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   27-MAR-2024, entry version 199.
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; 174.
DR   CORUM; O75146; -.
DR   DIP; DIP-17042N; -.
DR   IntAct; O75146; 51.
DR   MINT; O75146; -.
DR   STRING; 9606.ENSP00000253083; -.
DR   GlyCosmos; O75146; 2 sites, 2 glycans.
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; 9606-ENSP00000253083; -.
DR   PeptideAtlas; O75146; -.
DR   ProteomicsDB; 49810; -. [O75146-1]
DR   Pumba; O75146; -.
DR   Antibodypedia; 31710; 339 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   AGR; HGNC:18415; -.
DR   CTD; 9026; -.
DR   DisGeNET; 9026; -.
DR   GeneCards; HIP1R; -.
DR   HGNC; HGNC:18415; HIP1R.
DR   HPA; ENSG00000130787; Low tissue specificity.
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; NREMSDL; -.
DR   OrthoDB; 7775at2759; -.
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; 28 hits in 1154 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 186 other cell types or tissues.
DR   ExpressionAtlas; O75146; baseline and differential.
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:0098978; C:glutamatergic synapse; IEA:Ensembl.
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: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:0099173; P:postsynapse organization; IEA:Ensembl.
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   CDD; cd17014; ANTH_N_HIP1R; 1.
DR   Gene3D; 1.20.5.1700; -; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 6.10.250.920; -; 1.
DR   Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR   InterPro; IPR011417; ANTH_dom.
DR   InterPro; IPR013809; ENTH.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR032422; HIP1_clath-bd.
DR   InterPro; IPR035964; I/LWEQ_dom_sf.
DR   InterPro; IPR002558; ILWEQ_dom.
DR   InterPro; IPR030224; Sla2_fam.
DR   PANTHER; PTHR10407; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR10407:SF10; HUNTINGTIN-INTERACTING PROTEIN 1-RELATED PROTEIN; 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; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF109885; I/LWEQ domain; 1.
DR   PROSITE; PS50942; ENTH; 1.
DR   PROSITE; PS50945; I_LWEQ; 1.
DR   Genevisible; O75146; HS.
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
//