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Protein

Protein Hook homolog 3

Gene

HOOK3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity3 Publications

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • microtubule binding Source: UniProtKB

GO - Biological processi

  • cytoplasmic microtubule organization Source: UniProtKB
  • early endosome to late endosome transport Source: UniProtKB
  • endosome organization Source: UniProtKB
  • endosome to lysosome transport Source: UniProtKB
  • Golgi localization Source: UniProtKB
  • interkinetic nuclear migration Source: BHF-UCL
  • lysosome organization Source: UniProtKB
  • microtubule anchoring at centrosome Source: BHF-UCL
  • negative regulation of neurogenesis Source: BHF-UCL
  • neuronal stem cell maintenance Source: Ensembl
  • protein localization to centrosome Source: BHF-UCL
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Hook homolog 3
Short name:
h-hook3
Short name:
hHK3
Gene namesi
Name:HOOK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:23576. HOOK3.

Subcellular locationi

  • Cytoplasmcytoskeleton 1 Publication
  • Golgi apparatus 1 Publication

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

GO - Cellular componenti

  • centriolar satellite Source: Ensembl
  • centrosome Source: BHF-UCL
  • cis-Golgi network Source: UniProtKB
  • cytoplasm Source: HPA
  • FHF complex Source: UniProtKB
  • Golgi apparatus Source: HPA
  • microtubule Source: UniProtKB-KW
  • microtubule organizing center Source: HPA
  • pericentriolar material Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134961305.

Polymorphism and mutation databases

BioMutaiHOOK3.
DMDMi41688581.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 718718Protein Hook homolog 3PRO_0000219197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei238 – 2381Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ86VS8.
PaxDbiQ86VS8.
PRIDEiQ86VS8.

PTM databases

PhosphoSiteiQ86VS8.

Expressioni

Gene expression databases

BgeeiQ86VS8.
CleanExiHS_HOOK3.
ExpressionAtlasiQ86VS8. baseline and differential.
GenevisibleiQ86VS8. HS.

Organism-specific databases

HPAiHPA024756.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MSR1P217574EBI-1777078,EBI-1776976

Protein-protein interaction databases

BioGridi124068. 16 interactions.
IntActiQ86VS8. 2 interactions.
STRINGi9606.ENSP00000305699.

Structurei

3D structure databases

ProteinModelPortaliQ86VS8.
SMRiQ86VS8. Positions 12-166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 164164Sufficient for interaction with microtubulesAdd
BLAST
Regioni553 – 718166Required for association with GolgiAdd
BLAST
Regioni556 – 718163Required for interaction with MSR1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili167 – 433267Sequence AnalysisAdd
BLAST
Coiled coili462 – 667206Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the hook family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG130433.
GeneTreeiENSGT00690000101702.
HOGENOMiHOG000294112.
HOVERGENiHBG051920.
InParanoidiQ86VS8.
KOiK16536.
OMAiDARMSEL.
OrthoDBiEOG7ZD1V5.
PhylomeDBiQ86VS8.
TreeFamiTF320231.

Family and domain databases

InterProiIPR008636. Hook-related_fam.
[Graphical view]
PANTHERiPTHR18947. PTHR18947. 1 hit.
PfamiPF05622. HOOK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q86VS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSVESLERA ELCESLLTWI QTFNVDAPCQ TVEDLTNGVV MAQVLQKIDP
60 70 80 90 100
AYFDENWLNR IKTEVGDNWR LKISNLKKIL KGILDYNHEI LGQQINDFTL
110 120 130 140 150
PDVNLIGEHS DAAELGRMLQ LILGCAVNCE QKQEYIQAIM MMEESVQHVV
160 170 180 190 200
MTAIQELMSK ESPVSAGNDA YVDLDRQLKK TTEELNEALS AKEEIAQRCH
210 220 230 240 250
ELDMQVAALQ EEKSSLLAEN QVLMERLNQS DSIEDPNSPA GRRHLQLQTQ
260 270 280 290 300
LEQLQEETFR LEAAKDDYRI RCEELEKEIS ELRQQNDELT TLADEAQSLK
310 320 330 340 350
DEIDVLRHSS DKVSKLEGQV ESYKKKLEDL GDLRRQVKLL EEKNTMYMQN
360 370 380 390 400
TVSLEEELRK ANAARSQLET YKRQVVELQN RLSEESKKAD KLDFEYKRLK
410 420 430 440 450
EKVDSLQKEK DRLRTERDSL KETIEELRCV QAQEGQLTTQ GLMPLGSQES
460 470 480 490 500
SDSLAAEIVT PEIREKLIRL QHENKMLKLN QEGSDNEKIA LLQSLLDDAN
510 520 530 540 550
LRKNELETEN RLVNQRLLEV QSQVEELQKS LQDQGSKAED SVLLKKKLEE
560 570 580 590 600
HLEKLHEANN ELQKKRAIIE DLEPRFNNSS LKIEELQEAL RKKEEEMKQM
610 620 630 640 650
EERYKKYLEK AKSVIRTLDP KQNQGAAPEI QALKNQLQER DRLFHSLEKE
660 670 680 690 700
YEKTKSQREM EEKYIVSAWY NMGMTLHKKA AEDRLASTGS GQSFLARQRQ
710
ATSSRRSYPG HVQPATAR
Length:718
Mass (Da):83,126
Last modified:February 2, 2004 - v2
Checksum:i9528EC9C854D39FA
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti348 – 3481M → V in BAC03473 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211Q → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_035710
Natural varianti670 – 6701Y → S.
Corresponds to variant rs34131505 [ dbSNP | Ensembl ].
VAR_049363

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6139.1.
RefSeqiNP_115786.1. NM_032410.3.
UniGeneiHs.162852.

Genome annotation databases

EnsembliENST00000307602; ENSP00000305699; ENSG00000168172.
GeneIDi84376.
KEGGihsa:84376.
UCSCiuc003xpr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6139.1.
RefSeqiNP_115786.1. NM_032410.3.
UniGeneiHs.162852.

3D structure databases

ProteinModelPortaliQ86VS8.
SMRiQ86VS8. Positions 12-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124068. 16 interactions.
IntActiQ86VS8. 2 interactions.
STRINGi9606.ENSP00000305699.

PTM databases

PhosphoSiteiQ86VS8.

Polymorphism and mutation databases

BioMutaiHOOK3.
DMDMi41688581.

Proteomic databases

MaxQBiQ86VS8.
PaxDbiQ86VS8.
PRIDEiQ86VS8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307602; ENSP00000305699; ENSG00000168172.
GeneIDi84376.
KEGGihsa:84376.
UCSCiuc003xpr.3. human.

Organism-specific databases

CTDi84376.
GeneCardsiGC08P042769.
HGNCiHGNC:23576. HOOK3.
HPAiHPA024756.
MIMi607825. gene.
neXtProtiNX_Q86VS8.
PharmGKBiPA134961305.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG130433.
GeneTreeiENSGT00690000101702.
HOGENOMiHOG000294112.
HOVERGENiHBG051920.
InParanoidiQ86VS8.
KOiK16536.
OMAiDARMSEL.
OrthoDBiEOG7ZD1V5.
PhylomeDBiQ86VS8.
TreeFamiTF320231.

Miscellaneous databases

ChiTaRSiHOOK3. human.
GeneWikiiHOOK3.
GenomeRNAii84376.
NextBioi74148.
PROiQ86VS8.
SOURCEiSearch...

Gene expression databases

BgeeiQ86VS8.
CleanExiHS_HOOK3.
ExpressionAtlasiQ86VS8. baseline and differential.
GenevisibleiQ86VS8. HS.

Family and domain databases

InterProiIPR008636. Hook-related_fam.
[Graphical view]
PANTHERiPTHR18947. PTHR18947. 1 hit.
PfamiPF05622. HOOK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-221.

Entry informationi

Entry nameiHOOK3_HUMAN
AccessioniPrimary (citable) accession number: Q86VS8
Secondary accession number(s): D3DSY8, Q8NBH0, Q9BY13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: June 24, 2015
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.