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   27-MAR-2024, entry version 171.
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=6; 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: DUSP13B; NbExp=3; IntAct=EBI-743290, EBI-749800;
CC       Q96ED9; Q5W0V3: FHIP2A; NbExp=4; IntAct=EBI-743290, EBI-7054959;
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; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-10961706, EBI-8643161;
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; 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; 192.
DR   ComplexPortal; CPX-2357; FTS-Hook-FHIP cargo adaptor complex, FHIP2A-HOOK2 variant.
DR   ComplexPortal; CPX-2359; FTS-Hook-FHIP cargo adaptor complex, FHIP2B-HOOK1/2/3 variant.
DR   CORUM; Q96ED9; -.
DR   IntAct; Q96ED9; 306.
DR   MINT; Q96ED9; -.
DR   STRING; 9606.ENSP00000380785; -.
DR   GlyGen; Q96ED9; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000380785; -.
DR   PeptideAtlas; Q96ED9; -.
DR   ProteomicsDB; 76396; -. [Q96ED9-1]
DR   ProteomicsDB; 76397; -. [Q96ED9-2]
DR   Pumba; Q96ED9; -.
DR   Antibodypedia; 26165; 137 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   AGR; HGNC:19885; -.
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; RGQLDTY; -.
DR   OrthoDB; 50921at2759; -.
DR   PhylomeDB; Q96ED9; -.
DR   TreeFam; TF320231; -.
DR   PathwayCommons; Q96ED9; -.
DR   SignaLink; Q96ED9; -.
DR   SIGNOR; Q96ED9; -.
DR   BioGRID-ORCS; 29911; 15 hits in 1154 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 153 other cell types or tissues.
DR   ExpressionAtlas; Q96ED9; baseline and differential.
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   CDD; cd22227; HkD_Hook2; 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:SF37; PROTEIN HOOK HOMOLOG 2; 1.
DR   Pfam; PF05622; HOOK; 1.
DR   Pfam; PF19047; HOOK_N; 1.
DR   SUPFAM; SSF116907; Hook domain; 1.
DR   PROSITE; PS50021; CH; 1.
DR   Genevisible; Q96ED9; HS.
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
//