HOOK1_HUMAN - dbPTM
HOOK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HOOK1_HUMAN
UniProt AC Q9UJC3
Protein Name Protein Hook homolog 1
Gene Name HOOK1
Organism Homo sapiens (Human).
Sequence Length 728
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Localizes to punctate cytoplasmic foci which do not appear to overlap with early or late endosomes, the endoplasmic reticulum, multivesicular bodies (MVBs), lysosomes, or mitochondria (By similarity). Often found
Protein Description Required for spermatid differentiation. Probably involved in the positioning of the microtubules of the manchette and the flagellum in relation to the membrane skeleton (By similarity). 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). [PubMed: 18799622]
Protein Sequence MEETQPPPQPKLPLCDSLMIWLQTFNTASPCQDVKQLTSGVAMAQVLHQIDAAWFNESWLSRIKEDVGDNWRIKASNVKKVLQGIMSYYHEFLGQQISEALIPDLNQITECSDPVELGRLLQLILGCAINCEKKQEHIQNIMTLEESVQHVVMTAIQELMSKEILSSPPNDAVGELEQQLKRALEELQEALAEKEELRQRCEELDMQVTTLQDEKNSLVSENEMMNEKLDQLDGSFDDPNTVVAKKYFHAQLQLEQLQEENFRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEIYRQKLQDLNDLRKQVKTLQETNMMYMHNTVSLEEELKKANAARTQLETYKRQVQDLHVKLSSESKRADTLAFEMKRLEEKHEALLKEKERLIEQRDTLKETNEELRCSQVQQDHLNQTDASATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGSENERIEELQEQLEQKHRKMNELETEQRLSKERIRELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDINQNVQKINELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKERRIEILESECKVAKFRDYEEKLIVSAWYNKSLAFQKLGMESRLVSGGGACSDTGACTPARSFLAQQRHITNTRRNLSVKVPATTSD
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-------MEETQPPP
-------CCCCCCCC		10.6819413330
166PhosphorylationLMSKEILSSPPNDAV
HHHCHHHCCCCCCHH		46.6029496963
167PhosphorylationMSKEILSSPPNDAVG
HHCHHHCCCCCCHHH		40.7118669648
194UbiquitinationLQEALAEKEELRQRC
HHHHHHHHHHHHHHH		51.3829967540
203UbiquitinationELRQRCEELDMQVTT
HHHHHHHHHHCHHHH		54.41-
203UbiquitinationELRQRCEELDMQVTT
HHHHHHHHHHCHHHH		54.4122817900
204UbiquitinationLRQRCEELDMQVTTL
HHHHHHHHHCHHHHH		2.8722817900
210PhosphorylationELDMQVTTLQDEKNS
HHHCHHHHHHHHHHC		24.4627251275
217PhosphorylationTLQDEKNSLVSENEM
HHHHHHHCCCCHHHH		41.0121815630
220PhosphorylationDEKNSLVSENEMMNE
HHHHCCCCHHHHHHH		39.7430622161
235PhosphorylationKLDQLDGSFDDPNTV
HHHHCCCCCCCCCCH		25.7625159151
241PhosphorylationGSFDDPNTVVAKKYF
CCCCCCCCHHHHHHH		23.0329396449
245UbiquitinationDPNTVVAKKYFHAQL
CCCCHHHHHHHHHHH		36.0722817900
246UbiquitinationPNTVVAKKYFHAQLQ
CCCHHHHHHHHHHHH		43.3322817900
299PhosphorylationLTSLAEETRALKDEI
HHHHHHHHHHHHHHH		16.85-
321PhosphorylationDKANKLESTVEIYRQ
HHHHHHHHHHHHHHH		48.4625690035
322PhosphorylationKANKLESTVEIYRQK
HHHHHHHHHHHHHHH		16.8725690035
337MethylationLQDLNDLRKQVKTLQ
HHHHHHHHHHHHHHH		30.17115479505
375AcetylationRTQLETYKRQVQDLH
HHHHHHHHHHHHHHH		43.727696137
424UbiquitinationIEQRDTLKETNEELR
HHHHHHHHHHCHHHH		65.6632015554
446PhosphorylationHLNQTDASATKSYEN
HHCCCCHHHCHHHHH		39.0028348404
450PhosphorylationTDASATKSYENLAAE
CCHHHCHHHHHHHHH		33.0728857561
451PhosphorylationDASATKSYENLAAEI
CHHHCHHHHHHHHHH		15.4727732954
484PhosphorylationLRLQQEGSENERIEE
HHHHHCCCHHHHHHH		36.1728857561
538PhosphorylationLQEQGSKSEGESSSK
HHHHCCCCCCCCCHH		53.1628985074
542PhosphorylationGSKSEGESSSKLKQK
CCCCCCCCCHHHHHH		51.2530624053
606PhosphorylationMKAMEERYKMYLEKA
HHHHHHHHHHHHHHH		11.9129759185
609PhosphorylationMEERYKMYLEKARNV
HHHHHHHHHHHHHHH		13.9329759185
678UbiquitinationNKSLAFQKLGMESRL
CCCHHHHHCCCCCEE		40.3232015554
687PhosphorylationGMESRLVSGGGACSD
CCCCEECCCCCCCCC		35.9927251275
693PhosphorylationVSGGGACSDTGACTP
CCCCCCCCCCCCCCC		37.3629396449
695PhosphorylationGGGACSDTGACTPAR
CCCCCCCCCCCCCHH		15.4729396449
699PhosphorylationCSDTGACTPARSFLA
CCCCCCCCCHHHHHH		21.3216964243
703PhosphorylationGACTPARSFLAQQRH
CCCCCHHHHHHHHHH		27.0728857561
719PhosphorylationTNTRRNLSVKVPATT
CCCCCCEEEECCCCC		24.3622617229
719O-linked_GlycosylationTNTRRNLSVKVPATT
CCCCCCEEEECCCCC		24.3630379171
725PhosphorylationLSVKVPATTSD----
EEEECCCCCCC----		22.2928450419
725O-linked_GlycosylationLSVKVPATTSD----
EEEECCCCCCC----		22.2930379171
726PhosphorylationSVKVPATTSD-----
EEECCCCCCC-----		32.7624719451
726O-linked_GlycosylationSVKVPATTSD-----
EEECCCCCCC-----		32.7630379171
727PhosphorylationVKVPATTSD------
EECCCCCCC------		36.6528450419
727O-linked_GlycosylationVKVPATTSD------
EECCCCCCC------		36.6530379171
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 HOOK1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HOOK1_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 HOOK1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN250_HUMANZNF250physical
16189514
AKTIP_HUMANAKTIPphysical
18799622
HOOK2_HUMANHOOK2physical
18799622
HOOK3_HUMANHOOK3physical
18799622
HOOK1_HUMANHOOK1physical
18799622
VPS16_HUMANVPS16physical
18799622
VPS18_HUMANVPS18physical
18799622
VPS39_HUMANVPS39physical
18799622
VPS41_HUMANVPS41physical
18799622
HOOK1_HUMANHOOK1physical
25416956
AKTIP_HUMANAKTIPphysical
25416956
SYCE1_HUMANSYCE1physical
25416956
ZN785_HUMANZNF785physical
25416956
TRIPB_HUMANTRIP11physical
27173435
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 HOOK1_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-235, AND MASS SPECTROMETRY.
Phosphorylation
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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-235, AND MASS SPECTROMETRY.
"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-235, AND MASSSPECTROMETRY.
"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-235 AND THR-699, ANDMASS SPECTROMETRY.

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