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O00291

- HIP1_HUMAN

UniProt

O00291 - HIP1_HUMAN

Protein

Huntingtin-interacting protein 1

Gene

HIP1

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 149 (01 Oct 2014)
      Sequence version 5 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    Plays a role in clathrin-mediated endocytosis and trafficking. Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner. Enhances androgen receptor (AR)-mediated transcription. May act as a proapoptotic protein that induces cell death by acting through the intrinsic apoptosis pathway. 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. May play a functional role in the cell filament networks. May be required for differentiation, proliferation, and/or survival of somatic and germline progenitors.8 Publications

    GO - Molecular functioni

    1. clathrin binding Source: MGI
    2. phosphatidylinositol binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. structural constituent of cytoskeleton Source: ProtInc

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    2. apoptotic process Source: MGI
    3. apoptotic signaling pathway Source: UniProtKB
    4. cell differentiation Source: UniProtKB-KW
    5. clathrin coat assembly Source: UniProtKB
    6. endocytosis Source: UniProtKB-KW
    7. positive regulation of receptor-mediated endocytosis Source: UniProtKB
    8. regulation of apoptotic process Source: MGI
    9. regulation of transcription, DNA-templated Source: UniProtKB-KW
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Apoptosis, Differentiation, Endocytosis, Transcription, Transcription regulation

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Huntingtin-interacting protein 1
    Short name:
    HIP-1
    Alternative name(s):
    Huntingtin-interacting protein I
    Short name:
    HIP-I
    Gene namesi
    Name:HIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:4913. HIP1.

    Subcellular locationi

    Cytoplasm. Nucleus. Endomembrane system. Cytoplasmic vesicleclathrin-coated vesicle membrane
    Note: Shuttles between cytoplasm and nucleus. Nuclear translocation can be induced by AR.

    GO - Cellular componenti

    1. clathrin-coated vesicle Source: UniProtKB
    2. clathrin-coated vesicle membrane Source: UniProtKB-SubCell
    3. cytoplasm Source: MGI
    4. cytoskeleton Source: ProtInc
    5. Golgi apparatus Source: MGI
    6. intracellular membrane-bounded organelle Source: HPA
    7. membrane Source: ProtInc
    8. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving HIP1 is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5;7)(q33;q11.2) with PDGFRB. The chimeric HIP1-PDGFRB transcript results from an in-frame fusion of the two genes. The reciprocal PDGFRB-HIP1 transcript is not expressed.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi56 – 561K → E: Abolishes 3-phosphoinositide-binding; when associated with E-58. 1 Publication
    Mutagenesisi58 – 581K → E: Abolishes 3-phosphoinositide-binding; when associated with E-56. 1 Publication
    Mutagenesisi432 – 4321F → G: Abolishes HIP1-induced cell death. 1 Publication
    Mutagenesisi1005 – 10051R → E: Reduces AR-induced nuclear translocation. 1 Publication

    Keywords - Diseasei

    Neurodegeneration

    Organism-specific databases

    PharmGKBiPA29289.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10371037Huntingtin-interacting protein 1PRO_0000083986Add
    BLAST

    Proteomic databases

    MaxQBiO00291.
    PaxDbiO00291.
    PRIDEiO00291.

    PTM databases

    PhosphoSiteiO00291.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with the highest level in brain. Expression is up-regulated in prostate and colon cancer.3 Publications

    Gene expression databases

    ArrayExpressiO00291.
    BgeeiO00291.
    CleanExiHS_HIP1.
    GenevestigatoriO00291.

    Organism-specific databases

    HPAiCAB015334.
    CAB016402.
    HPA013606.
    HPA017964.

    Interactioni

    Subunit structurei

    Homodimer. Binds actin. Binds HTT (via N-terminus). This interaction is restricted to the brain. Binds to IFT57. In normal conditions, it poorly interacts with IFT57, HIP1 being strongly associated with HTT. However, in mutant HTT proteins with a long poly-Gln region, interaction between HTT and HIP1 is inhibited, promoting the interaction between HIP1 and IFT57. Interacts with CLTB (via N-terminus). Interacts (via coiled coil domain) with AR. Interacts with AP2A1, AP2A2, CLTC and HIP1R. Interacts with GRIA1, GRIN2A AND GRIN2B.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Apaf1Q9EPV52EBI-473886,EBI-6978501From a different organism.
    HTTP428584EBI-473886,EBI-466029
    Necap1Q9CR953EBI-473886,EBI-7592476From a different organism.

    Protein-protein interaction databases

    BioGridi109339. 15 interactions.
    DIPiDIP-17041N.
    IntActiO00291. 12 interactions.
    MINTiMINT-208214.
    STRINGi9606.ENSP00000336747.

    Structurei

    Secondary structure

    1
    1037
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi373 – 44169
    Turni459 – 4613
    Helixi462 – 4654
    Helixi482 – 58099

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NO2X-ray2.80A482-586[»]
    2QA7X-ray2.80A/B/C/D370-481[»]
    3I00X-ray2.30A/B361-480[»]
    ProteinModelPortaliO00291.
    SMRiO00291. Positions 371-472, 481-581, 773-966.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00291.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 160129ENTHPROSITE-ProRule annotationAdd
    BLAST
    Domaini771 – 1012242I/LWEQPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni410 – 49182pDEDAdd
    BLAST
    Regioni867 – 92458Important for actin bindingBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili368 – 644277Sequence AnalysisAdd
    BLAST

    Domaini

    The pseudo DED region (pDED) mediates the interaction with IFT57.1 Publication
    Binds F-actin via the talin-like I/LWEQ domain.1 Publication

    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.
    InParanoidiO00291.
    KOiK04559.
    OMAiGRGKFEE.
    PhylomeDBiO00291.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform HIP1-1 (identifier: O00291-1) [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

    MDRMASSMKQ VPNPLPKVLS RRGVGAGLEA AERESFERTQ TVSINKAINT     50
    QEVAVKEKHA RTCILGTHHE KGAQTFWSVV NRLPLSSNAV LCWKFCHVFH 100
    KLLRDGHPNV LKDSLRYRNE LSDMSRMWGH LSEGYGQLCS IYLKLLRTKM 150
    EYHTKNPRFP GNLQMSDRQL DEAGESDVNN FFQLTVEMFD YLECELNLFQ 200
    TVFNSLDMSR SVSVTAAGQC RLAPLIQVIL DCSHLYDYTV KLLFKLHSCL 250
    PADTLQGHRD RFMEQFTKLK DLFYRSSNLQ YFKRLIQIPQ LPENPPNFLR 300
    ASALSEHISP VVVIPAEASS PDSEPVLEKD DLMDMDASQQ NLFDNKFDDI 350
    FGSSFSSDPF NFNSQNGVNK DEKDHLIERL YREISGLKAQ LENMKTESQR 400
    VVLQLKGHVS ELEADLAEQQ HLRQQAADDC EFLRAELDEL RRQREDTEKA 450
    QRSLSEIERK AQANEQRYSK LKEKYSELVQ NHADLLRKNA EVTKQVSMAR 500
    QAQVDLEREK KELEDSLERI SDQGQRKTQE QLEVLESLKQ ELATSQRELQ 550
    VLQGSLETSA QSEANWAAEF AELEKERDSL VSGAAHREEE LSALRKELQD 600
    TQLKLASTEE SMCQLAKDQR KMLLVGSRKA AEQVIQDALN QLEEPPLISC 650
    AGSADHLLST VTSISSCIEQ LEKSWSQYLA CPEDISGLLH SITLLAHLTS 700
    DAIAHGATTC LRAPPEPADS LTEACKQYGR ETLAYLASLE EEGSLENADS 750
    TAMRNCLSKI KAIGEELLPR GLDIKQEELG DLVDKEMAAT SAAIETATAR 800
    IEEMLSKSRA GDTGVKLEVN ERILGCCTSL MQAIQVLIVA SKDLQREIVE 850
    SGRGTASPKE FYAKNSRWTE GLISASKAVG WGATVMVDAA DLVVQGRGKF 900
    EELMVCSHEI AASTAQLVAA SKVKADKDSP NLAQLQQASR GVNQATAGVV 950
    ASTISGKSQI EETDNMDFSS MTLTQIKRQE MDSQVRVLEL ENELQKERQK 1000
    LGELRKKHYE LAGVAEGWEE GTEASPPTLQ EVVTEKE 1037
    Length:1,037
    Mass (Da):116,221
    Last modified:September 23, 2008 - v5
    Checksum:iF8C0369DBF0A836F
    GO
    Isoform HIP1-2 (identifier: O00291-2)

    Sequence is not available
    Length:
    Mass (Da):
    Isoform 3 (identifier: O00291-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         803-853: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:986
    Mass (Da):110,663
    Checksum:iC09BAD680242941A
    GO

    Sequence cautioni

    The sequence AAC51257.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891A → P in AAC33564. (PubMed:11788820)Curated
    Sequence conflicti245 – 2517KLHSCLP → EFAAAST in CAA70574. (PubMed:9147654)Curated
    Sequence conflicti357 – 3571S → R in BAG65499. (PubMed:14702039)Curated
    Sequence conflicti639 – 6446LNQLEE → STRPRI in CAA70574. (PubMed:9147654)Curated
    Sequence conflicti688 – 6881L → F in AAL87037. (PubMed:11788820)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti263 – 2631M → K.
    Corresponds to variant rs17149023 [ dbSNP | Ensembl ].
    VAR_051032

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei803 – 85351Missing in isoform 3. 1 PublicationVSP_044736Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK304738 mRNA. Translation: BAG65499.1.
    AC004491 Genomic DNA. No translation available.
    AC018720 Genomic DNA. No translation available.
    BC110545 mRNA. Translation: AAI10546.1.
    AF365404 mRNA. Translation: AAL87037.1.
    AH006397 Genomic DNA. Translation: AAC33564.1.
    U79734 mRNA. Translation: AAC51257.1. Different initiation.
    Y09420 mRNA. Translation: CAA70574.1.
    CCDSiCCDS34669.1. [O00291-1]
    CCDS59060.1. [O00291-3]
    RefSeqiNP_001230127.1. NM_001243198.2. [O00291-3]
    NP_005329.3. NM_005338.6. [O00291-1]
    UniGeneiHs.329266.
    Hs.619089.
    Hs.674397.

    Genome annotation databases

    EnsembliENST00000336926; ENSP00000336747; ENSG00000127946. [O00291-1]
    ENST00000434438; ENSP00000410300; ENSG00000127946. [O00291-3]
    GeneIDi3092.
    KEGGihsa:3092.
    UCSCiuc003uds.2. human. [O00291-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK304738 mRNA. Translation: BAG65499.1 .
    AC004491 Genomic DNA. No translation available.
    AC018720 Genomic DNA. No translation available.
    BC110545 mRNA. Translation: AAI10546.1 .
    AF365404 mRNA. Translation: AAL87037.1 .
    AH006397 Genomic DNA. Translation: AAC33564.1 .
    U79734 mRNA. Translation: AAC51257.1 . Different initiation.
    Y09420 mRNA. Translation: CAA70574.1 .
    CCDSi CCDS34669.1. [O00291-1 ]
    CCDS59060.1. [O00291-3 ]
    RefSeqi NP_001230127.1. NM_001243198.2. [O00291-3 ]
    NP_005329.3. NM_005338.6. [O00291-1 ]
    UniGenei Hs.329266.
    Hs.619089.
    Hs.674397.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NO2 X-ray 2.80 A 482-586 [» ]
    2QA7 X-ray 2.80 A/B/C/D 370-481 [» ]
    3I00 X-ray 2.30 A/B 361-480 [» ]
    ProteinModelPortali O00291.
    SMRi O00291. Positions 371-472, 481-581, 773-966.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109339. 15 interactions.
    DIPi DIP-17041N.
    IntActi O00291. 12 interactions.
    MINTi MINT-208214.
    STRINGi 9606.ENSP00000336747.

    PTM databases

    PhosphoSitei O00291.

    Proteomic databases

    MaxQBi O00291.
    PaxDbi O00291.
    PRIDEi O00291.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336926 ; ENSP00000336747 ; ENSG00000127946 . [O00291-1 ]
    ENST00000434438 ; ENSP00000410300 ; ENSG00000127946 . [O00291-3 ]
    GeneIDi 3092.
    KEGGi hsa:3092.
    UCSCi uc003uds.2. human. [O00291-1 ]

    Organism-specific databases

    CTDi 3092.
    GeneCardsi GC07M075162.
    HGNCi HGNC:4913. HIP1.
    HPAi CAB015334.
    CAB016402.
    HPA013606.
    HPA017964.
    MIMi 601767. gene.
    neXtProti NX_O00291.
    PharmGKBi PA29289.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG280957.
    HOGENOMi HOG000020612.
    HOVERGENi HBG005968.
    InParanoidi O00291.
    KOi K04559.
    OMAi GRGKFEE.
    PhylomeDBi O00291.
    TreeFami TF316860.

    Miscellaneous databases

    ChiTaRSi Hip1. human.
    EvolutionaryTracei O00291.
    GenomeRNAii 3092.
    NextBioi 12271.
    PROi O00291.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00291.
    Bgeei O00291.
    CleanExi HS_HIP1.
    Genevestigatori O00291.

    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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Uterus.
    2. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
    4. "Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi."
      Gervais F.G., Singaraja R., Xanthoudakis S., Gutekunst C.-A., Leavitt B.R., Metzler M., Hackam A.S., Tam J., Vaillancourt J.P., Houtzager V., Rasper D.M., Roy S., Hayden M.R., Nicholson D.W.
      Nat. Cell Biol. 4:95-105(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-1037, INTERACTION WITH IFT57, SUBUNIT, DOMAIN.
    5. "Genomic organization of the human HIP1 gene and its exclusion as a candidate gene in a family diagnosed with Huntington disease without CAG expansion."
      Huq A.H.M.M., Nichol K., Osborne L., Scherer S.W., Squitieri F., Hayden M.R.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-1037.
    6. "HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain."
      Kalchman M.A., Koide H.B., McCutcheon K., Graham R.K., Nichol K., Nishiyama K., Kazemi-Esfarjani P., Lynn F.C., Wellington C., Metzler M., Goldberg Y.P., Kanazawa I., Geitz R.D., Hayden M.R.
      Nat. Genet. 16:44-53(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-1037, INTERACTION WITH HTT, TISSUE SPECIFICITY.
    7. "HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system."
      Wanker E.E., Rovira C., Scherzinger E., Hasenbank R., Waelter S., Tait D., Colicelli J., Lehrach H.
      Hum. Mol. Genet. 6:487-495(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-644, FUNCTION, INTERACTION WITH HTT, TISSUE SPECIFICITY.
      Tissue: Brain.
    8. "Fusion of Huntingtin interacting protein 1 to platelet-derived growth factor beta receptor (PDGFbetaR) in chronic myelomonocytic leukemia with t(5;7)(q33;q11.2)."
      Ross T.S., Bernard O.A., Berger R., Gilliland D.G.
      Blood 91:4419-4426(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION.
    9. Cited for: FUNCTION, MUTAGENESIS OF PHE-432.
    10. "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: ALTERNATIVE SPLICING.
    11. "The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis."
      Waelter S., Scherzinger E., Hasenbank R., Nordhoff E., Lurz R., Goehler H., Gauss C., Sathasivam K., Bates G.P., Lehrach H., Wanker E.E.
      Hum. Mol. Genet. 10:1807-1817(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AP2A1; AP2A2 AND CLTC, SUBCELLULAR LOCATION.
    12. "HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2."
      Metzler M., Legendre-Guillemin V., Gan L., Chopra V., Kwok A., McPherson P.S., Hayden M.R.
      J. Biol. Chem. 276:39271-39276(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins."
      Mishra S.K., Agostinelli N.R., Brett T.J., Mizukami I., Ross T.S., Traub L.M.
      J. Biol. Chem. 276:46230-46236(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. "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 HIP1R, SUBCELLULAR LOCATION.
    15. "Huntingtin-interacting protein 1 is overexpressed in prostate and colon cancer and is critical for cellular survival."
      Rao D.S., Hyun T.S., Kumar P.D., Mizukami I.F., Rubin M.A., Lucas P.C., Sanda M.G., Ross T.S.
      J. Clin. Invest. 110:351-360(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    16. "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.
    17. "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.
    18. "Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors."
      Mills I.G., Gaughan L., Robson C., Ross T., McCracken S., Kelly J., Neal D.E.
      J. Cell Biol. 170:191-200(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AR, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-56; LYS-58 AND ARG-1005.
    19. "Actin binding by Hip1 (huntingtin-interacting protein 1) and Hip1R (Hip1-related protein) is regulated by clathrin light chain."
      Wilbur J.D., Chen C.-Y., Manalo V., Hwang P.K., Fletterick R.J., Brodsky F.M.
      J. Biol. Chem. 283:32870-32879(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH F-ACTIN.
    20. "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.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Crystal structure at 2.8 A of the DLLRKN-containing coiled-coil domain of huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding."
      Ybe J.A., Mishra S., Helms S., Nix J.
      J. Mol. Biol. 367:8-15(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 474-579.
    23. "Crystal structure at 2.8 A of Huntingtin-interacting protein 1 (HIP1) coiled-coil domain reveals a charged surface suitable for HIP1 protein interactor (HIPPI)."
      Niu Q., Ybe J.A.
      J. Mol. Biol. 375:1197-1205(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 362-474.

    Entry informationi

    Entry nameiHIP1_HUMAN
    AccessioniPrimary (citable) accession number: O00291
    Secondary accession number(s): B4E3I7
    , E7ES17, O00328, Q2TB58, Q8TDL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 149 of the entry and version 5 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

    Miscellaneous

    The affinity of the huntingtin protein-HIP1 interaction is inversely correlated to the length of the polyglutamine tract added to the huntingtin protein in Huntington disease.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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