CABL1_HUMAN - dbPTM
CABL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CABL1_HUMAN
UniProt AC Q8TDN4
Protein Name CDK5 and ABL1 enzyme substrate 1
Gene Name CABLES1
Organism Homo sapiens (Human).
Sequence Length 633
Subcellular Localization Nucleus. Cytoplasm. Located in the cell body and proximal region of the developing axonal shaft of immature neurons. Located in axonal growth cone, but not in the distal part of the axon shaft or in dendritic growth cone of mature neurons (By similar
Protein Description Cyclin-dependent kinase binding protein. Enhances cyclin-dependent kinase tyrosine phosphorylation by nonreceptor tyrosine kinases, such as that of CDK5 by activated ABL1, which leads to increased CDK5 activity and is critical for neuronal development, and that of CDK2 by WEE1, which leads to decreased CDK2 activity and growth inhibition. Positively affects neuronal outgrowth. Plays a role as a regulator for p53/p73-induced cell death (By similarity)..
Protein Sequence MAAAAAAATTAACSSGSAGTDAAGASGLQQPPPQPQPQPAAAAPAQPPPEPPRKPRMDPRRRQAALSFLTNISLDGRLPPQDAEWGGGEEGGAAKPGAGGACGARTRFSLLAAAERGGCIALAAPGTPAAGLAAGSGPCLPQPSSLPPLIPGGHATVSGPGVARGFASPLGAGRASGEQWQPPRPAPLAACAQLQLLDGSGAAGQEELEEDDAFISVQVPAAAFLGSGTPGSGSGSRGRLNSFTQGILPIAFSRPTSQNYCSLEQPGQGGSTSAFEQLQRSRRRLISQRSSLETLEDIEENAPLRRCRTLSGSPRPKNFKKIHFIKNMRQHDTRNGRIVLISGRRSFCSIFSVLPYRDSTQVGDLKLDGGRQSTGAVSLKEIIGLEGVELGADGKTVSYTQFLLPTNAFGARRNTIDSTSSFSQFRNLSHRSLSIGRASGTQGSLDTGSDLGDFMDYDPNLLDDPQWPCGKHKRVLIFPSYMTTVIDYVKPSDLKKDMNETFKEKFPHIKLTLSKIRSLKREMRKLAQEDCGLEEPTVAMAFVYFEKLALKGKLNKQNRKLCAGACVLLAAKIGSDLKKHEVKHLIDKLEEKFRLNRRELIAFEFPVLVALEFALHLPEHEVMPHYRRLVQSS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
22 (in isoform 2)Phosphorylation-13.9718691976
25 (in isoform 2)Phosphorylation-8.8325849741
26PhosphorylationGTDAAGASGLQQPPP
CCCCCCCCCCCCCCC		38.8318691976
26 (in isoform 2)Phosphorylation-38.8325849741
67PhosphorylationRRRQAALSFLTNISL
HHHHHHHHHHHCCCC		17.3027080861
70PhosphorylationQAALSFLTNISLDGR
HHHHHHHHCCCCCCC		28.6127174698
73PhosphorylationLSFLTNISLDGRLPP
HHHHHCCCCCCCCCC		23.6027174698
106PhosphorylationGGACGARTRFSLLAA
CCCCCHHHHHHHHHH		35.2223312004
107MethylationGACGARTRFSLLAAA
CCCCHHHHHHHHHHH		17.38-
109PhosphorylationCGARTRFSLLAAAER
CCHHHHHHHHHHHHH		21.1228857561
168PhosphorylationGVARGFASPLGAGRA
CCCCCCCCCCCCCCC		20.5616964243
242PhosphorylationGSRGRLNSFTQGILP
CCCCCCCHHCCCCHH		33.9723898821
244PhosphorylationRGRLNSFTQGILPIA
CCCCCHHCCCCHHEE		26.2122210691
256PhosphorylationPIAFSRPTSQNYCSL
HEECCCCCCCCCCCC		41.6622210691
257PhosphorylationIAFSRPTSQNYCSLE
EECCCCCCCCCCCCC		21.0722210691
260PhosphorylationSRPTSQNYCSLEQPG
CCCCCCCCCCCCCCC		3.9322817900
262PhosphorylationPTSQNYCSLEQPGQG
CCCCCCCCCCCCCCC		25.28-
287PhosphorylationRSRRRLISQRSSLET
HHHHHHHHHHHHCHH		24.9222617229
290PhosphorylationRRLISQRSSLETLED
HHHHHHHHHCHHHHH		31.4723401153
291PhosphorylationRLISQRSSLETLEDI
HHHHHHHHCHHHHHH		32.2028355574
294PhosphorylationSQRSSLETLEDIEEN
HHHHHCHHHHHHHHH		40.5230183078
309PhosphorylationAPLRRCRTLSGSPRP
CCHHHCCCCCCCCCC		28.9727794612
311PhosphorylationLRRCRTLSGSPRPKN
HHHCCCCCCCCCCCC		36.2926055452
313PhosphorylationRCRTLSGSPRPKNFK
HCCCCCCCCCCCCCC		17.8526055452
333PhosphorylationKNMRQHDTRNGRIVL
ECCCCCCCCCCEEEE		24.74-
346PhosphorylationVLISGRRSFCSIFSV
EEEECCCCCEEEEEE		29.2828857561
373PhosphorylationKLDGGRQSTGAVSLK
EECCCCCCCCCEEHH		27.7025159151
374PhosphorylationLDGGRQSTGAVSLKE
ECCCCCCCCCEEHHH		22.3329978859
378PhosphorylationRQSTGAVSLKEIIGL
CCCCCCEEHHHHHCC		32.9425159151
415PhosphorylationAFGARRNTIDSTSSF
CCCCCCCCCCCCCCH		25.0923401153
418PhosphorylationARRNTIDSTSSFSQF
CCCCCCCCCCCHHHH		26.7423927012
419PhosphorylationRRNTIDSTSSFSQFR
CCCCCCCCCCHHHHC		25.3323927012
420PhosphorylationRNTIDSTSSFSQFRN
CCCCCCCCCHHHHCC		33.0829255136
421PhosphorylationNTIDSTSSFSQFRNL
CCCCCCCCHHHHCCC		29.0729255136
423PhosphorylationIDSTSSFSQFRNLSH
CCCCCCHHHHCCCCC		30.2929255136
429PhosphorylationFSQFRNLSHRSLSIG
HHHHCCCCCCCEEEC		22.0220363803
432PhosphorylationFRNLSHRSLSIGRAS
HCCCCCCCEEECCCC		22.5020363803
434PhosphorylationNLSHRSLSIGRASGT
CCCCCCEEECCCCCC		25.0121712546
439PhosphorylationSLSIGRASGTQGSLD
CEEECCCCCCCCCCC		40.8027251275
444PhosphorylationRASGTQGSLDTGSDL
CCCCCCCCCCCCCCC		17.1628348404
447PhosphorylationGTQGSLDTGSDLGDF
CCCCCCCCCCCCHHH		43.8328348404
449PhosphorylationQGSLDTGSDLGDFMD
CCCCCCCCCCHHHCC		31.5828348404
457PhosphorylationDLGDFMDYDPNLLDD
CCHHHCCCCCCCCCC		22.8528348404
483PhosphorylationLIFPSYMTTVIDYVK
EEECCCEEHHHHHCC		15.0724719451
488PhosphorylationYMTTVIDYVKPSDLK
CEEHHHHHCCHHHHH		10.1527642862
515UbiquitinationHIKLTLSKIRSLKRE
CHHHHHHHHHHHHHH		45.30-
575PhosphorylationLLAAKIGSDLKKHEV
HHHHHHCCHHHHHHH		43.1524719451
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
309TPhosphorylationKinaseAKT1P31749
PSP
313SPhosphorylationKinaseCDK2P24941
Uniprot
313SPhosphorylationKinaseCDK3Q00526
Uniprot
415TPhosphorylationKinaseAKT1P31749
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
313SPhosphorylation

-
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CABL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CABL1_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CABL1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-242; SER-287;SER-290; SER-291; THR-294; SER-311; SER-313; SER-373; THR-415;SER-418; THR-419; SER-421; SER-434 AND SER-439, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-242; SER-287;SER-290; SER-291; SER-311; SER-313; SER-373; THR-415; SER-418 ANDSER-434, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-415, AND MASSSPECTROMETRY.

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