HOOK2_HUMAN - dbPTM
HOOK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HOOK2_HUMAN
UniProt AC Q96ED9
Protein Name Protein Hook homolog 2
Gene Name HOOK2
Organism Homo sapiens (Human).
Sequence Length 719
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm. Cytoplasm, cytoskeleton . Colocalizes with aggresomes, which are aggregates of misfolded proteins, at the centrosome (PubMed:17540036). Also localizes to punctate cytopla
Protein Description Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Contributes to the establishment and maintenance of centrosome function. May function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones..
Protein Sequence MSVDKAELCGSLLTWLQTFHVPSPCASPQDLSSGLAVAYVLNQIDPSWFNEAWLQGISEDPGPNWKLKVSNLKMVLRSLVEYSQDVLAHPVSEEHLPDVSLIGEFSDPAELGKLLQLVLGCAISCEKKQDHIQRIMTLEESVQHVVMEAIQELMTKDTPDSLSPETYGNFDSQSRRYYFLSEEAEEGDELQQRCLDLERQLMLLSEEKQSLAQENAGLRERMGRPEGEGTPGLTAKKLLLLQSQLEQLQEENFRLESGREDERLRCAELEREVAELQHRNQALTSLAQEAQALKDEMDELRQSSERAGQLEATLTSCRRRLGELRELRRQVRQLEERNAGHAERTRQLEDELRRAGSLRAQLEAQRRQVQELQGQRQEEAMKAEKWLFECRNLEEKYESVTKEKERLLAERDSLREANEELRCAQLQPRGLTQADPSLDPTSTPVDNLAAEILPAELRETLLRLQLENKRLCRQEAADRERQEELQRHLEDANRARHGLETQHRLNQQQLSELRAQVEDLQKALQEQGGKTEDAISILLKRKLEEHLQKLHEADLELQRKREYIEELEPPTDSSTARRIEELQHNLQKKDADLRAMEERYRRYVDKARMVMQTMEPKQRPAAGAPPELHSLRTQLRERDVRIRHLEMDFEKSRSQREQEEKLLISAWYNMGMALQQRAGEERAPAHAQSFLAQQRLATNSRRGPLGRLASLNLRPTDKH
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
158PhosphorylationQELMTKDTPDSLSPE
HHHHCCCCCCCCCHH		30.4720860994
161PhosphorylationMTKDTPDSLSPETYG
HCCCCCCCCCHHHCC		31.7626657352
163PhosphorylationKDTPDSLSPETYGNF
CCCCCCCCHHHCCCC		25.3325159151
166PhosphorylationPDSLSPETYGNFDSQ
CCCCCHHHCCCCCCC		39.8627251275
167PhosphorylationDSLSPETYGNFDSQS
CCCCHHHCCCCCCCC		14.3826471730
172PhosphorylationETYGNFDSQSRRYYF
HHCCCCCCCCCEEEE		26.3927251275
174PhosphorylationYGNFDSQSRRYYFLS
CCCCCCCCCEEEECC		23.7623403867
177PhosphorylationFDSQSRRYYFLSEEA
CCCCCCEEEECCHHH		9.4727642862
178PhosphorylationDSQSRRYYFLSEEAE
CCCCCEEEECCHHHH		9.0227642862
181PhosphorylationSRRYYFLSEEAEEGD
CCEEEECCHHHHCCH		24.4022617229
208UbiquitinationLMLLSEEKQSLAQEN
HHHHHHHHHHHHHHH		40.9329967540
210PhosphorylationLLSEEKQSLAQENAG
HHHHHHHHHHHHHHH		36.4223090842
230PhosphorylationGRPEGEGTPGLTAKK
CCCCCCCCCCHHHHH		15.1925159151
313PhosphorylationRAGQLEATLTSCRRR
HHHHHHHHHHHHHHH		22.6129414761
315PhosphorylationGQLEATLTSCRRRLG
HHHHHHHHHHHHHHH		22.7924719451
316PhosphorylationQLEATLTSCRRRLGE
HHHHHHHHHHHHHHH		14.5617192257
397PhosphorylationCRNLEEKYESVTKEK
HCCHHHHHHHHHHHH		19.4027642862
437PhosphorylationGLTQADPSLDPTSTP
CCCCCCCCCCCCCCC		46.05-
441PhosphorylationADPSLDPTSTPVDNL
CCCCCCCCCCCCHHH		44.9226657352
442PhosphorylationDPSLDPTSTPVDNLA
CCCCCCCCCCCHHHH		35.7830087585
443PhosphorylationPSLDPTSTPVDNLAA
CCCCCCCCCCHHHHH		29.7924719451
571PhosphorylationIEELEPPTDSSTARR
HHHHCCCCCCHHHHH		60.26-
613PhosphorylationKARMVMQTMEPKQRP
HHHHHHHHCCCCCCC		12.8527174698
630PhosphorylationGAPPELHSLRTQLRE
CCCHHHHHHHHHHHH		31.9728555341
665PhosphorylationQEEKLLISAWYNMGM
HHHHHHHHHHHHHHH		16.8427251275
668PhosphorylationKLLISAWYNMGMALQ
HHHHHHHHHHHHHHH		8.5927251275
689PhosphorylationRAPAHAQSFLAQQRL
CCHHHHHHHHHHHHH		24.0228857561
710PhosphorylationGPLGRLASLNLRPTD
CHHHHHHHCCCCCCC		23.5323401153
716PhosphorylationASLNLRPTDKH----
HHCCCCCCCCC----		51.7727251275
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 HOOK2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HOOK2_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 HOOK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCM10_HUMANMCM10physical
16189514
ZN250_HUMANZNF250physical
16189514
CCD33_HUMANCCDC33physical
16189514
AKTIP_HUMANAKTIPphysical
16189514
AKTIP_HUMANAKTIPphysical
18799622
HOOK1_HUMANHOOK1physical
18799622
HOOK2_HUMANHOOK2physical
18799622
HOOK3_HUMANHOOK3physical
18799622
VPS16_HUMANVPS16physical
18799622
VPS41_HUMANVPS41physical
18799622
DS13A_HUMANDUSP13physical
25416956
DS13B_HUMANDUSP13physical
25416956
ZC21C_HUMANZC2HC1Cphysical
25416956
C19L2_HUMANCWF19L2physical
25416956
KANL1_HUMANKANSL1physical
25416956
KLK15_HUMANKLK15physical
21516116
SUV91_HUMANSUV39H1physical
21516116
TPM3_HUMANTPM3physical
21516116
RITA1_HUMANRITA1physical
21516116
ZBT47_HUMANZBTB47physical
21516116
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 HOOK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-163, 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 THR-230 AND SER-316, ANDMASS SPECTROMETRY.

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