HOOK3_HUMAN - dbPTM
HOOK3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HOOK3_HUMAN
UniProt AC Q86VS8
Protein Name Protein Hook homolog 3
Gene Name HOOK3
Organism Homo sapiens (Human).
Sequence Length 718
Subcellular Localization Cytoplasm, cytoskeleton . Golgi apparatus . Enriched at the cis-face of the Golgi complex. Localizes to microtubule asters in prophase (PubMed:11238449). Localizes to the manchette in elongating spermatids (By similarity).
Protein Description Probably serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking (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). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex. Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). [PubMed: 25035494]
Protein Sequence MFSVESLERAELCESLLTWIQTFNVDAPCQTVEDLTNGVVMAQVLQKIDPAYFDENWLNRIKTEVGDNWRLKISNLKKILKGILDYNHEILGQQINDFTLPDVNLIGEHSDAAELGRMLQLILGCAVNCEQKQEYIQAIMMMEESVQHVVMTAIQELMSKESPVSAGNDAYVDLDRQLKKTTEELNEALSAKEEIAQRCHELDMQVAALQEEKSSLLAENQVLMERLNQSDSIEDPNSPAGRRHLQLQTQLEQLQEETFRLEAAKDDYRIRCEELEKEISELRQQNDELTTLADEAQSLKDEIDVLRHSSDKVSKLEGQVESYKKKLEDLGDLRRQVKLLEEKNTMYMQNTVSLEEELRKANAARSQLETYKRQVVELQNRLSEESKKADKLDFEYKRLKEKVDSLQKEKDRLRTERDSLKETIEELRCVQAQEGQLTTQGLMPLGSQESSDSLAAEIVTPEIREKLIRLQHENKMLKLNQEGSDNEKIALLQSLLDDANLRKNELETENRLVNQRLLEVQSQVEELQKSLQDQGSKAEDSVLLKKKLEEHLEKLHEANNELQKKRAIIEDLEPRFNNSSLKIEELQEALRKKEEEMKQMEERYKKYLEKAKSVIRTLDPKQNQGAAPEIQALKNQLQERDRLFHSLEKEYEKTKSQREMEEKYIVSAWYNMGMTLHKKAAEDRLASTGSGQSFLARQRQATSSRRSYPGHVQPATAR
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-------MFSVESLE
-------CCCHHHHH		5.2222223895
3Phosphorylation-----MFSVESLERA
-----CCCHHHHHHH		24.5529523821
6Phosphorylation--MFSVESLERAELC
--CCCHHHHHHHHHH		33.1229523821
74PhosphorylationDNWRLKISNLKKILK
CCCEEEHHHHHHHHH		34.2323403867
162PhosphorylationQELMSKESPVSAGND
HHHHCCCCCCCCCCC		34.0520068231
165PhosphorylationMSKESPVSAGNDAYV
HCCCCCCCCCCCHHH		33.5720068231
171PhosphorylationVSAGNDAYVDLDRQL
CCCCCCHHHCHHHHH		9.4328796482
180UbiquitinationDLDRQLKKTTEELNE
CHHHHHHHHHHHHHH		70.0824816145
181PhosphorylationLDRQLKKTTEELNEA
HHHHHHHHHHHHHHH		37.5426503514
224SulfoxidationLAENQVLMERLNQSD
HHHHHHHHHHHCCCC		2.7121406390
230PhosphorylationLMERLNQSDSIEDPN
HHHHHCCCCCCCCCC		32.0530266825
232PhosphorylationERLNQSDSIEDPNSP
HHHCCCCCCCCCCCH		32.8830266825
238PhosphorylationDSIEDPNSPAGRRHL
CCCCCCCCHHHHHHH		22.8630266825
280PhosphorylationEELEKEISELRQQND
HHHHHHHHHHHHHHH		31.5024719451
315MalonylationHSSDKVSKLEGQVES
HCHHHHHHHHHHHHH		54.2532601280
322PhosphorylationKLEGQVESYKKKLED
HHHHHHHHHHHHHHH		43.3120068231
323PhosphorylationLEGQVESYKKKLEDL
HHHHHHHHHHHHHHH		17.2020068231
324AcetylationEGQVESYKKKLEDLG
HHHHHHHHHHHHHHH		53.3525953088
3242-HydroxyisobutyrylationEGQVESYKKKLEDLG
HHHHHHHHHHHHHHH		53.35-
326MalonylationQVESYKKKLEDLGDL
HHHHHHHHHHHHHHH		53.6232601280
345PhosphorylationKLLEEKNTMYMQNTV
HHHHHHCCHHHHCCC		22.2822210691
347PhosphorylationLEEKNTMYMQNTVSL
HHHHCCHHHHCCCCH		8.1022210691
351PhosphorylationNTMYMQNTVSLEEEL
CCHHHHCCCCHHHHH		8.4522210691
353PhosphorylationMYMQNTVSLEEELRK
HHHHCCCCHHHHHHH		28.2022210691
366PhosphorylationRKANAARSQLETYKR
HHHHHHHHHHHHHHH		34.1021712546
371PhosphorylationARSQLETYKRQVVEL
HHHHHHHHHHHHHHH		8.5221712546
372AcetylationRSQLETYKRQVVELQ
HHHHHHHHHHHHHHH		43.7225953088
3972-HydroxyisobutyrylationDKLDFEYKRLKEKVD
HHCHHHHHHHHHHHH		44.02-
400UbiquitinationDFEYKRLKEKVDSLQ
HHHHHHHHHHHHHHH		60.5724816145
405PhosphorylationRLKEKVDSLQKEKDR
HHHHHHHHHHHHHHH		35.3723186163
421UbiquitinationRTERDSLKETIEELR
HHHHHHHHHHHHHHH		57.6824816145
447PhosphorylationQGLMPLGSQESSDSL
CCCCCCCCCCCCCCH		38.1628348404
450PhosphorylationMPLGSQESSDSLAAE
CCCCCCCCCCCHHHH		31.6328348404
451PhosphorylationPLGSQESSDSLAAEI
CCCCCCCCCCHHHHH		30.3928348404
453PhosphorylationGSQESSDSLAAEIVT
CCCCCCCCHHHHHCC		23.1228348404
460PhosphorylationSLAAEIVTPEIREKL
CHHHHHCCHHHHHHH		22.3624719451
488UbiquitinationQEGSDNEKIALLQSL
CCCCHHHHHHHHHHH		39.2629967540
494PhosphorylationEKIALLQSLLDDANL
HHHHHHHHHHHHHCC		30.7620068231
5452-HydroxyisobutyrylationAEDSVLLKKKLEEHL
HHHHHHHHHHHHHHH		43.64-
546AcetylationEDSVLLKKKLEEHLE
HHHHHHHHHHHHHHH		63.6611790847
547AcetylationDSVLLKKKLEEHLEK
HHHHHHHHHHHHHHH		60.5911790857
554AcetylationKLEEHLEKLHEANNE
HHHHHHHHHHHHCHH		62.6011790867
564AcetylationEANNELQKKRAIIED
HHCHHHHHHHHHHHC		57.7719666985
591MethylationEELQEALRKKEEEMK
HHHHHHHHHHHHHHH		55.86115479519
598UbiquitinationRKKEEEMKQMEERYK
HHHHHHHHHHHHHHH		50.1824816145
604PhosphorylationMKQMEERYKKYLEKA
HHHHHHHHHHHHHHH		18.3423403867
607PhosphorylationMEERYKKYLEKAKSV
HHHHHHHHHHHHHHH		18.88-
634UbiquitinationAPEIQALKNQLQERD
HHHHHHHHHHHHHHH		45.7429967540
646PhosphorylationERDRLFHSLEKEYEK
HHHHHHHHHHHHHHH		30.7823403867
649UbiquitinationRLFHSLEKEYEKTKS
HHHHHHHHHHHHHHH		71.5329967540
651PhosphorylationFHSLEKEYEKTKSQR
HHHHHHHHHHHHHHH		33.5223403867
654PhosphorylationLEKEYEKTKSQREME
HHHHHHHHHHHHHHH		24.8023403867
656PhosphorylationKEYEKTKSQREMEEK
HHHHHHHHHHHHHHH		39.4426503892
664PhosphorylationQREMEEKYIVSAWYN
HHHHHHHHHHHHHHH		15.1626503892
667PhosphorylationMEEKYIVSAWYNMGM
HHHHHHHHHHHHCCC		11.9726503892
670PhosphorylationKYIVSAWYNMGMTLH
HHHHHHHHHCCCCHH		8.5926503892
684MethylationHKKAAEDRLASTGSG
HHHHHHHHHHHCCCC		24.53115479513
687PhosphorylationAAEDRLASTGSGQSF
HHHHHHHHCCCCHHH		37.5829978859
688PhosphorylationAEDRLASTGSGQSFL
HHHHHHHCCCCHHHH		29.7430108239
690PhosphorylationDRLASTGSGQSFLAR
HHHHHCCCCHHHHHH		33.4728450419
693PhosphorylationASTGSGQSFLARQRQ
HHCCCCHHHHHHHHH		26.2528450419
702PhosphorylationLARQRQATSSRRSYP
HHHHHHHCCCCCCCC		20.9227282143
703PhosphorylationARQRQATSSRRSYPG
HHHHHHCCCCCCCCC		25.5127282143
707PhosphorylationQATSSRRSYPGHVQP
HHCCCCCCCCCCCCC		34.2730266825
708PhosphorylationATSSRRSYPGHVQPA
HCCCCCCCCCCCCCC		16.0630266825
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 HOOK3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HOOK3_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 HOOK3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKTIP_HUMANAKTIPphysical
18799622
HOOK2_HUMANHOOK2physical
18799622
HOOK1_HUMANHOOK1physical
18799622
HOOK3_HUMANHOOK3physical
18799622
F16A2_HUMANFAM160A2physical
18799622
VPS16_HUMANVPS16physical
18799622
VPS41_HUMANVPS41physical
18799622
SCFD1_HUMANSCFD1physical
22939629
MRE11_HUMANMRE11Aphysical
26344197
F16A2_HUMANFAM160A2physical
28514442
HOOK1_HUMANHOOK1physical
28514442
F16A1_HUMANFAM160A1physical
28514442
MTMR4_HUMANMTMR4physical
28514442
KLH20_HUMANKLHL20physical
28514442
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 HOOK3_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-238, 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-238, 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 TYR-708, AND MASSSPECTROMETRY.

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