ID HOOK1_HUMAN Reviewed; 728 AA. AC Q9UJC3; A8K8E9; A8MU44; B4DX15; O60561; Q5TG44; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 02-FEB-2004, sequence version 2. DT 24-JAN-2024, entry version 179. DE RecName: Full=Protein Hook homolog 1 {ECO:0000305}; DE Short=h-hook1; DE Short=hHK1; GN Name=HOOK1 {ECO:0000312|HGNC:HGNC:19884}; 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] (ISOFORM 1). RX PubMed=9927460; DOI=10.1093/genetics/151.2.675; RA Kraemer H., Phistry M.; RT "Genetic analysis of hook, a gene required for endocytic trafficking in RT Drosophila."; RL Genetics 151:675-684(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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 [6] RP INTERACTION WITH MICROTUBULES, AND 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 [7] RP INTERACTION WITH CLN3, AND SUBCELLULAR LOCATION. RX PubMed=15471887; DOI=10.1093/hmg/ddh321; RA Luiro K., Yliannala K., Ahtiainen L., Maunu H., Jaervelae I., Kyttaelae A., RA Jalanko A.; RT "Interconnections of CLN3, Hook1 and Rab proteins link Batten disease to RT defects in the endocytic pathway."; RL Hum. Mol. Genet. 13:3017-3027(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND THR-699, AND RP IDENTIFICATION BY 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FHF COMPLEX, RP SELF-ASSOCIATION, INTERACTION WITH AKTIP; HOOK2; HOOK3; VPS16; VPS18; VPS39 RP AND VPS41, AND MUTAGENESIS OF 661-GLU-GLU-662 AND 669-TRP-TYR-670. 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, 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 [16] RP FUNCTION, INTERACTION WITH AP4M1; AKTIP; FHIP1B; HOOK2 AND HOOK3, SUBUNIT, RP AND MUTAGENESIS OF 661-GLU-GLU-662 AND 669-TRP-TYR-670. 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] LEU-433. 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). RN [18] RP VARIANT SER-689. RX PubMed=26528954; DOI=10.1002/ana.24553; RG International Parkinsonism Genetics Network; RA Olgiati S., Quadri M., Fang M., Rood J.P., Saute J.A., Chien H.F., RA Bouwkamp C.G., Graafland J., Minneboo M., Breedveld G.J., Zhang J., RA Verheijen F.W., Boon A.J., Kievit A.J., Jardim L.B., Mandemakers W., RA Barbosa E.R., Rieder C.R., Leenders K.L., Wang J., Bonifati V.; RT "DNAJC6 mutations associated with early-onset Parkinson's disease."; RL Ann. Neurol. 79:244-256(2016). CC -!- FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex) CC (PubMed:18799622, PubMed:32073997). The FHF complex may function to CC promote vesicle trafficking and/or fusion via the homotypic vesicular CC protein sorting complex (the HOPS complex) (PubMed:18799622). FHF CC complex promotes the distribution of AP-4 complex to the perinuclear CC area of the cell (PubMed:32073997). Required for spermatid CC differentiation. Probably involved in the positioning of the CC microtubules of the manchette and the flagellum in relation to the CC membrane skeleton (By similarity). {ECO:0000250|UniProtKB:Q8BIL5, CC ECO:0000269|PubMed:18799622, ECO:0000269|PubMed:32073997}. CC -!- SUBUNIT: Self-associates (PubMed:18799622, PubMed:32073997). Component CC of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, CC FHIP1B, and one or more members of the Hook family of proteins HOOK1, CC HOOK2, and HOOK3 (PubMed:18799622, PubMed:32073997). Interacts directly CC with AKTIP/FTS, HOOK2 and HOOK3 (PubMed:18799622, PubMed:32073997). CC Associates with several subunits of the homotypic vesicular sorting CC complex (the HOPS complex) including VPS16, VPS18, VPS39 and VPS41; CC these interactions may be indirect (PubMed:18799622). Interacts with CC CCDC181 (By similarity). Interacts (via coiled-coil region) with RIMBP3 CC (via C-terminus) (By similarity). Interacts with LRGUK (via guanylate CC kinase-like domain) (By similarity). Interacts with microtubules CC (PubMed:11238449). May interact with CLN3 (PubMed:15471887). Interacts CC with AP4M1; the interaction is direct, mediates the interaction between CC FTS-Hook-FHIP (FHF) complex and AP-4 and the perinuclear distribution CC of AP-4 (PubMed:32073997). {ECO:0000250|UniProtKB:Q8BIL5, CC ECO:0000269|PubMed:11238449, ECO:0000269|PubMed:15471887, CC ECO:0000269|PubMed:18799622, ECO:0000269|PubMed:32073997}. CC -!- INTERACTION: CC Q9UJC3; Q9H8T0: AKTIP; NbExp=8; IntAct=EBI-746704, EBI-711399; CC Q9UJC3; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-746704, EBI-5661893; CC Q9UJC3; O00189: AP4M1; NbExp=4; IntAct=EBI-746704, EBI-3914106; CC Q9UJC3; P05067: APP; NbExp=3; IntAct=EBI-746704, EBI-77613; CC Q9UJC3; P35613: BSG; NbExp=3; IntAct=EBI-746704, EBI-750709; CC Q9UJC3; Q99459: CDC5L; NbExp=5; IntAct=EBI-746704, EBI-374880; CC Q9UJC3; P11802: CDK4; NbExp=14; IntAct=EBI-746704, EBI-295644; CC Q9UJC3; Q00535: CDK5; NbExp=3; IntAct=EBI-746704, EBI-1041567; CC Q9UJC3; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-746704, EBI-5453285; CC Q9UJC3; Q3B820: FAM161A; NbExp=5; IntAct=EBI-746704, EBI-719941; CC Q9UJC3; Q8N612-1: FHIP1B; NbExp=3; IntAct=EBI-746704, EBI-32806369; CC Q9UJC3; Q9UJC3: HOOK1; NbExp=6; IntAct=EBI-746704, EBI-746704; CC Q9UJC3; Q86VS8: HOOK3; NbExp=7; IntAct=EBI-746704, EBI-1777078; CC Q9UJC3; P25791: LMO2; NbExp=3; IntAct=EBI-746704, EBI-739696; CC Q9UJC3; P25791-3: LMO2; NbExp=3; IntAct=EBI-746704, EBI-11959475; CC Q9UJC3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-746704, EBI-16439278; CC Q9UJC3; O75376: NCOR1; NbExp=3; IntAct=EBI-746704, EBI-347233; CC Q9UJC3; O75928-2: PIAS2; NbExp=3; IntAct=EBI-746704, EBI-348567; CC Q9UJC3; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-746704, EBI-6872807; CC Q9UJC3; Q9P0N9: TBC1D7; NbExp=7; IntAct=EBI-746704, EBI-3258000; CC Q9UJC3; Q9UBB9: TFIP11; NbExp=8; IntAct=EBI-746704, EBI-1105213; CC Q9UJC3; O75604: USP2; NbExp=3; IntAct=EBI-746704, EBI-743272; CC Q9UJC3; Q5TAP6: UTP14C; NbExp=3; IntAct=EBI-746704, EBI-11737646; CC Q9UJC3; Q9UFB7: ZBTB47; NbExp=3; IntAct=EBI-746704, EBI-7781767; CC Q9UJC3; P13682: ZNF35; NbExp=3; IntAct=EBI-746704, EBI-11041653; CC Q9UJC3; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-746704, EBI-10172590; CC Q9UJC3; Q8N720: ZNF655; NbExp=3; IntAct=EBI-746704, EBI-625509; CC Q9UJC3; Q96H86: ZNF764; NbExp=3; IntAct=EBI-746704, EBI-745775; CC Q9UJC3; A8K8V0: ZNF785; NbExp=3; IntAct=EBI-746704, EBI-3925400; CC Q9UJC3; P51504: ZNF80; NbExp=3; IntAct=EBI-746704, EBI-12013828; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15471887}. CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11238449}. Note=Localizes CC to punctate cytoplasmic foci which do not appear to overlap with early CC or late endosomes, the endoplasmic reticulum, multivesicular bodies CC (MVBs), lysosomes, or mitochondria (By similarity). Often found in CC close association with microtubules (By similarity). Does not associate CC with the Golgi complex. During spermiogenesis, it localizes to the CC manchette in spermatids from steps 8-10. It is also present between the CC microtubule manchette and the nucleus. During manchette elongation, it CC is preferentially localized to the nuclear ring of the manchette, CC whereas the strong localization to the manchette decreases. In more CC mature spermatids, while the manchette migrates posteriorly, it CC localizes to punctuates spots. At later stages of spermatid CC differentiation, the punctuate expression pattern is found at both the CC attachment site and the proximal end of the elongated manchette. In CC contrast, it is not present in mature spermatozoa (By similarity). CC {ECO:0000250|UniProtKB:Q8BIL5}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UJC3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UJC3-2; Sequence=VSP_056226; CC -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF044923; AAC09298.1; -; mRNA. DR EMBL; AK292314; BAF85003.1; -; mRNA. DR EMBL; AK301768; BAG63227.1; -; mRNA. DR EMBL; AC113175; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL035416; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX06615.1; -; Genomic_DNA. DR EMBL; BC011621; AAH11621.1; -; mRNA. DR CCDS; CCDS612.1; -. [Q9UJC3-1] DR RefSeq; NP_056972.1; NM_015888.4. [Q9UJC3-1] DR AlphaFoldDB; Q9UJC3; -. DR SMR; Q9UJC3; -. DR BioGRID; 119496; 249. DR ComplexPortal; CPX-2353; FTS-Hook-FHIP cargo adaptor complex, FHIP1A-HOOK1/3 variant. DR ComplexPortal; CPX-2356; FTS-Hook-FHIP cargo adaptor complex, FHIP1B-HOOK1/3 variant. DR ComplexPortal; CPX-2359; FTS-Hook-FHIP cargo adaptor complex, FHIP2B-HOOK1/2/3 variant. DR CORUM; Q9UJC3; -. DR IntAct; Q9UJC3; 63. DR MINT; Q9UJC3; -. DR STRING; 9606.ENSP00000360252; -. DR GlyCosmos; Q9UJC3; 4 sites, 1 glycan. DR GlyGen; Q9UJC3; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q9UJC3; -. DR PhosphoSitePlus; Q9UJC3; -. DR BioMuta; HOOK1; -. DR DMDM; 41688595; -. DR EPD; Q9UJC3; -. DR jPOST; Q9UJC3; -. DR MassIVE; Q9UJC3; -. DR MaxQB; Q9UJC3; -. DR PaxDb; 9606-ENSP00000360252; -. DR PeptideAtlas; Q9UJC3; -. DR ProteomicsDB; 2080; -. DR ProteomicsDB; 84617; -. [Q9UJC3-1] DR Pumba; Q9UJC3; -. DR Antibodypedia; 19416; 287 antibodies from 28 providers. DR DNASU; 51361; -. DR Ensembl; ENST00000371208.5; ENSP00000360252.3; ENSG00000134709.13. [Q9UJC3-1] DR GeneID; 51361; -. DR KEGG; hsa:51361; -. DR MANE-Select; ENST00000371208.5; ENSP00000360252.3; NM_015888.6; NP_056972.1. DR UCSC; uc001czo.3; human. [Q9UJC3-1] DR AGR; HGNC:19884; -. DR CTD; 51361; -. DR DisGeNET; 51361; -. DR GeneCards; HOOK1; -. DR HGNC; HGNC:19884; HOOK1. DR HPA; ENSG00000134709; Tissue enhanced (retina). DR MIM; 607820; gene. DR neXtProt; NX_Q9UJC3; -. DR OpenTargets; ENSG00000134709; -. DR PharmGKB; PA134945565; -. DR VEuPathDB; HostDB:ENSG00000134709; -. DR eggNOG; ENOG502QW1T; Eukaryota. DR GeneTree; ENSGT00940000159251; -. DR HOGENOM; CLU_011214_1_0_1; -. DR InParanoid; Q9UJC3; -. DR OMA; TYKKQVQ; -. DR OrthoDB; 50921at2759; -. DR PhylomeDB; Q9UJC3; -. DR TreeFam; TF320231; -. DR PathwayCommons; Q9UJC3; -. DR SignaLink; Q9UJC3; -. DR SIGNOR; Q9UJC3; -. DR BioGRID-ORCS; 51361; 15 hits in 1155 CRISPR screens. DR ChiTaRS; HOOK1; human. DR GeneWiki; HOOK1; -. DR GenomeRNAi; 51361; -. DR Pharos; Q9UJC3; Tbio. DR PRO; PR:Q9UJC3; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UJC3; Protein. DR Bgee; ENSG00000134709; Expressed in sperm and 158 other cell types or tissues. DR ExpressionAtlas; Q9UJC3; baseline and differential. DR Genevisible; Q9UJC3; HS. DR GO; GO:0005813; C:centrosome; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. 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:0003779; F:actin binding; IEA:Ensembl. 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; IBA:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central. 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:0007030; P:Golgi organization; IEA:Ensembl. DR GO; GO:0007040; P:lysosome organization; IMP:UniProtKB. DR GO; GO:1905198; P:manchette assembly; IEA:Ensembl. 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 CDD; cd22225; HkD_Hook1; 1. DR Gene3D; 1.10.418.10; Calponin-like domain; 1. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR008636; Hook_C. DR InterPro; IPR043936; HOOK_N. DR PANTHER; PTHR18947; HOOK PROTEINS; 1. DR PANTHER; PTHR18947:SF36; PROTEIN HOOK HOMOLOG 1; 1. DR Pfam; PF05622; HOOK; 1. DR Pfam; PF19047; HOOK_N; 1. DR SUPFAM; SSF116907; Hook domain; 1. DR PROSITE; PS50021; CH; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; KW Developmental protein; Differentiation; Microtubule; Phosphoprotein; KW Protein transport; Reference proteome; Spermatogenesis; Transport. FT CHAIN 1..728 FT /note="Protein Hook homolog 1" FT /id="PRO_0000219192" FT DOMAIN 12..128 FT /note="Calponin-homology (CH)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT REGION 1..555 FT /note="Sufficient for interaction with microtubules" FT REGION 169..444 FT /note="Sufficient for homodimerization, interaction wit FT HOOK2, HOOK3 and AP4M1" FT /evidence="ECO:0000269|PubMed:32073997" FT REGION 481..512 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 657..728 FT /note="Sufficient for interaction with AKTIP and VPS18" FT /evidence="ECO:0000269|PubMed:18799622" FT COILED 169..434 FT /evidence="ECO:0000255" FT COILED 477..658 FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 235 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 699 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243" FT MOD_RES 719 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 727 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BIL5" FT VAR_SEQ 1..42 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056226" FT VARIANT 433 FT /note="S -> L (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035709" FT VARIANT 689 FT /note="G -> S (in dbSNP:rs1008809819)" FT /evidence="ECO:0000269|PubMed:26528954" FT /id="VAR_077930" FT MUTAGEN 661..662 FT /note="EE->AA: Abrogates interaction with AKTIP, VPS16, FT VPS18, VPS39 and VPS41, AP4M1, FHIP1B, decreases FT interaction with HOOK2 but does not affect interaction FT withHOOK3; when associated with 669-A-A-670." FT /evidence="ECO:0000269|PubMed:18799622, FT ECO:0000269|PubMed:32073997" FT MUTAGEN 669..670 FT /note="WY->AA: Abrogates interaction with AKTIP, VPS16, FT VPS18, VPS39 and VPS41, AP4M1, FHIP1B, decreases FT interaction with HOOK2 but does not affect interaction FT withHOOK3; when associated with 661-A-A-662." FT /evidence="ECO:0000269|PubMed:18799622, FT ECO:0000269|PubMed:32073997" SQ SEQUENCE 728 AA; 84648 MW; E35CA91F2BB89B3E CRC64; MEETQPPPQP KLPLCDSLMI WLQTFNTASP CQDVKQLTSG VAMAQVLHQI DAAWFNESWL SRIKEDVGDN WRIKASNVKK VLQGIMSYYH EFLGQQISEA LIPDLNQITE CSDPVELGRL LQLILGCAIN CEKKQEHIQN IMTLEESVQH VVMTAIQELM SKEILSSPPN DAVGELEQQL KRALEELQEA LAEKEELRQR CEELDMQVTT LQDEKNSLVS ENEMMNEKLD QLDGSFDDPN TVVAKKYFHA QLQLEQLQEE NFRLEAAKDD YRVHCEELEK QLIEFQHRND ELTSLAEETR ALKDEIDVLR ATSDKANKLE STVEIYRQKL QDLNDLRKQV KTLQETNMMY MHNTVSLEEE LKKANAARTQ LETYKRQVQD LHVKLSSESK RADTLAFEMK RLEEKHEALL KEKERLIEQR DTLKETNEEL RCSQVQQDHL NQTDASATKS YENLAAEIMP VEYREVFIRL QHENKMLRLQ QEGSENERIE ELQEQLEQKH RKMNELETEQ RLSKERIREL QQQIEDLQKS LQEQGSKSEG ESSSKLKQKL EAHMEKLTEV HEELQKKQEL IEDLQPDINQ NVQKINELEA ALQKKDEDMK AMEERYKMYL EKARNVIKTL DPKLNPASAE IMLLRKQLAE KERRIEILES ECKVAKFRDY EEKLIVSAWY NKSLAFQKLG MESRLVSGGG ACSDTGACTP ARSFLAQQRH ITNTRRNLSV KVPATTSD //