HAKAI_HUMAN - dbPTM
HAKAI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HAKAI_HUMAN
UniProt AC Q75N03
Protein Name E3 ubiquitin-protein ligase Hakai {ECO:0000305}
Gene Name CBLL1 {ECO:0000312|HGNC:HGNC:21225}
Organism Homo sapiens (Human).
Sequence Length 491
Subcellular Localization Nucleus speckle . Nucleus, nucleoplasm . Cytoplasm . Mainly nuclear with some fraction located in the cytoplasm. ZC3H13 is required to anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus.
Protein Description E3 ubiquitin-protein ligase that mediates ubiquitination of several tyrosine-phosphorylated Src substrates, including CDH1, CTTN and DOK1 (By similarity). Targets CDH1 for endocytosis and degradation (By similarity). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. [PubMed: 29507755 Its function in the WMM complex is unknown]
Protein Sequence MDHTDNELQGTNSSGSLGGLDVRRRIPIKLISKQANKAKPAPRTQRTINRMPAKAPPGDEEGFDYNEEERYDCKGGELFANQRRFPGHLFWDFQINILGEKDDTPVHFCDKCGLPIKIYGRMIPCKHVFCYDCAILHEKKGDKMCPGCSDPVQRIEQCTRGSLFMCSIVQGCKRTYLSQRDLQAHINHRHMRAGKPVTRASLENVHPPIAPPPTEIPERFIMPPDKHHMSHIPPKQHIMMPPPPLQHVPHEHYNQPHEDIRAPPAELSMAPPPPRSVSQETFRISTRKHSNLITVPIQDDSNSGAREPPPPAPAPAHHHPEYQGQPVVSHPHHIMPPQQHYAPPPPPPPPISHPMPHPPQAAGTPHLVYSQAPPPPMTSAPPPITPPPGHIIAQMPPYMNHPPPGPPPPQHGGPPVTAPPPHHYNPNSLPQFTEDQGTLSPPFTQPGGMSPGIWPAPRGPPPPPRLQGPPSQTPLPGPHHPDQTRYRPYYQ
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
1Acetylation-------MDHTDNEL
-------CCCCCCCC		8.43-
4Phosphorylation----MDHTDNELQGT
----CCCCCCCCCCC		35.9328387310
11PhosphorylationTDNELQGTNSSGSLG
CCCCCCCCCCCCCCC		20.9728387310
16PhosphorylationQGTNSSGSLGGLDVR
CCCCCCCCCCCCCHH		26.2829507054
29MethylationVRRRIPIKLISKQAN
HHHCCCHHHHHHHHC		34.12-
29AcetylationVRRRIPIKLISKQAN
HHHCCCHHHHHHHHC		34.1223954790
29AcetylationVRRRIPIKLISKQAN
HHHCCCHHHHHHHHC		34.12-
29UbiquitinationVRRRIPIKLISKQAN
HHHCCCHHHHHHHHC		34.12-
33UbiquitinationIPIKLISKQANKAKP
CCHHHHHHHHCCCCC		46.57-
44PhosphorylationKAKPAPRTQRTINRM
CCCCCCCCHHHHHCC		22.73-
65PhosphorylationGDEEGFDYNEEERYD
CCCCCCCCCHHHCCC		23.3927642862
73UbiquitinationNEEERYDCKGGELFA
CHHHCCCCCCCCEEE		3.06-
74UbiquitinationEEERYDCKGGELFAN
HHHCCCCCCCCEEEC		68.03-
119PhosphorylationCGLPIKIYGRMIPCK
CCCEEEEECEECCCC		8.15-
143AcetylationLHEKKGDKMCPGCSD
HCCCCCCCCCCCCCC		51.5826051181
144SulfoxidationHEKKGDKMCPGCSDP
CCCCCCCCCCCCCCH		3.8721406390
175PhosphorylationIVQGCKRTYLSQRDL
HHHHCCHHCCCHHHH		17.8228102081
176PhosphorylationVQGCKRTYLSQRDLQ
HHHCCHHCCCHHHHH		14.3728102081
178PhosphorylationGCKRTYLSQRDLQAH
HCCHHCCCHHHHHHH		16.8628102081
192MethylationHINHRHMRAGKPVTR
HHHHHHHHCCCCCCH		33.78-
198PhosphorylationMRAGKPVTRASLENV
HHCCCCCCHHHHHCC		29.1029978859
201PhosphorylationGKPVTRASLENVHPP
CCCCCHHHHHCCCCC		32.6930266825
219MethylationPPTEIPERFIMPPDK
CCCCCCCCCCCCCCC		22.49-
276O-linked_GlycosylationMAPPPPRSVSQETFR
CCCCCCCCCCCCEEE		31.7130059200
276PhosphorylationMAPPPPRSVSQETFR
CCCCCCCCCCCCEEE		31.7129449344
278O-linked_GlycosylationPPPPRSVSQETFRIS
CCCCCCCCCCEEEEE		24.4430059200
278PhosphorylationPPPPRSVSQETFRIS
CCCCCCCCCCEEEEE		24.4425159151
281PhosphorylationPRSVSQETFRISTRK
CCCCCCCEEEEECCC		15.5826434776
283MethylationSVSQETFRISTRKHS
CCCCCEEEEECCCCC		29.39-
285PhosphorylationSQETFRISTRKHSNL
CCCEEEEECCCCCCC		20.2226434776
286PhosphorylationQETFRISTRKHSNLI
CCEEEEECCCCCCCE		41.1727080861
290PhosphorylationRISTRKHSNLITVPI
EEECCCCCCCEEEEC		36.0423401153
294PhosphorylationRKHSNLITVPIQDDS
CCCCCCEEEECCCCC		24.3230266825
301PhosphorylationTVPIQDDSNSGAREP
EEECCCCCCCCCCCC		40.9825850435
303PhosphorylationPIQDDSNSGAREPPP
ECCCCCCCCCCCCCC		37.4725850435
458MethylationPGIWPAPRGPPPPPR
CCCCCCCCCCCCCCC		72.81-
465MethylationRGPPPPPRLQGPPSQ
CCCCCCCCCCCCCCC		45.47-
471PhosphorylationPRLQGPPSQTPLPGP
CCCCCCCCCCCCCCC		50.2328555341
473PhosphorylationLQGPPSQTPLPGPHH
CCCCCCCCCCCCCCC		31.0028555341
485MethylationPHHPDQTRYRPYYQ-
CCCCCCCCCCCCCC-		21.60-
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

Oops, there are no upstream regulatory protein records of HAKAI_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HAKAI_HUMAN !!
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 HAKAI_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAKAI_MOUSECbll1physical
22252131
CADH1_HUMANCDH1physical
22252131
DOK1_HUMANDOK1physical
22252131
SRC8_HUMANCTTNphysical
22252131
VIR_HUMANKIAA1429physical
26344197
FL2D_HUMANWTAPphysical
26344197
CADH1_HUMANCDH1physical
28069439
SRC_HUMANSRCphysical
28069439
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 HAKAI_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND MASSSPECTROMETRY.

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