HIP1R_HUMAN
ID HIP1R_HUMAN Reviewed; 1068 AA.
AC O75146; A6NHQ6; Q6NXG8; Q9UED9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Huntingtin-interacting protein 1-related protein;
DE Short=HIP1-related protein;
DE AltName: Full=Huntingtin-interacting protein 12;
DE Short=HIP-12;
GN Name=HIP1R; Synonyms=HIP12, KIAA0655;
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=11063258; DOI=10.1007/s003350010195;
RA Chopra V.S., Metzler M., Rasper D.M., Engqvist-Goldstein A.E.Y.,
RA Singaraja R., Gan L., Fichter K.M., McCutcheon K., Drubin D.,
RA Nicholson D.W., Hayden M.R.;
RT "HIP12 is a non-proapoptotic member of a gene family including HIP1, an
RT interacting protein with huntingtin.";
RL Mamm. Genome 11:1006-1015(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-345.
RC TISSUE=Pancreas;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 179-1068 (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RX PubMed=9852681; DOI=10.1007/s100380050087;
RA Seki N., Muramatsu M., Sugano S., Suzuki Y., Nakagawara A., Ohhira M.,
RA Hayashi A., Hori T., Saito T.;
RT "Cloning, expression analysis, and chromosomal localization of HIP1R, an
RT isolog of huntingtin interacting protein (HIP1).";
RL J. Hum. Genet. 43:268-271(1998).
RN [6]
RP FUNCTION, INTERACTION WITH CLTB AND HIP1, AND SUBCELLULAR LOCATION.
RX PubMed=11889126; DOI=10.1074/jbc.m112310200;
RA Legendre-Guillemin V., Metzler M., Charbonneau M., Gan L., Chopra V.,
RA Philie J., Hayden M.R., McPherson P.S.;
RT "HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin.
RT Identification of a novel interaction with clathrin light chain.";
RL J. Biol. Chem. 277:19897-19904(2002).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14732715; DOI=10.1074/jbc.m312645200;
RA Hyun T.S., Rao D.S., Saint-Dic D., Michael L.E., Kumar P.D., Bradley S.V.,
RA Mizukami I.F., Oravecz-Wilson K.I., Ross T.S.;
RT "HIP1 and HIP1r stabilize receptor tyrosine kinases and bind 3-
RT phosphoinositides via epsin N-terminal homology domains.";
RL J. Biol. Chem. 279:14294-14306(2004).
RN [8]
RP INTERACTION WITH CLTB.
RX PubMed=15533940; DOI=10.1074/jbc.m408454200;
RA Chen C.-Y., Brodsky F.M.;
RT "Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R)
RT bind the conserved sequence of clathrin light chains and thereby influence
RT clathrin assembly in vitro and actin distribution in vivo.";
RL J. Biol. Chem. 280:6109-6117(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1017, 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 BCL2L10.
RX PubMed=19255499; DOI=10.1159/000204088;
RA Kim J.H., Yoon S., Won M., Sim S.H., Ko J.J., Han S., Lee K.A., Lee K.,
RA Bae J.;
RT "HIP1R interacts with a member of Bcl-2 family, BCL2L10, and induces BAK-
RT dependent cell death.";
RL Cell. Physiol. Biochem. 23:43-52(2009).
RN [11]
RP IDENTIFICATION BY 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP IDENTIFICATION BY 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 [15]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 771-971, PARTIAL PROTEIN SEQUENCE,
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND MUTAGENESIS OF ARG-867;
RP GLY-871; ALA-875 AND 922-LYS--LYS-924.
RX PubMed=16415883; DOI=10.1038/nsmb1043;
RA Brett T.J., Legendre-Guillemin V., McPherson P.S., Fremont D.H.;
RT "Structural definition of the F-actin-binding THATCH domain from HIP1R.";
RL Nat. Struct. Mol. Biol. 13:121-130(2006).
CC -!- FUNCTION: Component of clathrin-coated pits and vesicles, that may link
CC the endocytic machinery to the actin cytoskeleton. Binds 3-
CC phosphoinositides (via ENTH domain). May act through the ENTH domain to
CC promote cell survival by stabilizing receptor tyrosine kinases
CC following ligand-induced endocytosis. {ECO:0000269|PubMed:11889126,
CC ECO:0000269|PubMed:14732715}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with actin;
CC homodimerization promotes actin binding (PubMed:16415883). Interacts
CC with CLTB (PubMed:11889126, PubMed:15533940). Interacts with HIP1
CC (PubMed:11889126). Interacts (via ENTH and I/LWEQ domains) with BCL2L10
CC (PubMed:19255499). {ECO:0000250|UniProtKB:Q9JKY5,
CC ECO:0000269|PubMed:11889126, ECO:0000269|PubMed:15533940,
CC ECO:0000269|PubMed:16415883, ECO:0000269|PubMed:19255499}.
CC -!- INTERACTION:
CC O75146; O75146: HIP1R; NbExp=2; IntAct=EBI-4402639, EBI-4402639;
CC O75146-2; O14777: NDC80; NbExp=3; IntAct=EBI-12292427, EBI-715849;
CC O75146-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-12292427, EBI-1105213;
CC O75146-2; P14373: TRIM27; NbExp=3; IntAct=EBI-12292427, EBI-719493;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endomembrane
CC system. Cytoplasmic vesicle, clathrin-coated vesicle membrane.
CC Note=Membrane-associated protein, mainly localized at the endocytic
CC compartments and in the perinuclear region.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75146-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75146-2; Sequence=VSP_054238, VSP_054239;
CC -!- TISSUE SPECIFICITY: Brain, heart, kidney, pancreas, and liver, but not
CC in lung or placenta.
CC -!- DOMAIN: Binds F-actin via the talin-like I/LWEQ domain.
CC -!- SIMILARITY: Belongs to the SLA2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31630.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB014555; BAA31630.1; ALT_INIT; mRNA.
DR EMBL; AC027290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067085; AAH67085.1; -; mRNA.
DR EMBL; AB013384; BAA33713.1; -; mRNA.
DR CCDS; CCDS31922.1; -. [O75146-1]
DR RefSeq; NP_001290026.1; NM_001303097.1. [O75146-2]
DR RefSeq; NP_003950.1; NM_003959.2. [O75146-1]
DR PDB; 1R0D; X-ray; 1.90 A; A/B/D/E/F/G/H/I=771-971.
DR PDBsum; 1R0D; -.
DR AlphaFoldDB; O75146; -.
DR SMR; O75146; -.
DR BioGRID; 114493; 160.
DR CORUM; O75146; -.
DR DIP; DIP-17042N; -.
DR IntAct; O75146; 50.
DR MINT; O75146; -.
DR STRING; 9606.ENSP00000253083; -.
DR GlyGen; O75146; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; O75146; -.
DR MetOSite; O75146; -.
DR PhosphoSitePlus; O75146; -.
DR SwissPalm; O75146; -.
DR BioMuta; HIP1R; -.
DR EPD; O75146; -.
DR jPOST; O75146; -.
DR MassIVE; O75146; -.
DR MaxQB; O75146; -.
DR PaxDb; O75146; -.
DR PeptideAtlas; O75146; -.
DR PRIDE; O75146; -.
DR ProteomicsDB; 49810; -. [O75146-1]
DR Antibodypedia; 31710; 307 antibodies from 32 providers.
DR DNASU; 9026; -.
DR Ensembl; ENST00000253083.9; ENSP00000253083.4; ENSG00000130787.14. [O75146-1]
DR GeneID; 9026; -.
DR KEGG; hsa:9026; -.
DR MANE-Select; ENST00000253083.9; ENSP00000253083.4; NM_003959.3; NP_003950.1.
DR UCSC; uc001udj.2; human. [O75146-1]
DR CTD; 9026; -.
DR DisGeNET; 9026; -.
DR GeneCards; HIP1R; -.
DR HGNC; HGNC:18415; HIP1R.
DR HPA; ENSG00000130787; Tissue enhanced (brain).
DR MIM; 605613; gene.
DR neXtProt; NX_O75146; -.
DR OpenTargets; ENSG00000130787; -.
DR PharmGKB; PA128394543; -.
DR VEuPathDB; HostDB:ENSG00000130787; -.
DR eggNOG; KOG0980; Eukaryota.
DR GeneTree; ENSGT00940000153594; -.
DR HOGENOM; CLU_006034_0_0_1; -.
DR InParanoid; O75146; -.
DR OMA; IREYVYF; -.
DR OrthoDB; 104219at2759; -.
DR PhylomeDB; O75146; -.
DR TreeFam; TF316860; -.
DR PathwayCommons; O75146; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; O75146; -.
DR SIGNOR; O75146; -.
DR BioGRID-ORCS; 9026; 15 hits in 1076 CRISPR screens.
DR ChiTaRS; HIP1R; human.
DR EvolutionaryTrace; O75146; -.
DR GeneWiki; HIP1R; -.
DR GenomeRNAi; 9026; -.
DR Pharos; O75146; Tbio.
DR PRO; PR:O75146; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O75146; protein.
DR Bgee; ENSG00000130787; Expressed in C1 segment of cervical spinal cord and 184 other tissues.
DR ExpressionAtlas; O75146; baseline and differential.
DR Genevisible; O75146; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0032839; C:dendrite cytoplasm; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043197; C:dendritic spine; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0043025; C:neuronal cell body; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0014069; C:postsynaptic density; ISS:ParkinsonsUK-UCL.
DR GO; GO:0032587; C:ruffle membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097060; C:synaptic membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0051015; F:actin filament binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:ParkinsonsUK-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0055123; P:digestive system development; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:ParkinsonsUK-UCL.
DR GO; GO:1905445; P:positive regulation of clathrin coat assembly; IEA:Ensembl.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IGI:ParkinsonsUK-UCL.
DR GO; GO:2000588; P:positive regulation of platelet-derived growth factor receptor-beta signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0050821; P:protein stabilization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; NAS:ParkinsonsUK-UCL.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0060453; P:regulation of gastric acid secretion; IEA:Ensembl.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR032422; HIP1_clath-bd.
DR InterPro; IPR030555; HIP1R.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR030224; Sla2_fam.
DR PANTHER; PTHR10407; PTHR10407; 1.
DR PANTHER; PTHR10407:SF10; PTHR10407:SF10; 1.
DR Pfam; PF07651; ANTH; 1.
DR Pfam; PF16515; HIP1_clath_bdg; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF109885; SSF109885; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW Endocytosis; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1068
FT /note="Huntingtin-interacting protein 1-related protein"
FT /id="PRO_0000083984"
FT DOMAIN 23..151
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 771..1012
FT /note="I/LWEQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00292"
FT REGION 424..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..924
FT /note="Important for actin binding"
FT REGION 1016..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 347..599
FT /evidence="ECO:0000255"
FT COMPBIAS 427..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 606..615
FT /note="ESQEQGLRQR -> VWPPQMQQHH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054238"
FT VAR_SEQ 616..1068
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054239"
FT VARIANT 345
FT /note="N -> S (in dbSNP:rs149504879)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_070814"
FT VARIANT 404
FT /note="K -> Q (in dbSNP:rs7972242)"
FT /id="VAR_051029"
FT VARIANT 516
FT /note="K -> Q (in dbSNP:rs7972242)"
FT /id="VAR_051030"
FT VARIANT 782
FT /note="V -> M (in dbSNP:rs2271051)"
FT /id="VAR_020043"
FT VARIANT 943
FT /note="N -> S (in dbSNP:rs3736414)"
FT /id="VAR_051031"
FT MUTAGEN 867
FT /note="R->D: Reduced acting binding."
FT /evidence="ECO:0000269|PubMed:16415883"
FT MUTAGEN 871
FT /note="G->D: Reduced acting binding."
FT /evidence="ECO:0000269|PubMed:16415883"
FT MUTAGEN 875
FT /note="A->D: Reduced acting binding."
FT /evidence="ECO:0000269|PubMed:16415883"
FT MUTAGEN 922..924
FT /note="KVK->DDD: Strongly reduced actin binding."
FT /evidence="ECO:0000269|PubMed:16415883"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:1R0D"
FT HELIX 779..811
FT /evidence="ECO:0007829|PDB:1R0D"
FT HELIX 814..852
FT /evidence="ECO:0007829|PDB:1R0D"
FT HELIX 858..864
FT /evidence="ECO:0007829|PDB:1R0D"
FT HELIX 866..895
FT /evidence="ECO:0007829|PDB:1R0D"
FT HELIX 900..922
FT /evidence="ECO:0007829|PDB:1R0D"
FT TURN 929..931
FT /evidence="ECO:0007829|PDB:1R0D"
FT HELIX 932..964
FT /evidence="ECO:0007829|PDB:1R0D"
SQ SEQUENCE 1068 AA; 119388 MW; 3CBC7CF1191BFF8F CRC64;
MNSIKNVPAR VLSRRPGHSL EAEREQFDKT QAISISKAIN TQEAPVKEKH ARRIILGTHH
EKGAFTFWSY AIGLPLPSSS ILSWKFCHVL HKVLRDGHPN VLHDCQRYRS NIREIGDLWG
HLHDRYGQLV NVYTKLLLTK ISFHLKHPQF PAGLEVTDEV LEKAAGTDVN NIFQLTVEMF
DYMDCELKLS ESVFRQLNTA IAVSQMSSGQ CRLAPLIQVI QDCSHLYHYT VKLLFKLHSC
LPADTLQGHR DRFHEQFHSL RNFFRRASDM LYFKRLIQIP RLPEGPPNFL RASALAEHIK
PVVVIPEEAP EDEEPENLIE ISTGPPAGEP VVVADLFDQT FGPPNGSVKD DRDLQIESLK
REVEMLRSEL EKIKLEAQRY IAQLKSQVNA LEGELEEQRK QKQKALVDNE QLRHELAQLR
AAQLEGERSQ GLREEAERKA SATEARYNKL KEKHSELVHV HAELLRKNAD TAKQLTVTQQ
SQEEVARVKE QLAFQVEQVK RESELKLEEK SDQLEKLKRE LEAKAGELAR AQEALSHTEQ
SKSELSSRLD TLSAEKDALS GAVRQREADL LAAQSLVRET EAALSREQQR SSQEQGELQG
RLAERESQEQ GLRQRLLDEQ FAVLRGAAAE AAGILQDAVS KLDDPLHLRC TSSPDYLVSR
AQEALDAVST LEEGHAQYLT SLADASALVA ALTRFSHLAA DTIINGGATS HLAPTDPADR
LIDTCRECGA RALELMGQLQ DQQALRHMQA SLVRTPLQGI LQLGQELKPK SLDVRQEELG
AVVDKEMAAT SAAIEDAVRR IEDMMNQARH ASSGVKLEVN ERILNSCTDL MKAIRLLVTT
STSLQKEIVE SGRGAATQQE FYAKNSRWTE GLISASKAVG WGATQLVEAA DKVVLHTGKY
EELIVCSHEI AASTAQLVAA SKVKANKHSP HLSRLQECSR TVNERAANVV ASTKSGQEQI
EDRDTMDFSG LSLIKLKKQE METQVRVLEL EKTLEAERMR LGELRKQHYV LAGASGSPGE
EVAIRPSTAP RSVTTKKPPL AQKPSVAPRQ DHQLDKKDGI YPAQLVNY
