HOOK3_HUMAN
ID HOOK3_HUMAN Reviewed; 718 AA.
AC Q86VS8; D3DSY8; Q8NBH0; Q9BY13;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein Hook homolog 3;
DE Short=h-hook3;
DE Short=hHK3;
GN Name=HOOK3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MICROTUBULES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11238449; DOI=10.1083/jcb.152.5.923;
RA Walenta J.H., Didier A.J., Liu X., Kraemer H.;
RT "The Golgi-associated hook3 protein is a member of a novel family of
RT microtubule-binding proteins.";
RL J. Cell Biol. 152:923-934(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Duodenum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-718.
RC TISSUE=Astrocyte;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP FUNCTION, AND INTERACTION WITH MSR1.
RX PubMed=17237231; DOI=10.1074/jbc.m611537200;
RA Sano H., Ishino M., Kraemer H., Shimizu T., Mitsuzawa H., Nishitani C.,
RA Kuroki Y.;
RT "The microtubule-binding protein Hook3 interacts with a cytoplasmic domain
RT of scavenger receptor A.";
RL J. Biol. Chem. 282:7973-7981(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FHF COMPLEX,
RP FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH AKTIP; HOOK1; HOOK2; VPS16
RP AND VPS41.
RX PubMed=18799622; DOI=10.1091/mbc.e08-05-0473;
RA Xu L., Sowa M.E., Chen J., Li X., Gygi S.P., Harper J.W.;
RT "An FTS/Hook/p107(FHIP) complex interacts with and promotes endosomal
RT clustering by the homotypic vacuolar protein sorting complex.";
RL Mol. Biol. Cell 19:5059-5071(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-6; SER-238; SER-693
RP AND SER-707, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP FUNCTION, AND INTERACTION WITH DYNEIN INTERMEDIATE CHAIN AND DCTN1.
RX PubMed=25035494; DOI=10.1126/science.1254198;
RA McKenney R.J., Huynh W., Tanenbaum M.E., Bhabha G., Vale R.D.;
RT "Activation of cytoplasmic dynein motility by dynactin-cargo adapter
RT complexes.";
RL Science 345:337-341(2014).
RN [16]
RP FUNCTION, AND INTERACTION WITH HOOK1.
RX PubMed=32073997; DOI=10.1091/mbc.e19-11-0658;
RA Mattera R., Williamson C.D., Ren X., Bonifacino J.S.;
RT "The FTS-Hook-FHIP (FHF) complex interacts with AP-4 to mediate perinuclear
RT distribution of AP-4 and its cargo ATG9A.";
RL Mol. Biol. Cell 31:963-979(2020).
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-221.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Probably serves as a target for the spiC protein from
CC Salmonella typhimurium, which inactivates it, leading to a strong
CC alteration in cellular trafficking (By similarity). Component of the
CC FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to
CC promote vesicle trafficking and/or fusion via the homotypic vesicular
CC protein sorting complex (the HOPS complex). May regulate clearance of
CC endocytosed receptors such as MSR1. Participates in defining the
CC architecture and localization of the Golgi complex. Acts as an adapter
CC protein linking the dynein motor complex to various cargos and converts
CC dynein from a non-processive to a highly processive motor in the
CC presence of dynactin. Facilitates the interaction between dynein and
CC dynactin and activates dynein processivity (the ability to move along a
CC microtubule for a long distance without falling off the track)
CC (PubMed:25035494). FHF complex promotes the distribution of AP-4
CC complex to the perinuclear area of the cell (PubMed:32073997).
CC {ECO:0000250|UniProtKB:Q8BUK6, ECO:0000269|PubMed:11238449,
CC ECO:0000269|PubMed:17237231, ECO:0000269|PubMed:18799622,
CC ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:32073997}.
CC -!- FUNCTION: (Microbial infection) May serve as a target for the spiC
CC protein from Salmonella typhimurium, which inactivates it, leading to a
CC strong alteration in cellular trafficking. {ECO:0000305}.
CC -!- SUBUNIT: Self-associates. Component of the FTS/Hook/FHIP complex (FHF
CC complex), composed of AKTIP/FTS, FHIP1B, and one or more members of the
CC Hook family of proteins HOOK1, HOOK2, and HOOK3. May interact directly
CC with AKTIP/FTS, HOOK1 and HOOK2 (PubMed:32073997). Associates with
CC several subunits of the homotypic vesicular sorting complex (the HOPS
CC complex) including VPS16 and VPS41; these interactions may be indirect
CC (PubMed:18799622). Interacts with MSR1, and this association is
CC stimulated by ligand binding to MSR1 (PubMed:17237231). Interacts with
CC microtubules (PubMed:11238449). Interacts with dynein intermediate
CC chain and dynactin (DCTN1) (PubMed:25035494). Interacts with CCDC181
CC (By similarity). Interacts with LRGUK (By similarity).
CC {ECO:0000250|UniProtKB:Q8BUK6, ECO:0000269|PubMed:11238449,
CC ECO:0000269|PubMed:17237231, ECO:0000269|PubMed:18799622,
CC ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:32073997}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Salmonella typhimurium
CC spiC. {ECO:0000305}.
CC -!- INTERACTION:
CC Q86VS8; O43310-2: CTIF; NbExp=3; IntAct=EBI-1777078, EBI-12180013;
CC Q86VS8; Q9UJC3: HOOK1; NbExp=4; IntAct=EBI-1777078, EBI-746704;
CC Q86VS8; P13646: KRT13; NbExp=3; IntAct=EBI-1777078, EBI-1223876;
CC Q86VS8; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-1777078, EBI-3044087;
CC Q86VS8; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1777078, EBI-16439278;
CC Q86VS8; P21757: MSR1; NbExp=4; IntAct=EBI-1777078, EBI-1776976;
CC Q86VS8; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-1777078, EBI-10171633;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11238449}. Golgi apparatus
CC {ECO:0000269|PubMed:11238449}. Note=Enriched at the cis-face of the
CC Golgi complex. Localizes to microtubule asters in prophase
CC (PubMed:11238449). Localizes to the manchette in elongating spermatids
CC (By similarity). {ECO:0000250|UniProtKB:Q8BUK6,
CC ECO:0000269|PubMed:11238449}.
CC -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48304.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF241830; AAK29204.1; -; mRNA.
DR EMBL; CH471080; EAW63197.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63198.1; -; Genomic_DNA.
DR EMBL; BC048304; AAH48304.1; ALT_SEQ; mRNA.
DR EMBL; BC056146; AAH56146.1; -; mRNA.
DR EMBL; AK090540; BAC03473.1; -; mRNA.
DR CCDS; CCDS6139.1; -.
DR RefSeq; NP_115786.1; NM_032410.3.
DR PDB; 5J8E; X-ray; 1.70 A; A/B=1-160.
DR PDB; 6B9H; X-ray; 1.50 A; A=1-160.
DR PDBsum; 5J8E; -.
DR PDBsum; 6B9H; -.
DR AlphaFoldDB; Q86VS8; -.
DR SMR; Q86VS8; -.
DR BioGRID; 124068; 201.
DR CORUM; Q86VS8; -.
DR IntAct; Q86VS8; 33.
DR STRING; 9606.ENSP00000305699; -.
DR GlyGen; Q86VS8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86VS8; -.
DR MetOSite; Q86VS8; -.
DR PhosphoSitePlus; Q86VS8; -.
DR BioMuta; HOOK3; -.
DR DMDM; 41688581; -.
DR EPD; Q86VS8; -.
DR jPOST; Q86VS8; -.
DR MassIVE; Q86VS8; -.
DR MaxQB; Q86VS8; -.
DR PaxDb; Q86VS8; -.
DR PeptideAtlas; Q86VS8; -.
DR PRIDE; Q86VS8; -.
DR ProteomicsDB; 70068; -.
DR Antibodypedia; 11516; 110 antibodies from 27 providers.
DR DNASU; 84376; -.
DR Ensembl; ENST00000307602.9; ENSP00000305699.3; ENSG00000168172.9.
DR GeneID; 84376; -.
DR KEGG; hsa:84376; -.
DR MANE-Select; ENST00000307602.9; ENSP00000305699.3; NM_032410.4; NP_115786.1.
DR UCSC; uc003xpr.4; human.
DR CTD; 84376; -.
DR DisGeNET; 84376; -.
DR GeneCards; HOOK3; -.
DR HGNC; HGNC:23576; HOOK3.
DR HPA; ENSG00000168172; Low tissue specificity.
DR MIM; 607825; gene.
DR neXtProt; NX_Q86VS8; -.
DR OpenTargets; ENSG00000168172; -.
DR PharmGKB; PA134961305; -.
DR VEuPathDB; HostDB:ENSG00000168172; -.
DR eggNOG; ENOG502QQM8; Eukaryota.
DR GeneTree; ENSGT00940000158075; -.
DR HOGENOM; CLU_011214_1_0_1; -.
DR InParanoid; Q86VS8; -.
DR OMA; LEFNNHA; -.
DR OrthoDB; 398210at2759; -.
DR PhylomeDB; Q86VS8; -.
DR TreeFam; TF320231; -.
DR PathwayCommons; Q86VS8; -.
DR SignaLink; Q86VS8; -.
DR SIGNOR; Q86VS8; -.
DR BioGRID-ORCS; 84376; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; HOOK3; human.
DR GeneWiki; HOOK3; -.
DR GenomeRNAi; 84376; -.
DR Pharos; Q86VS8; Tbio.
DR PRO; PR:Q86VS8; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q86VS8; protein.
DR Bgee; ENSG00000168172; Expressed in calcaneal tendon and 190 other tissues.
DR ExpressionAtlas; Q86VS8; baseline and differential.
DR Genevisible; Q86VS8; HS.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; ISS:BHF-UCL.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0070695; C:FHF complex; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000242; C:pericentriolar material; ISS:BHF-UCL.
DR GO; GO:0034452; F:dynactin binding; IDA:UniProtKB.
DR GO; GO:0045505; F:dynein intermediate chain binding; IDA:UniProtKB.
DR GO; GO:0045503; F:dynein light chain binding; IPI:UniProtKB.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
DR GO; GO:0051645; P:Golgi localization; IMP:UniProtKB.
DR GO; GO:0022027; P:interkinetic nuclear migration; ISS:BHF-UCL.
DR GO; GO:0007040; P:lysosome organization; IMP:UniProtKB.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; ISS:BHF-UCL.
DR GO; GO:0050768; P:negative regulation of neurogenesis; ISS:BHF-UCL.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0071539; P:protein localization to centrosome; ISS:BHF-UCL.
DR GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR008636; Hook_C.
DR InterPro; IPR043936; HOOK_N.
DR Pfam; PF05622; HOOK; 1.
DR Pfam; PF19047; HOOK_N; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Microtubule; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..718
FT /note="Protein Hook homolog 3"
FT /id="PRO_0000219197"
FT DOMAIN 10..126
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..164
FT /note="Sufficient for interaction with microtubules"
FT REGION 553..718
FT /note="Required for association with Golgi"
FT REGION 556..718
FT /note="Required for interaction with MSR1"
FT /evidence="ECO:0000269|PubMed:17237231"
FT REGION 682..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..433
FT /evidence="ECO:0000255"
FT COILED 462..667
FT /evidence="ECO:0000255"
FT COMPBIAS 686..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 221
FT /note="Q -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035710"
FT VARIANT 670
FT /note="Y -> S (in dbSNP:rs34131505)"
FT /id="VAR_049363"
FT CONFLICT 348
FT /note="M -> V (in Ref. 4; BAC03473)"
FT /evidence="ECO:0000305"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:6B9H"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:6B9H"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6B9H"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:6B9H"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6B9H"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:6B9H"
FT HELIX 69..89
FT /evidence="ECO:0007829|PDB:6B9H"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:6B9H"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:6B9H"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:6B9H"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:6B9H"
SQ SEQUENCE 718 AA; 83126 MW; 9528EC9C854D39FA CRC64;
MFSVESLERA ELCESLLTWI QTFNVDAPCQ TVEDLTNGVV MAQVLQKIDP AYFDENWLNR
IKTEVGDNWR LKISNLKKIL KGILDYNHEI LGQQINDFTL PDVNLIGEHS DAAELGRMLQ
LILGCAVNCE QKQEYIQAIM MMEESVQHVV MTAIQELMSK ESPVSAGNDA YVDLDRQLKK
TTEELNEALS AKEEIAQRCH ELDMQVAALQ EEKSSLLAEN QVLMERLNQS DSIEDPNSPA
GRRHLQLQTQ LEQLQEETFR LEAAKDDYRI RCEELEKEIS ELRQQNDELT TLADEAQSLK
DEIDVLRHSS DKVSKLEGQV ESYKKKLEDL GDLRRQVKLL EEKNTMYMQN TVSLEEELRK
ANAARSQLET YKRQVVELQN RLSEESKKAD KLDFEYKRLK EKVDSLQKEK DRLRTERDSL
KETIEELRCV QAQEGQLTTQ GLMPLGSQES SDSLAAEIVT PEIREKLIRL QHENKMLKLN
QEGSDNEKIA LLQSLLDDAN LRKNELETEN RLVNQRLLEV QSQVEELQKS LQDQGSKAED
SVLLKKKLEE HLEKLHEANN ELQKKRAIIE DLEPRFNNSS LKIEELQEAL RKKEEEMKQM
EERYKKYLEK AKSVIRTLDP KQNQGAAPEI QALKNQLQER DRLFHSLEKE YEKTKSQREM
EEKYIVSAWY NMGMTLHKKA AEDRLASTGS GQSFLARQRQ ATSSRRSYPG HVQPATAR
