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O75146

- HIP1R_HUMAN

UniProt

O75146 - HIP1R_HUMAN

Protein

Huntingtin-interacting protein 1-related protein

Gene

HIP1R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (27 Apr 2001)
      Previous versions | rss
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    Functioni

    Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis.2 Publications

    GO - Molecular functioni

    1. phosphatidylinositol binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. receptor-mediated endocytosis Source: UniProtKB

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Huntingtin-interacting protein 1-related protein
    Short name:
    HIP1-related protein
    Alternative name(s):
    Huntingtin-interacting protein 12
    Short name:
    HIP-12
    Gene namesi
    Name:HIP1R
    Synonyms:HIP12, KIAA0655
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18415. HIP1R.

    Subcellular locationi

    Cytoplasmperinuclear region. Endomembrane system. Cytoplasmic vesicleclathrin-coated vesicle membrane
    Note: Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region.

    GO - Cellular componenti

    1. clathrin-coated vesicle Source: UniProtKB
    2. clathrin-coated vesicle membrane Source: UniProtKB-SubCell
    3. coated pit Source: Ensembl
    4. cytoplasm Source: HPA
    5. cytoskeleton Source: Ensembl
    6. intracellular membrane-bounded organelle Source: HPA
    7. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi867 – 8671R → D: Reduced acting binding. 1 Publication
    Mutagenesisi871 – 8711G → D: Reduced acting binding. 1 Publication
    Mutagenesisi875 – 8751A → D: Reduced acting binding. 1 Publication
    Mutagenesisi922 – 9243KVK → DDD: Strongly reduced actin binding.

    Organism-specific databases

    PharmGKBiPA128394543.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10681068Huntingtin-interacting protein 1-related proteinPRO_0000083984Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei1017 – 10171Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO75146.
    PaxDbiO75146.
    PRIDEiO75146.

    PTM databases

    PhosphoSiteiO75146.

    Expressioni

    Tissue specificityi

    Brain, heart, kidney, pancreas, and liver, but not in lung or placenta.

    Gene expression databases

    ArrayExpressiO75146.
    BgeeiO75146.
    CleanExiHS_HIP1R.
    GenevestigatoriO75146.

    Organism-specific databases

    HPAiCAB017187.
    HPA038135.
    HPA038136.

    Interactioni

    Subunit structurei

    Interacts with actin. Does not interact with huntingtin By similarity. Interacts with CLTB and HIP1. Homodimer. Homodimerization promotes actin binding.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q53HG75EBI-4402639,EBI-7285164

    Protein-protein interaction databases

    BioGridi114493. 9 interactions.
    DIPiDIP-17042N.
    IntActiO75146. 4 interactions.
    MINTiMINT-2797489.
    STRINGi9606.ENSP00000253083.

    Structurei

    Secondary structure

    1
    1068
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi776 – 7783
    Helixi779 – 81133
    Helixi814 – 85239
    Helixi858 – 8647
    Helixi866 – 89530
    Helixi900 – 92223
    Turni929 – 9313
    Helixi932 – 96433

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R0DX-ray1.90A/B/D/E/F/G/H/I771-971[»]
    ProteinModelPortaliO75146.
    SMRiO75146. Positions 349-451, 461-559, 773-966.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75146.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 151129ENTHPROSITE-ProRule annotationAdd
    BLAST
    Domaini771 – 1012242I/LWEQPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni867 – 92458Important for actin bindingAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili347 – 599253Sequence AnalysisAdd
    BLAST

    Domaini

    Binds F-actin via the talin-like I/LWEQ domain.

    Sequence similaritiesi

    Belongs to the SLA2 family.Curated
    Contains 1 ENTH (epsin N-terminal homology) domain.PROSITE-ProRule annotation
    Contains 1 I/LWEQ domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG280957.
    HOGENOMiHOG000020612.
    HOVERGENiHBG005968.
    InParanoidiO75146.
    OMAiAFQMEQV.
    OrthoDBiEOG72JWFF.
    PhylomeDBiO75146.
    TreeFamiTF316860.

    Family and domain databases

    Gene3Di1.20.1410.10. 1 hit.
    1.25.40.90. 1 hit.
    InterProiIPR011417. ANTH_dom.
    IPR008942. ENTH_VHS.
    IPR013809. Epsin-like_N.
    IPR002558. ILWEQ_dom.
    [Graphical view]
    PfamiPF07651. ANTH. 1 hit.
    PF01608. I_LWEQ. 1 hit.
    [Graphical view]
    ProDomiPD011820. ILWEQ. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00273. ENTH. 1 hit.
    SM00307. ILWEQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF109885. SSF109885. 1 hit.
    SSF48464. SSF48464. 1 hit.
    PROSITEiPS50942. ENTH. 1 hit.
    PS50945. I_LWEQ. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75146-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNSIKNVPAR VLSRRPGHSL EAEREQFDKT QAISISKAIN TQEAPVKEKH     50
    ARRIILGTHH EKGAFTFWSY AIGLPLPSSS ILSWKFCHVL HKVLRDGHPN 100
    VLHDCQRYRS NIREIGDLWG HLHDRYGQLV NVYTKLLLTK ISFHLKHPQF 150
    PAGLEVTDEV LEKAAGTDVN NIFQLTVEMF DYMDCELKLS ESVFRQLNTA 200
    IAVSQMSSGQ CRLAPLIQVI QDCSHLYHYT VKLLFKLHSC LPADTLQGHR 250
    DRFHEQFHSL RNFFRRASDM LYFKRLIQIP RLPEGPPNFL RASALAEHIK 300
    PVVVIPEEAP EDEEPENLIE ISTGPPAGEP VVVADLFDQT FGPPNGSVKD 350
    DRDLQIESLK REVEMLRSEL EKIKLEAQRY IAQLKSQVNA LEGELEEQRK 400
    QKQKALVDNE QLRHELAQLR AAQLEGERSQ GLREEAERKA SATEARYNKL 450
    KEKHSELVHV HAELLRKNAD TAKQLTVTQQ SQEEVARVKE QLAFQVEQVK 500
    RESELKLEEK SDQLEKLKRE LEAKAGELAR AQEALSHTEQ SKSELSSRLD 550
    TLSAEKDALS GAVRQREADL LAAQSLVRET EAALSREQQR SSQEQGELQG 600
    RLAERESQEQ GLRQRLLDEQ FAVLRGAAAE AAGILQDAVS KLDDPLHLRC 650
    TSSPDYLVSR AQEALDAVST LEEGHAQYLT SLADASALVA ALTRFSHLAA 700
    DTIINGGATS HLAPTDPADR LIDTCRECGA RALELMGQLQ DQQALRHMQA 750
    SLVRTPLQGI LQLGQELKPK SLDVRQEELG AVVDKEMAAT SAAIEDAVRR 800
    IEDMMNQARH ASSGVKLEVN ERILNSCTDL MKAIRLLVTT STSLQKEIVE 850
    SGRGAATQQE FYAKNSRWTE GLISASKAVG WGATQLVEAA DKVVLHTGKY 900
    EELIVCSHEI AASTAQLVAA SKVKANKHSP HLSRLQECSR TVNERAANVV 950
    ASTKSGQEQI EDRDTMDFSG LSLIKLKKQE METQVRVLEL EKTLEAERMR 1000
    LGELRKQHYV LAGASGSPGE EVAIRPSTAP RSVTTKKPPL AQKPSVAPRQ 1050
    DHQLDKKDGI YPAQLVNY 1068
    Length:1,068
    Mass (Da):119,388
    Last modified:April 27, 2001 - v2
    Checksum:i3CBC7CF1191BFF8F
    GO
    Isoform 2 (identifier: O75146-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         606-615: ESQEQGLRQR → VWPPQMQQHH
         616-1068: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:615
    Mass (Da):70,288
    Checksum:i8C8EA2E9117EE27E
    GO

    Sequence cautioni

    The sequence BAA31630.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti345 – 3451N → S.1 Publication
    Corresponds to variant rs149504879 [ dbSNP | Ensembl ].
    VAR_070814
    Natural varianti404 – 4041K → Q.
    Corresponds to variant rs7972242 [ dbSNP | Ensembl ].
    VAR_051029
    Natural varianti516 – 5161K → Q.
    Corresponds to variant rs7972242 [ dbSNP | Ensembl ].
    VAR_051030
    Natural varianti782 – 7821V → M.
    Corresponds to variant rs2271051 [ dbSNP | Ensembl ].
    VAR_020043
    Natural varianti943 – 9431N → S.
    Corresponds to variant rs3736414 [ dbSNP | Ensembl ].
    VAR_051031

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei606 – 61510ESQEQGLRQR → VWPPQMQQHH in isoform 2. 1 PublicationVSP_054238
    Alternative sequencei616 – 1068453Missing in isoform 2. 1 PublicationVSP_054239Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014555 mRNA. Translation: BAA31630.1. Different initiation.
    AC027290 Genomic DNA. No translation available.
    BC067085 mRNA. Translation: AAH67085.1.
    AB013384 mRNA. Translation: BAA33713.1.
    CCDSiCCDS31922.1. [O75146-1]
    RefSeqiNP_003950.1. NM_003959.1. [O75146-1]
    UniGeneiHs.524815.
    Hs.714965.

    Genome annotation databases

    EnsembliENST00000253083; ENSP00000253083; ENSG00000130787. [O75146-1]
    GeneIDi9026.
    KEGGihsa:9026.
    UCSCiuc001udi.1. human. [O75146-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014555 mRNA. Translation: BAA31630.1 . Different initiation.
    AC027290 Genomic DNA. No translation available.
    BC067085 mRNA. Translation: AAH67085.1 .
    AB013384 mRNA. Translation: BAA33713.1 .
    CCDSi CCDS31922.1. [O75146-1 ]
    RefSeqi NP_003950.1. NM_003959.1. [O75146-1 ]
    UniGenei Hs.524815.
    Hs.714965.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R0D X-ray 1.90 A/B/D/E/F/G/H/I 771-971 [» ]
    ProteinModelPortali O75146.
    SMRi O75146. Positions 349-451, 461-559, 773-966.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114493. 9 interactions.
    DIPi DIP-17042N.
    IntActi O75146. 4 interactions.
    MINTi MINT-2797489.
    STRINGi 9606.ENSP00000253083.

    PTM databases

    PhosphoSitei O75146.

    Proteomic databases

    MaxQBi O75146.
    PaxDbi O75146.
    PRIDEi O75146.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253083 ; ENSP00000253083 ; ENSG00000130787 . [O75146-1 ]
    GeneIDi 9026.
    KEGGi hsa:9026.
    UCSCi uc001udi.1. human. [O75146-1 ]

    Organism-specific databases

    CTDi 9026.
    GeneCardsi GC12P123319.
    HGNCi HGNC:18415. HIP1R.
    HPAi CAB017187.
    HPA038135.
    HPA038136.
    MIMi 605613. gene.
    neXtProti NX_O75146.
    PharmGKBi PA128394543.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG280957.
    HOGENOMi HOG000020612.
    HOVERGENi HBG005968.
    InParanoidi O75146.
    OMAi AFQMEQV.
    OrthoDBi EOG72JWFF.
    PhylomeDBi O75146.
    TreeFami TF316860.

    Enzyme and pathway databases

    Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.

    Miscellaneous databases

    ChiTaRSi HIP1R. human.
    EvolutionaryTracei O75146.
    GeneWikii HIP1R.
    GenomeRNAii 9026.
    NextBioi 33819.
    PROi O75146.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75146.
    Bgeei O75146.
    CleanExi HS_HIP1R.
    Genevestigatori O75146.

    Family and domain databases

    Gene3Di 1.20.1410.10. 1 hit.
    1.25.40.90. 1 hit.
    InterProi IPR011417. ANTH_dom.
    IPR008942. ENTH_VHS.
    IPR013809. Epsin-like_N.
    IPR002558. ILWEQ_dom.
    [Graphical view ]
    Pfami PF07651. ANTH. 1 hit.
    PF01608. I_LWEQ. 1 hit.
    [Graphical view ]
    ProDomi PD011820. ILWEQ. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00273. ENTH. 1 hit.
    SM00307. ILWEQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF109885. SSF109885. 1 hit.
    SSF48464. SSF48464. 1 hit.
    PROSITEi PS50942. ENTH. 1 hit.
    PS50945. I_LWEQ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "HIP12 is a non-proapoptotic member of a gene family including HIP1, an interacting protein with huntingtin."
      Chopra V.S., Metzler M., Rasper D.M., Engqvist-Goldstein A.E.Y., Singaraja R., Gan L., Fichter K.M., McCutcheon K., Drubin D., Nicholson D.W., Hayden M.R.
      Mamm. Genome 11:1006-1015(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT SER-345.
      Tissue: Pancreas.
    5. "Cloning, expression analysis, and chromosomal localization of HIP1R, an isolog of huntingtin interacting protein (HIP1)."
      Seki N., Muramatsu M., Sugano S., Suzuki Y., Nakagawara A., Ohhira M., Hayashi A., Hori T., Saito T.
      J. Hum. Genet. 43:268-271(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 179-1068 (ISOFORM 1).
      Tissue: Neuroblastoma.
    6. "HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. Identification of a novel interaction with clathrin light chain."
      Legendre-Guillemin V., Metzler M., Charbonneau M., Gan L., Chopra V., Philie J., Hayden M.R., McPherson P.S.
      J. Biol. Chem. 277:19897-19904(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CLTB AND HIP1, SUBCELLULAR LOCATION.
    7. "HIP1 and HIP1r stabilize receptor tyrosine kinases and bind 3-phosphoinositides via epsin N-terminal homology domains."
      Hyun T.S., Rao D.S., Saint-Dic D., Michael L.E., Kumar P.D., Bradley S.V., Mizukami I.F., Oravecz-Wilson K.I., Ross T.S.
      J. Biol. Chem. 279:14294-14306(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R) bind the conserved sequence of clathrin light chains and thereby influence clathrin assembly in vitro and actin distribution in vivo."
      Chen C.-Y., Brodsky F.M.
      J. Biol. Chem. 280:6109-6117(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CLTB.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1017, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structural definition of the F-actin-binding THATCH domain from HIP1R."
      Brett T.J., Legendre-Guillemin V., McPherson P.S., Fremont D.H.
      Nat. Struct. Mol. Biol. 13:121-130(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 771-971, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, MUTAGENESIS OF ARG-867; GLY-871; ALA-875 AND 922-LYS--LYS-924.

    Entry informationi

    Entry nameiHIP1R_HUMAN
    AccessioniPrimary (citable) accession number: O75146
    Secondary accession number(s): A6NHQ6, Q6NXG8, Q9UED9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3