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Q86VS8 (HOOK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein Hook homolog 3

Short name=h-hook3
Short name=hHK3
Gene names
Name:HOOK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length718 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.7

Subunit structure

Interacts with Salmonella typhimurium spiC By similarity. Self-associates. Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FAM160A2, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3. May interact directly with AKTIP/FTS, HOOK1 and HOOK2. Associates with several subunits of the homotypic vesicular sorting complex (the HOPS complex) including VPS16 and VPS41; these interactions may be indirect. Interacts with MSR1, and this association is stimulated by ligand binding to MSR1. Interacts with microtubules. Ref.1 Ref.6 Ref.7

Subcellular location

Cytoplasmcytoskeleton. Golgi apparatus. Note: Enriched at the cis-face of the Golgi complex By similarity. Localizes to microtubule asters in prophase By similarity. Ref.1

Sequence similarities

Belongs to the hook family.

Sequence caution

The sequence AAH48304.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Cytoskeleton
Golgi apparatus
Microtubule
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi localization

Inferred from mutant phenotype Ref.1. Source: UniProtKB

cytoplasmic microtubule organization

Inferred from mutant phenotype Ref.1. Source: UniProtKB

early endosome to late endosome transport

Inferred from mutant phenotype Ref.7. Source: UniProtKB

endosome organization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

endosome to lysosome transport

Inferred from mutant phenotype Ref.7. Source: UniProtKB

interkinetic nuclear migration

Inferred from sequence or structural similarity. Source: BHF-UCL

lysosome organization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

microtubule anchoring at centrosome

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of neurogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

neuronal stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

protein localization to centrosome

Inferred from sequence or structural similarity. Source: BHF-UCL

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentFHF complex

Inferred from direct assay Ref.7. Source: UniProtKB

Golgi apparatus

Inferred from direct assay. Source: HPA

centriolar satellite

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from sequence or structural similarity. Source: BHF-UCL

cis-Golgi network

Inferred from direct assay Ref.1. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule organizing center

Inferred from direct assay. Source: HPA

pericentriolar material

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionidentical protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

microtubule binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MSR1P217574EBI-1777078,EBI-1776976

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 718718Protein Hook homolog 3
PRO_0000219197

Regions

Region1 – 164164Sufficient for interaction with microtubules
Region553 – 718166Required for association with Golgi
Region556 – 718163Required for interaction with MSR1
Coiled coil167 – 433267 Potential
Coiled coil462 – 667206 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11 Ref.12
Modified residue2381Phosphoserine Ref.5 Ref.8 Ref.9

Natural variations

Natural variant2211Q → R in a breast cancer sample; somatic mutation. Ref.13
VAR_035710
Natural variant6701Y → S.
Corresponds to variant rs34131505 [ dbSNP | Ensembl ].
VAR_049363

Experimental info

Sequence conflict3481M → V in BAC03473. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q86VS8 [UniParc].

Last modified February 2, 2004. Version 2.
Checksum: 9528EC9C854D39FA

FASTA71883,126
        10         20         30         40         50         60 
MFSVESLERA ELCESLLTWI QTFNVDAPCQ TVEDLTNGVV MAQVLQKIDP AYFDENWLNR 

        70         80         90        100        110        120 
IKTEVGDNWR LKISNLKKIL KGILDYNHEI LGQQINDFTL PDVNLIGEHS DAAELGRMLQ 

       130        140        150        160        170        180 
LILGCAVNCE QKQEYIQAIM MMEESVQHVV MTAIQELMSK ESPVSAGNDA YVDLDRQLKK 

       190        200        210        220        230        240 
TTEELNEALS AKEEIAQRCH ELDMQVAALQ EEKSSLLAEN QVLMERLNQS DSIEDPNSPA 

       250        260        270        280        290        300 
GRRHLQLQTQ LEQLQEETFR LEAAKDDYRI RCEELEKEIS ELRQQNDELT TLADEAQSLK 

       310        320        330        340        350        360 
DEIDVLRHSS DKVSKLEGQV ESYKKKLEDL GDLRRQVKLL EEKNTMYMQN TVSLEEELRK 

       370        380        390        400        410        420 
ANAARSQLET YKRQVVELQN RLSEESKKAD KLDFEYKRLK EKVDSLQKEK DRLRTERDSL 

       430        440        450        460        470        480 
KETIEELRCV QAQEGQLTTQ GLMPLGSQES SDSLAAEIVT PEIREKLIRL QHENKMLKLN 

       490        500        510        520        530        540 
QEGSDNEKIA LLQSLLDDAN LRKNELETEN RLVNQRLLEV QSQVEELQKS LQDQGSKAED 

       550        560        570        580        590        600 
SVLLKKKLEE HLEKLHEANN ELQKKRAIIE DLEPRFNNSS LKIEELQEAL RKKEEEMKQM 

       610        620        630        640        650        660 
EERYKKYLEK AKSVIRTLDP KQNQGAAPEI QALKNQLQER DRLFHSLEKE YEKTKSQREM 

       670        680        690        700        710 
EEKYIVSAWY NMGMTLHKKA AEDRLASTGS GQSFLARQRQ ATSSRRSYPG HVQPATAR 

« Hide

References

« Hide 'large scale' references
[1]"The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins."
Walenta J.H., Didier A.J., Liu X., Kraemer H.
J. Cell Biol. 152:923-934(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cervix and Duodenum.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-718.
Tissue: Astrocyte.
[5]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"The microtubule-binding protein Hook3 interacts with a cytoplasmic domain of scavenger receptor A."
Sano H., Ishino M., Kraemer H., Shimizu T., Mitsuzawa H., Nishitani C., Kuroki Y.
J. Biol. Chem. 282:7973-7981(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MSR1.
[7]"An FTS/Hook/p107(FHIP) complex interacts with and promotes endosomal clustering by the homotypic vacuolar protein sorting complex."
Xu L., Sowa M.E., Chen J., Li X., Gygi S.P., Harper J.W.
Mol. Biol. Cell 19:5059-5071(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FHF COMPLEX, FUNCTION, SELF-ASSOCIATION, INTERACTION WITH AKTIP; HOOK1; HOOK2; VPS16 AND VPS41.
[8]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-221.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF241830 mRNA. Translation: AAK29204.1.
CH471080 Genomic DNA. Translation: EAW63197.1.
CH471080 Genomic DNA. Translation: EAW63198.1.
BC048304 mRNA. Translation: AAH48304.1. Sequence problems.
BC056146 mRNA. Translation: AAH56146.1.
AK090540 mRNA. Translation: BAC03473.1.
RefSeqNP_115786.1. NM_032410.3.
UniGeneHs.162852.

3D structure databases

ProteinModelPortalQ86VS8.
SMRQ86VS8. Positions 12-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124068. 11 interactions.
IntActQ86VS8. 2 interactions.
STRING9606.ENSP00000305699.

PTM databases

PhosphoSiteQ86VS8.

Polymorphism databases

DMDM41688581.

Proteomic databases

PaxDbQ86VS8.
PRIDEQ86VS8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307602; ENSP00000305699; ENSG00000168172.
GeneID84376.
KEGGhsa:84376.
UCSCuc003xpr.3. human.

Organism-specific databases

CTD84376.
GeneCardsGC08P042769.
HGNCHGNC:23576. HOOK3.
HPAHPA024756.
MIM607825. gene.
neXtProtNX_Q86VS8.
PharmGKBPA134961305.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG130433.
HOGENOMHOG000294112.
HOVERGENHBG051920.
InParanoidQ86VS8.
KOK16536.
OMAELQANIM.
OrthoDBEOG7ZD1V5.
PhylomeDBQ86VS8.
TreeFamTF320231.

Gene expression databases

ArrayExpressQ86VS8.
BgeeQ86VS8.
CleanExHS_HOOK3.
GenevestigatorQ86VS8.

Family and domain databases

InterProIPR008636. Hook-related_fam.
[Graphical view]
PANTHERPTHR18947. PTHR18947. 1 hit.
PfamPF05622. HOOK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHOOK3. human.
GeneWikiHOOK3.
GenomeRNAi84376.
NextBio74148.
PROQ86VS8.
SOURCESearch...

Entry information

Entry nameHOOK3_HUMAN
AccessionPrimary (citable) accession number: Q86VS8
Secondary accession number(s): D3DSY8, Q8NBH0, Q9BY13
Entry history
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: April 16, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM