HOOK1_HUMAN
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 03-AUG-2022, entry version 171.
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=6; IntAct=EBI-746704, EBI-711399;
CC Q9UJC3; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-746704, EBI-5661893;
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; Q9UJC3: HOOK1; NbExp=4; IntAct=EBI-746704, EBI-746704;
CC Q9UJC3; Q86VS8: HOOK3; NbExp=4; 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}.
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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; 231.
DR CORUM; Q9UJC3; -.
DR IntAct; Q9UJC3; 52.
DR MINT; Q9UJC3; -.
DR STRING; 9606.ENSP00000360252; -.
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; Q9UJC3; -.
DR PeptideAtlas; Q9UJC3; -.
DR PRIDE; Q9UJC3; -.
DR ProteomicsDB; 2080; -.
DR ProteomicsDB; 84617; -. [Q9UJC3-1]
DR Antibodypedia; 19416; 262 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 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; LRYSQMQ; -.
DR OrthoDB; 398210at2759; -.
DR PhylomeDB; Q9UJC3; -.
DR TreeFam; TF320231; -.
DR PathwayCommons; Q9UJC3; -.
DR SignaLink; Q9UJC3; -.
DR SIGNOR; Q9UJC3; -.
DR BioGRID-ORCS; 51361; 13 hits in 1076 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 156 other 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 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 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
