HOOK2_MOUSE
ID HOOK2_MOUSE Reviewed; 716 AA.
AC Q7TMK6; Q66JV2; Q8BY47; Q8R347; Q8VCN4; Q99LU2;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein Hook homolog 2;
DE Short=mHK2;
GN Name=Hook2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Kidney, Liver, and Mammary tumor;
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 [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [4]
RP INTERACTION WITH LRGUK, AND SUBCELLULAR LOCATION.
RX PubMed=25781171; DOI=10.1371/journal.pgen.1005090;
RA Liu Y., DeBoer K., de Kretser D.M., O'Donnell L., O'Connor A.E.,
RA Merriner D.J., Okuda H., Whittle B., Jans D.A., Efthymiadis A.,
RA McLachlan R.I., Ormandy C.J., Goodnow C.C., Jamsai D., O'Bryan M.K.;
RT "LRGUK-1 is required for basal body and manchette function during
RT spermatogenesis and male fertility.";
RL PLoS Genet. 11:E1005090-E1005090(2015).
RN [5]
RP INTERACTION WITH CCDC181.
RX PubMed=28283191; DOI=10.1016/j.ejcb.2017.02.003;
RA Schwarz T., Prieler B., Schmid J.A., Grzmil P., Neesen J.;
RT "Ccdc181 is a microtubule-binding protein that interacts with Hook1 in
RT haploid male germ cells and localizes to the sperm tail and motile cilia.";
RL Eur. J. Cell Biol. 96:276-288(2017).
RN [6]
RP INTERACTION WITH LRGUK, AND SUBCELLULAR LOCATION.
RX PubMed=28003339; DOI=10.1096/fj.201600909r;
RA Okuda H., DeBoer K., O'Connor A.E., Merriner D.J., Jamsai D., O'Bryan M.K.;
RT "LRGUK1 is part of a multiprotein complex required for manchette function
RT and male fertility.";
RL FASEB J. 31:1141-1152(2017).
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.
CC {ECO:0000250|UniProtKB:Q96ED9}.
CC -!- SUBUNIT: Self-associates (By similarity). 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 (By similarity). May interact directly with AKTIP/FTS, HOOK1 and
CC HOOK3 (By similarity). Associates with several subunits of the
CC homotypic vesicular sorting complex (the HOPS complex) including VPS16
CC and VPS41; these interactions may be indirect (By similarity).
CC Interacts with CNTRL (By similarity). Interacts with microtubules (By
CC similarity). Interacts with ZC3H14 (By similarity). Interacts with
CC LRGUK (via guanylate kinase-like domain) (PubMed:25781171,
CC PubMed:28003339). Interacts with CCDC181 (PubMed:28283191). 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 (By similarity). {ECO:0000250|UniProtKB:Q96ED9,
CC ECO:0000269|PubMed:25781171, ECO:0000269|PubMed:28003339,
CC ECO:0000269|PubMed:28283191}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:17140400,
CC ECO:0000269|PubMed:25781171}. Cytoplasm {ECO:0000269|PubMed:17140400}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17140400,
CC ECO:0000269|PubMed:28003339}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q96ED9}. Note=Colocalizes with aggresomes, which
CC are aggregates of misfolded proteins, at the centrosome. Also 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), lysosome, or mitochondria (By similarity). Often found in close
CC association with microtubules (By similarity). Localizes to the
CC manchette in elongating spermatids (PubMed:28003339).
CC {ECO:0000250|UniProtKB:Q96ED9, ECO:0000269|PubMed:28003339}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, cerebellum, kidney, liver and
CC heart, with highest levels in heart and kidney (at protein level).
CC {ECO:0000269|PubMed:17140400}.
CC -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02226.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK042048; BAC31143.1; -; mRNA.
DR EMBL; AK145768; BAE26639.1; -; mRNA.
DR EMBL; AK169073; BAE40859.1; -; mRNA.
DR EMBL; BC002226; AAH02226.1; ALT_INIT; mRNA.
DR EMBL; BC019486; AAH19486.1; -; mRNA.
DR EMBL; BC026609; AAH26609.1; -; mRNA.
DR EMBL; BC055881; AAH55881.1; -; mRNA.
DR EMBL; BC080744; AAH80744.1; -; mRNA.
DR CCDS; CCDS22489.1; -.
DR RefSeq; NP_001161463.1; NM_001167991.1.
DR RefSeq; NP_573518.2; NM_133255.2.
DR AlphaFoldDB; Q7TMK6; -.
DR SMR; Q7TMK6; -.
DR BioGRID; 228463; 3.
DR IntAct; Q7TMK6; 3.
DR STRING; 10090.ENSMUSP00000067752; -.
DR iPTMnet; Q7TMK6; -.
DR PhosphoSitePlus; Q7TMK6; -.
DR EPD; Q7TMK6; -.
DR MaxQB; Q7TMK6; -.
DR PaxDb; Q7TMK6; -.
DR PRIDE; Q7TMK6; -.
DR ProteomicsDB; 273377; -.
DR Antibodypedia; 26165; 111 antibodies from 22 providers.
DR DNASU; 170833; -.
DR Ensembl; ENSMUST00000064495; ENSMUSP00000067752; ENSMUSG00000052566.
DR GeneID; 170833; -.
DR KEGG; mmu:170833; -.
DR UCSC; uc009moq.2; mouse.
DR CTD; 29911; -.
DR MGI; MGI:2181664; Hook2.
DR VEuPathDB; HostDB:ENSMUSG00000052566; -.
DR eggNOG; ENOG502QTJ1; Eukaryota.
DR GeneTree; ENSGT00940000160152; -.
DR HOGENOM; CLU_011214_1_0_1; -.
DR InParanoid; Q7TMK6; -.
DR OMA; QRYKRYM; -.
DR OrthoDB; 398210at2759; -.
DR PhylomeDB; Q7TMK6; -.
DR TreeFam; TF320231; -.
DR BioGRID-ORCS; 170833; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Hook2; mouse.
DR PRO; PR:Q7TMK6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q7TMK6; protein.
DR Bgee; ENSMUSG00000052566; Expressed in submandibular gland primordium and 175 other tissues.
DR ExpressionAtlas; Q7TMK6; baseline and differential.
DR Genevisible; Q7TMK6; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070695; C:FHF complex; ISS:UniProtKB.
DR GO; GO:0030897; C:HOPS complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; ISS: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 Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus; Microtubule;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..716
FT /note="Protein Hook homolog 2"
FT /id="PRO_0000219195"
FT DOMAIN 6..122
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..546
FT /note="Sufficient for interaction with microtubules"
FT /evidence="ECO:0000250"
FT REGION 1..161
FT /note="Required for localization to the centrosome and
FT induction of aggresome formation"
FT /evidence="ECO:0000250"
FT REGION 533..716
FT /note="Required for localization to the centrosome and
FT induction of aggresome formation"
FT /evidence="ECO:0000250"
FT REGION 582..716
FT /note="Sufficient for interaction with CNTRL"
FT /evidence="ECO:0000250"
FT COILED 188..427
FT /evidence="ECO:0000255"
FT COILED 455..605
FT /evidence="ECO:0000255"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ED9"
FT CONFLICT 51
FT /note="N -> D (in Ref. 2; AAH19486)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="T -> A (in Ref. 2; AAH19486)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="A -> T (in Ref. 2; AAH19486/AAH26609)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="Missing (in Ref. 2; AAH55881)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="L -> M (in Ref. 1; BAC31143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 83366 MW; F8056FDE58E83DC5 CRC64;
MSVDKAELCG SLLTWLQTFQ VSPPCASPQD LSSGLAIAHV LNQIDPSWFN NEWLQGISED
SSPSWRLKVR KLEKILQSLV EYSKNVLGHP VSDQHLPDVS LIGEFSNPAE LGKLLQLVLG
CAISCEKKQE YIQRIMTLEE SVQHVVMEAI QELMTKDTPD SLSPENYGNF DTQSRRYYFL
SEEVEEGDHL QQHYLDLERQ LLLLSEEKQN LAQENAALRE RVGRSEVESA PGLTAKKLLL
LQSQLEQLQE ENFRLESSRE DDRLRCLELE REVAELQQRN QALTSLSQEA QALKDEMDEL
RQSSERARQL EATLNSCRRR LGELQELRRQ VRQLEERNAG HAERTRQLEE ELRRAGSLRA
QLEAQRRQVQ ELQGQWQEEA MKAEKWLFEC RNLEEKCDLV TKEKERLLTE RDSLREANEE
LRCAQLQPRG LAQADLSLDP TPSGLENLAA EILPAELRET LVRLQLENKR LCQQEAADRE
RQEELQRHLE EANRARHGLE AQQRLNQQQL SELRAQVEEL QKALQEQGGK TEDPTLLKRK
LEDHLQKLHE ADLELQRKRE YIEELEPPTD SSTARRIEEL QDSLQKKDAD LRAMEERYRR
YVDKARTVIQ TLEPKQRPPT VVSPEFHTLR SQLWERNLRI RQMEMDYEKS RRRQEQEEKL
LISAWYSMGM ALEHRAGEEH APAHAQSFLA QQRLATNARR GPLGRQALSL RPTDKH
