HOOK2_HUMAN
ID HOOK2_HUMAN Reviewed; 719 AA.
AC Q96ED9; O60562;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Protein Hook homolog 2;
DE Short=h-hook2;
DE Short=hHK2;
GN Name=HOOK2;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLN-488.
RC TISSUE=Ovary;
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 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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17540036; DOI=10.1186/1471-2121-8-19;
RA Szebenyi G., Wigley W.C., Hall B., Didier A.J., Yu M., Thomas P.,
RA Kraemer H.;
RT "Hook2 contributes to aggresome formation.";
RL BMC Cell Biol. 8:19-19(2007).
RN [6]
RP FUNCTION, INTERACTION WITH CNTRL, AND SUBCELLULAR LOCATION.
RX PubMed=17140400; DOI=10.1111/j.1600-0854.2006.00511.x;
RA Szebenyi G., Hall B., Yu R., Hashim A.I., Kraemer H.;
RT "Hook2 localizes to the centrosome, binds directly to centriolin/CEP110 and
RT contributes to centrosomal function.";
RL Traffic 8:32-46(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FHF COMPLEX,
RP FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH AKTIP; HOOK1; HOOK3; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, 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 [10]
RP INTERACTION WITH ZC3H14.
RX PubMed=19273536; DOI=10.1093/hmg/ddp099;
RA Guthrie C.R., Schellenberg G.D., Kraemer B.C.;
RT "SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans.";
RL Hum. Mol. Genet. 18:1825-1838(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, 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 [13]
RP FUNCTION, INTERACTION WITH AP4M1 AND HOOK1, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF
CC complex may function to promote vesicle trafficking and/or fusion via
CC the homotypic vesicular protein sorting complex (the HOPS complex).
CC Contributes to the establishment and maintenance of centrosome
CC function. May function in the positioning or formation of aggresomes,
CC which are pericentriolar accumulations of misfolded proteins,
CC proteasomes and chaperones. FHF complex promotes the distribution of
CC AP-4 complex to the perinuclear area of the cell (PubMed:32073997).
CC {ECO:0000269|PubMed:17140400, ECO:0000269|PubMed:17540036,
CC ECO:0000269|PubMed:18799622, ECO:0000269|PubMed:32073997}.
CC -!- SUBUNIT: Self-associates (PubMed:18799622). Component of the
CC FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FHIP1B, and
CC one or more members of the Hook family of proteins HOOK1, HOOK2, and
CC HOOK3 (PubMed:18799622). May interact directly with AKTIP/FTS, HOOK1
CC and HOOK3 (PubMed:18799622, PubMed:32073997). Associates with several
CC subunits of the homotypic vesicular sorting complex (the HOPS complex)
CC including VPS16 and VPS41; these interactions may be indirect
CC (PubMed:18799622). Interacts with CNTRL (PubMed:17140400). Interacts
CC with microtubules (PubMed:11238449). Interacts with ZC3H14
CC (PubMed:19273536). Interacts with LRGUK (via guanylate kinase-like
CC domain) (By similarity). Interacts with CCDC181 (By similarity).
CC Interacts with AP4M1; the interaction is direct, mediates the
CC interaction between FTS-Hook-FHIP (FHF) complex and AP-4 and the
CC perinuclear distribution of AP-4 (PubMed:32073997).
CC {ECO:0000250|UniProtKB:Q7TMK6, ECO:0000269|PubMed:11238449,
CC ECO:0000269|PubMed:17140400, ECO:0000269|PubMed:18799622,
CC ECO:0000269|PubMed:19273536, ECO:0000269|PubMed:32073997}.
CC -!- INTERACTION:
CC Q96ED9; Q9H8T0: AKTIP; NbExp=3; IntAct=EBI-743290, EBI-711399;
CC Q96ED9; Q96IX9: ANKRD36BP1; NbExp=3; IntAct=EBI-743290, EBI-744859;
CC Q96ED9; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-743290, EBI-541426;
CC Q96ED9; Q8N5R6: CCDC33; NbExp=2; IntAct=EBI-743290, EBI-740841;
CC Q96ED9; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-743290, EBI-5453285;
CC Q96ED9; Q9UII6: DUSP13; NbExp=3; IntAct=EBI-743290, EBI-749800;
CC Q96ED9; Q7Z3B3: KANSL1; NbExp=4; IntAct=EBI-743290, EBI-740244;
CC Q96ED9; Q15311: RALBP1; NbExp=3; IntAct=EBI-743290, EBI-749285;
CC Q96ED9; O43463: SUV39H1; NbExp=4; IntAct=EBI-743290, EBI-349968;
CC Q96ED9; Q08E77: UTP14C; NbExp=3; IntAct=EBI-743290, EBI-10225961;
CC Q96ED9; Q53FD0: ZC2HC1C; NbExp=3; IntAct=EBI-743290, EBI-740767;
CC Q96ED9-2; Q9H8T0: AKTIP; NbExp=3; IntAct=EBI-10961706, EBI-711399;
CC Q96ED9-2; X5D778: ANKRD11; NbExp=4; IntAct=EBI-10961706, EBI-17183751;
CC Q96ED9-2; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-10961706, EBI-541426;
CC Q96ED9-2; Q9H1Y0: ATG5; NbExp=3; IntAct=EBI-10961706, EBI-1047414;
CC Q96ED9-2; Q13895: BYSL; NbExp=3; IntAct=EBI-10961706, EBI-358049;
CC Q96ED9-2; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-10961706, EBI-8643161;
CC Q96ED9-2; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-10961706, EBI-12011224;
CC Q96ED9-2; Q9HC52: CBX8; NbExp=3; IntAct=EBI-10961706, EBI-712912;
CC Q96ED9-2; E9PSE9: CCDC198; NbExp=3; IntAct=EBI-10961706, EBI-11748295;
CC Q96ED9-2; Q07002: CDK18; NbExp=3; IntAct=EBI-10961706, EBI-746238;
CC Q96ED9-2; P38936: CDKN1A; NbExp=3; IntAct=EBI-10961706, EBI-375077;
CC Q96ED9-2; Q96GE4: CEP95; NbExp=3; IntAct=EBI-10961706, EBI-372775;
CC Q96ED9-2; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-10961706, EBI-5453285;
CC Q96ED9-2; Q9UIA0: CYTH4; NbExp=3; IntAct=EBI-10961706, EBI-11521003;
CC Q96ED9-2; O43602-2: DCX; NbExp=3; IntAct=EBI-10961706, EBI-14148644;
CC Q96ED9-2; P26196: DDX6; NbExp=3; IntAct=EBI-10961706, EBI-351257;
CC Q96ED9-2; O15371: EIF3D; NbExp=3; IntAct=EBI-10961706, EBI-353818;
CC Q96ED9-2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-10961706, EBI-744099;
CC Q96ED9-2; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-10961706, EBI-1752811;
CC Q96ED9-2; Q3B820: FAM161A; NbExp=3; IntAct=EBI-10961706, EBI-719941;
CC Q96ED9-2; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-10961706, EBI-7225287;
CC Q96ED9-2; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-10961706, EBI-742802;
CC Q96ED9-2; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-10961706, EBI-6658203;
CC Q96ED9-2; O43320: FGF16; NbExp=3; IntAct=EBI-10961706, EBI-11479104;
CC Q96ED9-2; Q4VC44: FLYWCH1; NbExp=3; IntAct=EBI-10961706, EBI-719415;
CC Q96ED9-2; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-10961706, EBI-7960826;
CC Q96ED9-2; P55040: GEM; NbExp=3; IntAct=EBI-10961706, EBI-744104;
CC Q96ED9-2; Q92917: GPKOW; NbExp=3; IntAct=EBI-10961706, EBI-746309;
CC Q96ED9-2; P56524-2: HDAC4; NbExp=3; IntAct=EBI-10961706, EBI-11953488;
CC Q96ED9-2; P09067: HOXB5; NbExp=3; IntAct=EBI-10961706, EBI-3893317;
CC Q96ED9-2; Q14005-2: IL16; NbExp=3; IntAct=EBI-10961706, EBI-17178971;
CC Q96ED9-2; Q9Y573-2: IPP; NbExp=3; IntAct=EBI-10961706, EBI-10976190;
CC Q96ED9-2; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-10961706, EBI-8472129;
CC Q96ED9-2; P04264: KRT1; NbExp=3; IntAct=EBI-10961706, EBI-298429;
CC Q96ED9-2; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-10961706, EBI-726510;
CC Q96ED9-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10961706, EBI-739832;
CC Q96ED9-2; Q96M69: LRGUK; NbExp=3; IntAct=EBI-10961706, EBI-9478535;
CC Q96ED9-2; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-10961706, EBI-348259;
CC Q96ED9-2; P55081: MFAP1; NbExp=3; IntAct=EBI-10961706, EBI-1048159;
CC Q96ED9-2; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-10961706, EBI-14086479;
CC Q96ED9-2; Q6PF18: MORN3; NbExp=3; IntAct=EBI-10961706, EBI-9675802;
CC Q96ED9-2; Q15777: MPPED2; NbExp=3; IntAct=EBI-10961706, EBI-2350461;
CC Q96ED9-2; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-10961706, EBI-6952711;
CC Q96ED9-2; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-10961706, EBI-11750983;
CC Q96ED9-2; P00973-2: OAS1; NbExp=3; IntAct=EBI-10961706, EBI-12081862;
CC Q96ED9-2; Q9NR21-1: PARP11; NbExp=3; IntAct=EBI-10961706, EBI-17644640;
CC Q96ED9-2; Q9BSJ6: PIMREG; NbExp=3; IntAct=EBI-10961706, EBI-2568609;
CC Q96ED9-2; Q13835-2: PKP1; NbExp=3; IntAct=EBI-10961706, EBI-9087684;
CC Q96ED9-2; Q99959-2: PKP2; NbExp=3; IntAct=EBI-10961706, EBI-10987518;
CC Q96ED9-2; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-10961706, EBI-2557469;
CC Q96ED9-2; Q5T8A7: PPP1R26; NbExp=3; IntAct=EBI-10961706, EBI-308500;
CC Q96ED9-2; Q99633: PRPF18; NbExp=3; IntAct=EBI-10961706, EBI-2798416;
CC Q96ED9-2; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-10961706, EBI-1567797;
CC Q96ED9-2; P0CG20: PRR35; NbExp=3; IntAct=EBI-10961706, EBI-11986293;
CC Q96ED9-2; P25786: PSMA1; NbExp=3; IntAct=EBI-10961706, EBI-359352;
CC Q96ED9-2; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-10961706, EBI-14093916;
CC Q96ED9-2; Q15311: RALBP1; NbExp=3; IntAct=EBI-10961706, EBI-749285;
CC Q96ED9-2; Q96IZ5: RBM41; NbExp=3; IntAct=EBI-10961706, EBI-740773;
CC Q96ED9-2; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-10961706, EBI-1504830;
CC Q96ED9-2; P57771-2: RGS8; NbExp=3; IntAct=EBI-10961706, EBI-12058229;
CC Q96ED9-2; Q8NCN4: RNF169; NbExp=3; IntAct=EBI-10961706, EBI-6380946;
CC Q96ED9-2; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-10961706, EBI-16428950;
CC Q96ED9-2; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-10961706, EBI-748391;
CC Q96ED9-2; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-10961706, EBI-747035;
CC Q96ED9-2; Q13573: SNW1; NbExp=3; IntAct=EBI-10961706, EBI-632715;
CC Q96ED9-2; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-10961706, EBI-11995806;
CC Q96ED9-2; O43463: SUV39H1; NbExp=3; IntAct=EBI-10961706, EBI-349968;
CC Q96ED9-2; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-10961706, EBI-745392;
CC Q96ED9-2; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-10961706, EBI-10246152;
CC Q96ED9-2; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-10961706, EBI-8787464;
CC Q96ED9-2; Q9Y2I9-2: TBC1D30; NbExp=3; IntAct=EBI-10961706, EBI-17455779;
CC Q96ED9-2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-10961706, EBI-11955057;
CC Q96ED9-2; Q9BT92: TCHP; NbExp=3; IntAct=EBI-10961706, EBI-740781;
CC Q96ED9-2; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-10961706, EBI-744794;
CC Q96ED9-2; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-10961706, EBI-10241197;
CC Q96ED9-2; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-10961706, EBI-9090990;
CC Q96ED9-2; O75604: USP2; NbExp=3; IntAct=EBI-10961706, EBI-743272;
CC Q96ED9-2; Q5TAP6: UTP14C; NbExp=3; IntAct=EBI-10961706, EBI-11737646;
CC Q96ED9-2; Q9UFB7: ZBTB47; NbExp=3; IntAct=EBI-10961706, EBI-7781767;
CC Q96ED9-2; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-10961706, EBI-14104088;
CC Q96ED9-2; Q6P2D0: ZFP1; NbExp=3; IntAct=EBI-10961706, EBI-2555749;
CC Q96ED9-2; Q68DK2-5: ZFYVE26; NbExp=3; IntAct=EBI-10961706, EBI-8656416;
CC Q96ED9-2; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-10961706, EBI-10183064;
CC Q96ED9-2; Q9UII5: ZNF107; NbExp=3; IntAct=EBI-10961706, EBI-7234993;
CC Q96ED9-2; P15622-3: ZNF250; NbExp=3; IntAct=EBI-10961706, EBI-10177272;
CC Q96ED9-2; P13682: ZNF35; NbExp=3; IntAct=EBI-10961706, EBI-11041653;
CC Q96ED9-2; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-10961706, EBI-740727;
CC Q96ED9-2; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-10961706, EBI-12006434;
CC Q96ED9-2; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-10961706, EBI-10486136;
CC Q96ED9-2; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-10961706, EBI-10172590;
CC Q96ED9-2; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-10961706, EBI-6427977;
CC Q96ED9-2; Q5T619: ZNF648; NbExp=3; IntAct=EBI-10961706, EBI-11985915;
CC Q96ED9-2; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-10961706, EBI-5667516;
CC Q96ED9-2; Q08AG5: ZNF844; NbExp=3; IntAct=EBI-10961706, EBI-10225757;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:17140400}. Cytoplasm
CC {ECO:0000269|PubMed:32073997}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q7TMK6}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:32073997}. Note=Colocalizes with aggresomes, which
CC are aggregates of misfolded proteins, at the centrosome
CC (PubMed:17540036). Also localizes to punctate cytoplasmic foci which do
CC not appear to overlap with early or late endosomes, the endoplasmic
CC reticulum, multivesicular bodies (MVBs), lysosome, or mitochondria
CC (PubMed:17540036, PubMed:32073997). Often found in close association
CC with microtubules (PubMed:17540036). Localizes to the manchette in
CC elongating spermatids (By similarity). {ECO:0000250|UniProtKB:Q7TMK6,
CC ECO:0000269|PubMed:17540036, ECO:0000269|PubMed:32073997}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96ED9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96ED9-2; Sequence=VSP_009342;
CC -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
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DR EMBL; AF044924; AAC09299.1; -; mRNA.
DR EMBL; AC018761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012443; AAH12443.1; -; mRNA.
DR CCDS; CCDS42507.1; -. [Q96ED9-2]
DR CCDS; CCDS42508.1; -. [Q96ED9-1]
DR RefSeq; NP_001093646.1; NM_001100176.1. [Q96ED9-2]
DR RefSeq; NP_037444.2; NM_013312.2. [Q96ED9-1]
DR AlphaFoldDB; Q96ED9; -.
DR SMR; Q96ED9; -.
DR BioGRID; 118957; 188.
DR CORUM; Q96ED9; -.
DR IntAct; Q96ED9; 140.
DR MINT; Q96ED9; -.
DR STRING; 9606.ENSP00000380785; -.
DR iPTMnet; Q96ED9; -.
DR PhosphoSitePlus; Q96ED9; -.
DR BioMuta; HOOK2; -.
DR DMDM; 296439323; -.
DR EPD; Q96ED9; -.
DR jPOST; Q96ED9; -.
DR MassIVE; Q96ED9; -.
DR MaxQB; Q96ED9; -.
DR PaxDb; Q96ED9; -.
DR PeptideAtlas; Q96ED9; -.
DR PRIDE; Q96ED9; -.
DR ProteomicsDB; 76396; -. [Q96ED9-1]
DR ProteomicsDB; 76397; -. [Q96ED9-2]
DR Antibodypedia; 26165; 111 antibodies from 22 providers.
DR DNASU; 29911; -.
DR Ensembl; ENST00000264827.9; ENSP00000264827.4; ENSG00000095066.12. [Q96ED9-2]
DR Ensembl; ENST00000397668.8; ENSP00000380785.2; ENSG00000095066.12. [Q96ED9-1]
DR GeneID; 29911; -.
DR KEGG; hsa:29911; -.
DR MANE-Select; ENST00000397668.8; ENSP00000380785.2; NM_013312.3; NP_037444.2.
DR UCSC; uc002muy.3; human. [Q96ED9-1]
DR CTD; 29911; -.
DR DisGeNET; 29911; -.
DR GeneCards; HOOK2; -.
DR HGNC; HGNC:19885; HOOK2.
DR HPA; ENSG00000095066; Low tissue specificity.
DR MIM; 607824; gene.
DR neXtProt; NX_Q96ED9; -.
DR OpenTargets; ENSG00000095066; -.
DR PharmGKB; PA134986864; -.
DR VEuPathDB; HostDB:ENSG00000095066; -.
DR eggNOG; ENOG502QTJ1; Eukaryota.
DR GeneTree; ENSGT00940000160152; -.
DR HOGENOM; CLU_011214_2_0_1; -.
DR InParanoid; Q96ED9; -.
DR OMA; QRYKRYM; -.
DR OrthoDB; 398210at2759; -.
DR PhylomeDB; Q96ED9; -.
DR TreeFam; TF320231; -.
DR PathwayCommons; Q96ED9; -.
DR SignaLink; Q96ED9; -.
DR SIGNOR; Q96ED9; -.
DR BioGRID-ORCS; 29911; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; HOOK2; human.
DR GeneWiki; HOOK2; -.
DR GenomeRNAi; 29911; -.
DR Pharos; Q96ED9; Tbio.
DR PRO; PR:Q96ED9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96ED9; protein.
DR Bgee; ENSG00000095066; Expressed in right lobe of thyroid gland and 151 other tissues.
DR ExpressionAtlas; Q96ED9; baseline and differential.
DR Genevisible; Q96ED9; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070695; C:FHF complex; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IDA: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; IBA:GO_Central.
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:0006897; P:endocytosis; TAS:ProtInc.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IMP:UniProtKB.
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 Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Microtubule; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..719
FT /note="Protein Hook homolog 2"
FT /id="PRO_0000219194"
FT DOMAIN 6..122
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..548
FT /note="Sufficient for interaction with microtubules"
FT REGION 1..161
FT /note="Required for localization to the centrosome and
FT induction of aggresome formation"
FT REGION 533..719
FT /note="Required for localization to the centrosome and
FT induction of aggresome formation"
FT REGION 584..719
FT /note="Sufficient for interaction with CNTRL"
FT /evidence="ECO:0000269|PubMed:17140400"
FT REGION 696..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..427
FT /evidence="ECO:0000255"
FT COILED 455..607
FT /evidence="ECO:0000255"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 534..535
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009342"
FT VARIANT 10
FT /note="G -> R (in dbSNP:rs2305376)"
FT /id="VAR_017575"
FT VARIANT 488
FT /note="H -> Q (in dbSNP:rs897804)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_017576"
FT CONFLICT 376
FT /note="R -> L (in Ref. 1; AAC09299)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 719 AA; 83207 MW; FDF5F8A53DEE9DB6 CRC64;
MSVDKAELCG SLLTWLQTFH VPSPCASPQD LSSGLAVAYV LNQIDPSWFN EAWLQGISED
PGPNWKLKVS NLKMVLRSLV EYSQDVLAHP VSEEHLPDVS LIGEFSDPAE LGKLLQLVLG
CAISCEKKQD HIQRIMTLEE SVQHVVMEAI QELMTKDTPD SLSPETYGNF DSQSRRYYFL
SEEAEEGDEL QQRCLDLERQ LMLLSEEKQS LAQENAGLRE RMGRPEGEGT PGLTAKKLLL
LQSQLEQLQE ENFRLESGRE DERLRCAELE REVAELQHRN QALTSLAQEA QALKDEMDEL
RQSSERAGQL EATLTSCRRR LGELRELRRQ VRQLEERNAG HAERTRQLED ELRRAGSLRA
QLEAQRRQVQ ELQGQRQEEA MKAEKWLFEC RNLEEKYESV TKEKERLLAE RDSLREANEE
LRCAQLQPRG LTQADPSLDP TSTPVDNLAA EILPAELRET LLRLQLENKR LCRQEAADRE
RQEELQRHLE DANRARHGLE TQHRLNQQQL SELRAQVEDL QKALQEQGGK TEDAISILLK
RKLEEHLQKL HEADLELQRK REYIEELEPP TDSSTARRIE ELQHNLQKKD ADLRAMEERY
RRYVDKARMV MQTMEPKQRP AAGAPPELHS LRTQLRERDV RIRHLEMDFE KSRSQREQEE
KLLISAWYNM GMALQQRAGE ERAPAHAQSF LAQQRLATNS RRGPLGRLAS LNLRPTDKH
