTAC 1320 1321 CCGGGAATTG ACCTGTCCCA GGTGTATGAG CTGCTAGAGA AGGACTACCG CATGGAGCGC 1380 1381 CCAGAAGGCT GCCCAGAGAA GGTCTATGAA CTCATGCGAG CATGTTGGCA GTGGAATCCC 1440 1441 TCTGACCGGC CCTCCTTTGC TGAAATCCAC CAAGCCTTTG AAACAATGTT CCAGGAATCC 1500 1501 AGTATCTCAG ACGAAGTGGA AAAGGAGCTG GGGAAACAAG GCGTCCGTGG GGCTGTGAGT 1560 1561 ACCTTGCTGC AGGCCCCAGA GCTGCCCACC AAGACGAGGA CCTCCAGGAG AGCTGCAGAG 1620 1621 CACAGAGACA CCACTGACGT GCCTGAGATG CCTCACTCCA AGGGCCAGGG AGAGAGCGAT 1680 1681 CCTCTGGACC ATGAGCCTGC CGTGTCTCCA TTGCTCCCTC GAAAAGAGCG AGGTCCCCCG 1740 1741 GAGGGCGGCC TGAATGAAGA TGAGCGCCTT CTCCCCAAAG ACAAAAAGAC CAACTTGTTC 1800 1801 AGCGCCTTGA TCAAGAAGAA GAAGAAGACA GCCCCAACCC CTCCCAAACG CAGCAGCTCC 1860 1861 TTCCGGGAGA TGGACGGCCA GCCGGAGCGC AGAGGGGCCG GCGAGGAAGA GGGCCGAGAC 1920 1921 ATCAGCAACG GGGCACTGGC TTTCACCCCC TTGGACACAG CTGACCCAGC CAAGTCCCCA 1980 1981 AAGCCCAGCA ATGGGGCTGG GGTCCCCAAT GGAGCCCTCC GGGAGTCCGG GGGCTCAGGC 2040 2041 TTCCGGTCTC CCCACCTGTG GAAGAAGTCC AGCACGCTGA CCAGCAGCCG CCTAGCCACC 2100 2101 GGCGAGGAGG AGGGCGGTGG CAGCTCCAGC AAGCGCTTCC TGCGCTCTTG CTCCGCCTCC 2160 2161 TGCGTTCCCC ATGGGGCCAA GGACACGGAG TGGAGGTCAG TCACGCTGCC TCGGGACTTG 2220 2221 CAGTCCACGG GAAGACAGTT TGACTCGTCC ACATTTGGAG GGCACAAAAG TGAGAAGCCG 2280 2281 GCTCTGCCTC GGAAGAGGGC AGGGGAGAAC AGGTCTGACC AGGTGACCCG AGGCACAGTA 2340 2341 ACGCCTCCCC CCAGGCTGGT GAAAAAGAAT GAGGAAGCTG CTGATGAGGT CTTCAAAGAC 2400 2401 ATCATGGAGT CCAGCCCGGG CTCCAGCCCG CCCAACCTGA CTCCAAAACC CCTCCGGCGG 2460 2461 CAGGTCACCG TGGCCCCTGC CTCGGGCCTC CCCCACAAGG AAGAAGCTGG AAAGGGCAGT 2520 2521 GCCTTAGGGA CCCCTGCTGC AGCTGAGCCA GTGACCCCCA CCAGCAAAGC AGGCTCAGGT 2580 2581 GCACCAGGGG GCACCAGCAA GGGCCCCGCC GAGGAGTCCA GAGTGAGGAG GCACAAGCAC 2640 2641 TCCTCTGAGT CGCCAGGGAG GGACAAGGGG AAATTGTCCA GGCTCAAACC TGCCCCGCCG 2700 2701 CCCCCACCAG CAGCCTCTGC AGGGAAGGCT GGAGGAAAGC CCTCGCAGAG CCCGAGCCAG 2760 2761 GAGGCGGCCG GGGAGGCAGT CCTGGGCGCA AAGACAAAAG CCACGAGTCT GGTTGATGCT 2820 2821 GTGAACAGTG ACGCTGCCAA GCCCAGCCAG CCGGGAGAGG GCCTCAAAAA GCCCGTGCTC 2880 2881 CCGGCCACTC CAAAGCCACA GTCCGCCAAG CCGTCGGGGA CCCCCATCAG CCCAGCCCCC 2940 2941 GTTCCCTCCA CGTTGCCATC AGCATCCTCG GCCCTGGCAG GGGACCAGCC GTCTTCCACC 3000 3001 GCCTTCATCC CTCTCATATC AACCCGAGTG TCTCTTCGGA AAACCCGCCA GCCTCCAGAG 3060 3061 CGGATCGCCA GCGGCGCCAT CACCAAGGGC GTGGTCCTGG ACAGCACCGA GGCGCTGTGC 3120 3121 CTCGCCATCT CTAGGAACTC CGAGCAGATG GCCAGCCACA GCGCAGTGCT GGAGGCCGGC 3180 3181 AAAAACCTCT ACACGTTCTG CGTGAGCTAT GTGGATTCCA TCCAGCAAAT GAGGAACAAG 3240 3241 TTTGCCTTCC GAGAGGCCAT CAACAAACTG GAGAATAATC TCCGGGAGCT TCAGATCTGC 3300 3301 CCGGCGACAG CAGGCAGTGG TCCAGCGGCC ACTCAGGACT TCAGCAAGCT CCTCAGTTCG 3360 3361 GTGAAGGAAA TCAGTGACAT AGTGCAGAGG TAG 3393

Nucleotide Sequence

>LLPS-Hos-3149|ENSG00000097007.17
ATGTTGGAGATCTGCCTGAAGCTGGTGGGCTGCAAATCCAAGAAGGGGCTGTCCTCGTCCTCCAGCTGTTATCTGGAAGAAGCCCTTCAGCGGCCAGTAGCATCTGACTTTGAGCCTCAGGGTCTGAGTGAAGCCGCTCGTTGGAACTCCAAGGAAAACCTTCTCGCTGGACCCAGTGAAAATGACCCCAACCTTTTCGTTGCACTGTATGATTTTGTGGCCAGTGGAGATAACACTCTAAGCATAACTAAAGGTGAAAAGCTCCGGGTCTTAGGCTATAATCACAATGGGGAATGGTGTGAAGCCCAAACCAAAAATGGCCAAGGCTGGGTCCCAAGCAACTACATCACGCCAGTCAACAGTCTGGAGAAACACTCCTGGTACCATGGGCCTGTGTCCCGCAATGCCGCTGAGTATCTGCTGAGCAGCGGGATCAATGGCAGCTTCTTGGTGCGTGAGAGTGAGAGCAGTCCTGGCCAGAGGTCCATCTCGCTGAGATACGAAGGGAGGGTGTACCATTACAGGATCAACACTGCTTCTGATGGCAAGCTCTACGTCTCCTCCGAGAGCCGCTTCAACACCCTGGCCGAGTTGGTTCATCATCATTCAACGGTGGCCGACGGGCTCATCACCACGCTCCATTATCCAGCCCCAAAGCGCAACAAGCCCACTGTCTATGGTGTGTCCCCCAACTACGACAAGTGGGAGATGGAACGCACGGACATCACCATGAAGCACAAGCTGGGCGGGGGCCAGTACGGGGAGGTGTACGAGGGCGTGTGGAAGAAATACAGCCTGACGGTGGCCGTGAAGACCTTGAAGGAGGACACCATGGAGGTGGAAGAGTTCTTGAAAGAAGCTGCAGTCATGAAAGAGATCAAACACCCTAACCTGGTGCAGCTCCTTGGGGTCTGCACCCGGGAGCCCCCGTTCTATATCATCACTGAGTTCATGACCTACGGGAACCTCCTGGACTACCTGAGGGAGTGCAACCGGCAGGAGGTGAACGCCGTGGTGCTGCTGTACATGGCCACTCAGATCTCGTCAGCCATGGAGTACCTGGAGAAGAAAAACTTCATCCACAGAGATCTTGCTGCCCGAAACTGCCTGGTAGGGGAGAACCACTTGGTGAAGGTAGCTGATTTTGGCCTGAGCAGGTTGATGACAGGGGACACCTACACAGCCCATGCTGGAGCCAAGTTCCCCATCAAATGGACTGCACCCGAGAGCCTGGCCTACAACAAGTTCTCCATCAAGTCCGACGTCTGGGCATTTGGAGTATTGCTTTGGGAAATTGCTACCTATGGCATGTCCCCTTACCCGGGAATTGACCTGTCCCAGGTGTATGAGCTGCTAGAGAAGGACTACCGCATGGAGCGCCCAGAAGGCTGCCCAGAGAAGGTCTATGAACTCATGCGAGCATGTTGGCAGTGGAATCCCTCTGACCGGCCCTCCTTTGCTGAAATCCACCAAGCCTTTGAAACAATGTTCCAGGAATCCAGTATCTCAGACGAAGTGGAAAAGGAGCTGGGGAAACAAGGCGTCCGTGGGGCTGTGAGTACCTTGCTGCAGGCCCCAGAGCTGCCCACCAAGACGAGGACCTCCAGGAGAGCTGCAGAGCACAGAGACACCACTGACGTGCCTGAGATGCCTCACTCCAAGGGCCAGGGAGAGAGCGATCCTCTGGACCATGAGCCTGCCGTGTCTCCATTGCTCCCTCGAAAAGAGCGAGGTCCCCCGGAGGGCGGCCTGAATGAAGATGAGCGCCTTCTCCCCAAAGACAAAAAGACCAACTTGTTCAGCGCCTTGATCAAGAAGAAGAAGAAGACAGCCCCAACCCCTCCCAAACGCAGCAGCTCCTTCCGGGAGATGGACGGCCAGCCGGAGCGCAGAGGGGCCGGCGAGGAAGAGGGCCGAGACATCAGCAACGGGGCACTGGCTTTCACCCCCTTGGACACAGCTGACCCAGCCAAGTCCCCAAAGCCCAGCAATGGGGCTGGGGTCCCCAATGGAGCCCTCCGGGAGTCCGGGGGCTCAGGCTTCCGGTCTCCCCACCTGTGGAAGAAGTCCAGCACGCTGACCAGCAGCCGCCTAGCCACCGGCGAGGAGGAGGGCGGTGGCAGCTCCAGCAAGCGCTTCCTGCGCTCTTGCTCCGCCTCCTGCGTTCCCCATGGGGCCAAGGACACGGAGTGGAGGTCAGTCACGCTGCCTCGGGACTTGCAGTCCACGGGAAGACAGTTTGACTCGTCCACATTTGGAGGGCACAAAAGTGAGAAGCCGGCTCTGCCTCGGAAGAGGGCAGGGGAGAACAGGTCTGACCAGGTGACCCGAGGCACAGTAACGCCTCCCCCCAGGCTGGTGAAAAAGAATGAGGAAGCTGCTGATGAGGTCTTCAAAGACATCATGGAGTCCAGCCCGGGCTCCAGCCCGCCCAACCTGACTCCAAAACCCCTCCGGCGGCAGGTCACCGTGGCCCCTGCCTCGGGCCTCCCCCACAAGGAAGAAGCTGGAAAGGGCAGTGCCTTAGGGACCCCTGCTGCAGCTGAGCCAGTGACCCCCACCAGCAAAGCAGGCTCAGGTGCACCAGGGGGCACCAGCAAGGGCCCCGCCGAGGAGTCCAGAGTGAGGAGGCACAAGCACTCCTCTGAGTCGCCAGGGAGGGACAAGGGGAAATTGTCCAGGCTCAAACCTGCCCCGCCGCCCCCACCAGCAGCCTCTGCAGGGAAGGCTGGAGGAAAGCCCTCGCAGAGCCCGAGCCAGGAGGCGGCCGGGGAGGCAGTCCTGGGCGCAAAGACAAAAGCCACGAGTCTGGTTGATGCTGTGAACAGTGACGCTGCCAAGCCCAGCCAGCCGGGAGAGGGCCTCAAAAAGCCCGTGCTCCCGGCCACTCCAAAGCCACAGTCCGCCAAGCCGTCGGGGACCCCCATCAGCCCAGCCCCCGTTCCCTCCACGTTGCCATCAGCATCCTCGGCCCTGGCAGGGGACCAGCCGTCTTCCACCGCCTTCATCCCTCTCATATCAACCCGAGTGTCTCTTCGGAAAACCCGCCAGCCTCCAGAGCGGATCGCCAGCGGCGCCATCACCAAGGGCGTGGTCCTGGACAGCACCGAGGCGCTGTGCCTCGCCATCTCTAGGAACTCCGAGCAGATGGCCAGCCACAGCGCAGTGCTGGAGGCCGGCAAAAACCTCTACACGTTCTGCGTGAGCTATGTGGATTCCATCCAGCAAATGAGGAACAAGTTTGCCTTCCGAGAGGCCATCAACAAACTGGAGAATAATCTCCGGGAGCTTCAGATCTGCCCGGCGACAGCAGGCAGTGGTCCAGCGGCCACTCAGGACTTCAGCAAGCTCCTCAGTTCGGTGAAGGAAATCAGTGACATAGTGCAGAGGTAG

▼ KEYWORD

ID	Family
KW-0002	3D-structure
KW-0007	Acetylation
KW-0025	Alternative splicing
KW-0053	Apoptosis
KW-0067	ATP-binding
KW-0072	Autophagy
KW-0130	Cell adhesion
KW-0160	Chromosomal rearrangement
KW-0181	Complete proteome
KW-0963	Cytoplasm
KW-0206	Cytoskeleton
KW-0225	Disease mutation
KW-0227	DNA damage
KW-0234	DNA repair
KW-0238	DNA-binding
KW-0254	Endocytosis
KW-0418	Kinase
KW-0449	Lipoprotein
KW-0460	Magnesium
KW-0464	Manganese
KW-0472	Membrane
KW-0479	Metal-binding
KW-0496	Mitochondrion
KW-0519	Myristate
KW-0547	Nucleotide-binding
KW-0539	Nucleus
KW-0597	Phosphoprotein
KW-0621	Polymorphism
KW-0656	Proto-oncogene
KW-1185	Reference proteome
KW-0727	SH2 domain
KW-0728	SH3 domain
KW-0808	Transferase
KW-0829	Tyrosine-protein kinase
KW-0832	Ubl conjugation

▼ GENE ONTOLOGY

ID	Classification	Description
GO:0015629	Cellular Component	Actin cytoskeleton
GO:0031252	Cellular Component	Cell leading edge
GO:0005737	Cellular Component	Cytoplasm
GO:0005829	Cellular Component	Cytosol
GO:0030425	Cellular Component	Dendrite
GO:0005739	Cellular Component	Mitochondrion
GO:0043025	Cellular Component	Neuronal cell body
GO:0016604	Cellular Component	Nuclear body
GO:0031965	Cellular Component	Nuclear membrane
GO:0005730	Cellular Component	Nucleolus
GO:0005654	Cellular Component	Nucleoplasm
GO:0005634	Cellular Component	Nucleus
GO:0048471	Cellular Component	Perinuclear region of cytoplasm
GO:0098794	Cellular Component	Postsynapse
GO:0032991	Cellular Component	Protein-containing complex
GO:0051015	Molecular Function	Actin filament binding
GO:0003785	Molecular Function	Actin monomer binding
GO:0005524	Molecular Function	ATP binding
GO:0000405	Molecular Function	Bubble DNA binding
GO:0003677	Molecular Function	DNA binding
GO:0046875	Molecular Function	Ephrin receptor binding
GO:0000400	Molecular Function	Four-way junction DNA binding
GO:0016301	Molecular Function	Kinase activity
GO:0000287	Molecular Function	Magnesium ion binding
GO:0030145	Molecular Function	Manganese ion binding
GO:0051019	Molecular Function	Mitogen-activated protein kinase binding
GO:0038191	Molecular Function	Neuropilin binding
GO:0004515	Molecular Function	Nicotinate-nucleotide adenylyltransferase activity
GO:0004715	Molecular Function	Non-membrane spanning protein tyrosine kinase activity
GO:0001784	Molecular Function	Phosphotyrosine residue binding
GO:0070064	Molecular Function	Proline-rich region binding
GO:0008022	Molecular Function	Protein C-terminus binding
GO:0004672	Molecular Function	Protein kinase activity
GO:0005080	Molecular Function	Protein kinase C binding
GO:0004713	Molecular Function	Protein tyrosine kinase activity
GO:1990837	Molecular Function	Sequence-specific double-stranded DNA binding
GO:0042169	Molecular Function	SH2 domain binding
GO:0017124	Molecular Function	SH3 domain binding
GO:0019905	Molecular Function	Syntaxin binding
GO:0003713	Molecular Function	Transcription coactivator activity
GO:0030036	Biological Process	Actin cytoskeleton organization
GO:0090135	Biological Process	Actin filament branching
GO:0050798	Biological Process	Activated T cell proliferation
GO:1990051	Biological Process	Activation of protein kinase C activity
GO:0046632	Biological Process	Alpha-beta T cell differentiation
GO:0006914	Biological Process	Autophagy
GO:0002322	Biological Process	B cell proliferation involved in immune response
GO:0050853	Biological Process	B cell receptor signaling pathway
GO:0001922	Biological Process	B-1 B cell homeostasis
GO:0060020	Biological Process	Bergmann glial cell differentiation
GO:0072358	Biological Process	Cardiovascular system development
GO:0007050	Biological Process	Cell cycle arrest
GO:0030154	Biological Process	Cell differentiation
GO:0006464	Biological Process	Cellular protein modification process
GO:0006974	Biological Process	Cellular response to DNA damage stimulus
GO:1903351	Biological Process	Cellular response to dopamine
GO:0070301	Biological Process	Cellular response to hydrogen peroxide
GO:0071222	Biological Process	Cellular response to lipopolysaccharide
GO:0034599	Biological Process	Cellular response to oxidative stress
GO:0021587	Biological Process	Cerebellum morphogenesis
GO:0048668	Biological Process	Collateral sprouting
GO:0071103	Biological Process	DNA conformation change
GO:0006975	Biological Process	DNA damage induced protein phosphorylation
GO:0043542	Biological Process	Endothelial cell migration
GO:0007173	Biological Process	Epidermal growth factor receptor signaling pathway
GO:0045184	Biological Process	Establishment of protein localization
GO:0038096	Biological Process	Fc-gamma receptor signaling pathway involved in phagocytosis
GO:0007229	Biological Process	Integrin-mediated signaling pathway
GO:0008630	Biological Process	Intrinsic apoptotic signaling pathway in response to DNA damage
GO:0030035	Biological Process	Microspike assembly
GO:0006298	Biological Process	Mismatch repair
GO:0051882	Biological Process	Mitochondrial depolarization
GO:0000278	Biological Process	Mitotic cell cycle
GO:0030514	Biological Process	Negative regulation of BMP signaling pathway
GO:0022408	Biological Process	Negative regulation of cell-cell adhesion
GO:2000773	Biological Process	Negative regulation of cellular senescence
GO:2000352	Biological Process	Negative regulation of endothelial cell apoptotic process
GO:0070373	Biological Process	Negative regulation of ERK1 and ERK2 cascade
GO:0043124	Biological Process	Negative regulation of I-kappaB kinase/NF-kappaB signaling
GO:1900272	Biological Process	Negative regulation of long-term synaptic potentiation
GO:0045930	Biological Process	Negative regulation of mitotic cell cycle
GO:1900275	Biological Process	Negative regulation of phospholipase C activity
GO:0071901	Biological Process	Negative regulation of protein serine/threonine kinase activity
GO:0051444	Biological Process	Negative regulation of ubiquitin-protein transferase activity
GO:0001843	Biological Process	Neural tube closure
GO:0060563	Biological Process	Neuroepithelial cell differentiation
GO:0050885	Biological Process	Neuromuscular process controlling balance
GO:0038189	Biological Process	Neuropilin signaling pathway
GO:0038083	Biological Process	Peptidyl-tyrosine autophosphorylation
GO:0018108	Biological Process	Peptidyl-tyrosine phosphorylation
GO:0035791	Biological Process	Platelet-derived growth factor receptor-beta signaling pathway
GO:1905555	Biological Process	Positive regulation blood vessel branching
GO:2000251	Biological Process	Positive regulation of actin cytoskeleton reorganization
GO:1904531	Biological Process	Positive regulation of actin filament binding
GO:0043065	Biological Process	Positive regulation of apoptotic process
GO:0090050	Biological Process	Positive regulation of cell migration involved in sprouting angiogenesis
GO:0007204	Biological Process	Positive regulation of cytosolic calcium ion concentration
GO:0010595	Biological Process	Positive regulation of endothelial cell migration
GO:0070374	Biological Process	Positive regulation of ERK1 and ERK2 cascade
GO:0051894	Biological Process	Positive regulation of focal adhesion assembly
GO:0043123	Biological Process	Positive regulation of I-kappaB kinase/NF-kappaB signaling
GO:1902715	Biological Process	Positive regulation of interferon-gamma secretion
GO:1900042	Biological Process	Positive regulation of interleukin-2 secretion
GO:1904528	Biological Process	Positive regulation of microtubule binding
GO:0045931	Biological Process	Positive regulation of mitotic cell cycle
GO:0051149	Biological Process	Positive regulation of muscle cell differentiation
GO:1901216	Biological Process	Positive regulation of neuron death
GO:0033690	Biological Process	Positive regulation of osteoblast proliferation
GO:0051353	Biological Process	Positive regulation of oxidoreductase activity
GO:0050731	Biological Process	Positive regulation of peptidyl-tyrosine phosphorylation
GO:0001934	Biological Process	Positive regulation of protein phosphorylation
GO:0051281	Biological Process	Positive regulation of release of sequestered calcium ion into cytosol
GO:0051496	Biological Process	Positive regulation of stress fiber assembly
GO:1900026	Biological Process	Positive regulation of substrate adhesion-dependent cell spreading
GO:0045944	Biological Process	Positive regulation of transcription by RNA polymerase II
GO:2000096	Biological Process	Positive regulation of Wnt signaling pathway, planar cell polarity pathway
GO:0009791	Biological Process	Post-embryonic development
GO:0046777	Biological Process	Protein autophosphorylation
GO:0006468	Biological Process	Protein phosphorylation
GO:0032956	Biological Process	Regulation of actin cytoskeleton organization
GO:2000249	Biological Process	Regulation of actin cytoskeleton reorganization
GO:0010506	Biological Process	Regulation of autophagy
GO:0030516	Biological Process	Regulation of axon extension
GO:0032489	Biological Process	Regulation of Cdc42 protein signal transduction
GO:0030155	Biological Process	Regulation of cell adhesion
GO:2000145	Biological Process	Regulation of cell motility
GO:0042127	Biological Process	Regulation of cell population proliferation
GO:0030100	Biological Process	Regulation of endocytosis
GO:1903053	Biological Process	Regulation of extracellular matrix organization
GO:1902036	Biological Process	Regulation of hematopoietic stem cell differentiation
GO:0031113	Biological Process	Regulation of microtubule polymerization
GO:1905244	Biological Process	Regulation of modification of synaptic structure
GO:2001020	Biological Process	Regulation of response to DNA damage stimulus
GO:0045580	Biological Process	Regulation of T cell differentiation
GO:0006355	Biological Process	Regulation of transcription, DNA-templated
GO:0006979	Biological Process	Response to oxidative stress
GO:0042770	Biological Process	Signal transduction in response to DNA damage
GO:0048536	Biological Process	Spleen development
GO:0034446	Biological Process	Substrate adhesion-dependent cell spreading
GO:0050852	Biological Process	T cell receptor signaling pathway
GO:0048538	Biological Process	Thymus development
GO:0002333	Biological Process	Transitional one stage B cell differentiation

▼ KEGG

hsa:25

▼ ANNOTATION

Disorder
D²P²	IUPred2A

Domain
SMART	Pfam	InterPro	LCR-eXXXplorer	CDD
PROSITE	Gene3D

PTM
EPSD	PLMD	PhosphoSitePlus	dbPTM	HPRD
BioGRID	PTMcode

Variation
dbSNP	VarCards	rSNPBase

Mutation
TCGA	ICGC	COSMIC	CGAP	IntOGen
BioMuta

Interaction
HINT	InWeb_IM	RISE	TRRUST	BindingDB
RAIN	Mentha	PINA	IID	MIST
DifferentialNET	RNAct

Disease
ClinVar	PTMD	BRONCO	TumorFusions	OMIM
DisGeNET	GWASdb	ActiveDriverDB

Drug
DrugBank	TTD	GRAC	ADReCS-Target	ECOdrug
DGIdb	CTD

Physicochemical
Compute pI/Mw	AAindex

Function
THANATOS	iEKPD	PIRSF	CORUM

Proteomics
THPA	HPM

Structure
PDB	MMDB

Localization
COMPARTMENTS

Expression
TCGA	ICGC	COSMIC	GEO	ArrayExpress
TISSUES	BioXpress	THPA

Element
UTRdb	circBase	CircNet	miRTarBase	miRWalk
miRecords	miRcode	RAID	microRNA.org	m6AVar

Methylation
TCGA	ICGC	COSMIC	MethyCancer

▼ ORTHOLOGY

DrLLPS ID	Organism	Identity	E-value	Score
LLPS-Maf-0591	Macaca fascicularis	100.0	2e-21	105
LLPS-Pat-3942	Pan troglodytes	99.91	0.0	2174
LLPS-Pap-4673	Pan paniscus	99.83	0.0	2170
LLPS-Gog-2697	Gorilla gorilla	99.74	0.0	2171
LLPS-Cea-4191	Cercocebus atys	99.04	0.0	2153
LLPS-Poa-2765	Pongo abelii	98.95	0.0	1733
LLPS-Man-2569	Macaca nemestrina	98.87	0.0	2148
LLPS-Mal-1140	Mandrillus leucophaeus	98.87	0.0	2150
LLPS-Rhb-0374	Rhinopithecus bieti	98.78	0.0	2150
LLPS-Mam-3902	Macaca mulatta	98.78	0.0	2150
LLPS-Chs-0412	Chlorocebus sabaeus	98.73	0.0	2046
LLPS-Aon-2766	Aotus nancymaae	97.39	0.0	2100
LLPS-Caj-1967	Callithrix jacchus	97.13	0.0	2097
LLPS-Fud-0848	Fukomys damarensis	96.96	0.0	1058
LLPS-Paa-0739	Papio anubis	94.78	0.0	1979
LLPS-Ova-3262	Ovis aries	94.72	0.0	1483
LLPS-Otg-2068	Otolemur garnettii	92.68	0.0	1924
LLPS-Eqc-2407	Equus caballus	92.09	0.0	1998
LLPS-Myl-3931	Myotis lucifugus	91.68	0.0	1888
LLPS-Fec-4397	Felis catus	91.66	0.0	1973
LLPS-Mod-3358	Monodelphis domestica	91.09	0.0	1358
LLPS-Ict-2823	Ictidomys tridecemlineatus	91.05	0.0	1985
LLPS-Aim-4092	Ailuropoda melanoleuca	91.05	0.0	1983
LLPS-Sus-1779	Sus scrofa	90.96	0.0	1989
LLPS-Caf-3726	Canis familiaris	90.7	0.0	1955
LLPS-Loa-1004	Loxodonta africana	90.62	0.0	1939
LLPS-Bot-3819	Bos taurus	90.03	0.0	1961
LLPS-Mup-2310	Mustela putorius furo	89.91	0.0	1933
LLPS-Urm-3951	Ursus maritimus	89.83	0.0	1942
LLPS-Cap-2792	Cavia porcellus	88.97	0.0	1914
LLPS-Mea-1831	Mesocricetus auratus	88.01	0.0	1891
LLPS-Ran-2700	Rattus norvegicus	86.82	0.0	1886
LLPS-Mum-2399	Mus musculus	86.73	0.0	1864
LLPS-Leo-2167	Lepisosteus oculatus	86.21	0.0	1041
LLPS-Sah-2411	Sarcophilus harrisii	86.02	0.0	1760
LLPS-Orc-2926	Oryctolagus cuniculus	84.55	0.0	1682
LLPS-Ora-1675	Ornithorhynchus anatinus	84.48	0.0	1761
LLPS-Tag-2681	Taeniopygia guttata	83.74	0.0	1818
LLPS-Fia-1210	Ficedula albicollis	82.99	0.0	1717
LLPS-Anp-1176	Anas platyrhynchos	82.81	0.0	1718
LLPS-Gaga-3980	Gallus gallus	82.53	0.0	1707
LLPS-Meg-1951	Meleagris gallopavo	82.43	0.0	1704
LLPS-Pes-2976	Pelodiscus sinensis	81.84	0.0	1684
LLPS-Nol-1141	Nomascus leucogenys	79.82	0.0	1596
LLPS-Lac-2151	Latimeria chalumnae	77.85	0.0	1625
LLPS-Drm-1666	Drosophila melanogaster	75.32	0.0	749
LLPS-Anc-2773	Anolis carolinensis	74.51	0.0	1504
LLPS-Icp-3407	Ictalurus punctatus	69.14	0.0	1367
LLPS-Xim-0804	Xiphophorus maculatus	68.93	0.0	1109
LLPS-Scm-2735	Scophthalmus maximus	68.77	0.0	1354
LLPS-Scf-1165	Scleropages formosus	68.72	0.0	1385
LLPS-Dar-0801	Danio rerio	68.59	0.0	1330
LLPS-Asm-3326	Astyanax mexicanus	68.44	0.0	1403
LLPS-Gaa-1968	Gasterosteus aculeatus	67.8	0.0	1324
LLPS-Cii-0103	Ciona intestinalis	67.66	0.0	617
LLPS-Tar-3456	Takifugu rubripes	67.57	0.0	1323
LLPS-Xet-1890	Xenopus tropicalis	66.67	0.0	1264
LLPS-Orn-3640	Oreochromis niloticus	66.12	0.0	1301
LLPS-Pof-1524	Poecilia formosa	65.45	0.0	1269
LLPS-Orl-2078	Oryzias latipes	64.29	0.0	1222
LLPS-Cis-0445	Ciona savignyi	63.62	0.0	597
LLPS-Ten-0860	Tetraodon nigroviridis	59.8	0.0	1114
LLPS-Cae-1021	Caenorhabditis elegans	53.04	0.0	585
LLPS-Cas-0715	Carlito syrichta	44.8	7e-110	361
LLPS-Tut-1237	Tursiops truncatus	44.77	6e-109	358
LLPS-Dio-2638	Dipodomys ordii	44.57	5e-110	361

LLPS-Hos-3149ABL1

Protein Sequence

Nucleotide Sequence

LLPS-Hos-3149
ABL1