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O00291 (HIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Huntingtin-interacting protein 1

Short name=HIP-1
Alternative name(s):
Huntingtin-interacting protein I
Short name=HIP-I
Gene names
Name:HIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1037 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18

Subunit structure

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. Ref.4 Ref.6 Ref.7 Ref.11 Ref.14 Ref.17 Ref.18 Ref.19

Subcellular location

Cytoplasm. Nucleus. Endomembrane system. Cytoplasmic vesicleclathrin-coated vesicle membrane. Note: Shuttles between cytoplasm and nucleus. Nuclear translocation can be induced by AR. Ref.11 Ref.12 Ref.13 Ref.14 Ref.18

Tissue specificity

Ubiquitously expressed with the highest level in brain. Expression is up-regulated in prostate and colon cancer. Ref.6 Ref.7 Ref.15

Domain

The pseudo DED region (pDED) mediates the interaction with IFT57. Ref.4

Binds F-actin via the talin-like I/LWEQ domain. Ref.4

Involvement in disease

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.

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.

Sequence similarities

Belongs to the SLA2 family.

Contains 1 ENTH (epsin N-terminal homology) domain.

Contains 1 I/LWEQ domain.

Sequence caution

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

Ontologies

Keywords
   Biological processApoptosis
Differentiation
Endocytosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Cytoplasmic vesicle
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseNeurodegeneration
   DomainCoiled coil
   LigandActin-binding
   Molecular functionActivator
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay Ref.4. Source: MGI

apoptotic process

Inferred from direct assay Ref.4. Source: MGI

apoptotic signaling pathway

Inferred from direct assay Ref.9. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin coat assembly

Inferred from direct assay Ref.14. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of receptor-mediated endocytosis

Inferred from mutant phenotype Ref.11Ref.13. Source: UniProtKB

regulation of apoptotic process

Inferred from direct assay Ref.4. Source: MGI

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.4. Source: MGI

clathrin-coated vesicle

Inferred from direct assay Ref.12. Source: UniProtKB

clathrin-coated vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 11604514. Source: MGI

cytoskeleton

Traceable author statement Ref.7. Source: ProtInc

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

membrane

Traceable author statement Ref.7. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionclathrin binding

Inferred from direct assay Ref.13. Source: MGI

phosphatidylinositol binding

Inferred from direct assay Ref.16. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.4Ref.14Ref.17Ref.18Ref.6. Source: UniProtKB

structural constituent of cytoskeleton

Traceable author statement Ref.6. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Apaf1Q9EPV52EBI-473886,EBI-6978501From a different organism.
HTTP428584EBI-473886,EBI-466029
Necap1Q9CR953EBI-473886,EBI-7592476From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform HIP1-1 (identifier: O00291-1)

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.
Isoform HIP1-2 (identifier: O00291-2)

The sequence of this isoform is not available.
Isoform 3 (identifier: O00291-3)

The sequence of this isoform differs from the canonical sequence as follows:
     803-853: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10371037Huntingtin-interacting protein 1
PRO_0000083986

Regions

Domain32 – 160129ENTH
Domain771 – 1012242I/LWEQ
Region410 – 49182pDED
Region867 – 92458Important for actin binding By similarity
Coiled coil368 – 644277 Potential

Natural variations

Alternative sequence803 – 85351Missing in isoform 3.
VSP_044736
Natural variant2631M → K.
Corresponds to variant rs17149023 [ dbSNP | Ensembl ].
VAR_051032

Experimental info

Mutagenesis561K → E: Abolishes 3-phosphoinositide-binding; when associated with E-58. Ref.18
Mutagenesis581K → E: Abolishes 3-phosphoinositide-binding; when associated with E-56. Ref.18
Mutagenesis4321F → G: Abolishes HIP1-induced cell death. Ref.9
Mutagenesis10051R → E: Reduces AR-induced nuclear translocation. Ref.18
Sequence conflict891A → P in AAC33564. Ref.4
Sequence conflict245 – 2517KLHSCLP → EFAAAST in CAA70574. Ref.7
Sequence conflict3571S → R in BAG65499. Ref.1
Sequence conflict639 – 6446LNQLEE → STRPRI in CAA70574. Ref.7
Sequence conflict6881L → F in AAL87037. Ref.4

Secondary structure

........ 1037
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform HIP1-1 [UniParc].

Last modified September 23, 2008. Version 5.
Checksum: F8C0369DBF0A836F

FASTA1,037116,221
        10         20         30         40         50         60 
MDRMASSMKQ VPNPLPKVLS RRGVGAGLEA AERESFERTQ TVSINKAINT QEVAVKEKHA 

        70         80         90        100        110        120 
RTCILGTHHE KGAQTFWSVV NRLPLSSNAV LCWKFCHVFH KLLRDGHPNV LKDSLRYRNE 

       130        140        150        160        170        180 
LSDMSRMWGH LSEGYGQLCS IYLKLLRTKM EYHTKNPRFP GNLQMSDRQL DEAGESDVNN 

       190        200        210        220        230        240 
FFQLTVEMFD YLECELNLFQ TVFNSLDMSR SVSVTAAGQC RLAPLIQVIL DCSHLYDYTV 

       250        260        270        280        290        300 
KLLFKLHSCL PADTLQGHRD RFMEQFTKLK DLFYRSSNLQ YFKRLIQIPQ LPENPPNFLR 

       310        320        330        340        350        360 
ASALSEHISP VVVIPAEASS PDSEPVLEKD DLMDMDASQQ NLFDNKFDDI FGSSFSSDPF 

       370        380        390        400        410        420 
NFNSQNGVNK DEKDHLIERL YREISGLKAQ LENMKTESQR VVLQLKGHVS ELEADLAEQQ 

       430        440        450        460        470        480 
HLRQQAADDC EFLRAELDEL RRQREDTEKA QRSLSEIERK AQANEQRYSK LKEKYSELVQ 

       490        500        510        520        530        540 
NHADLLRKNA EVTKQVSMAR QAQVDLEREK KELEDSLERI SDQGQRKTQE QLEVLESLKQ 

       550        560        570        580        590        600 
ELATSQRELQ VLQGSLETSA QSEANWAAEF AELEKERDSL VSGAAHREEE LSALRKELQD 

       610        620        630        640        650        660 
TQLKLASTEE SMCQLAKDQR KMLLVGSRKA AEQVIQDALN QLEEPPLISC AGSADHLLST 

       670        680        690        700        710        720 
VTSISSCIEQ LEKSWSQYLA CPEDISGLLH SITLLAHLTS DAIAHGATTC LRAPPEPADS 

       730        740        750        760        770        780 
LTEACKQYGR ETLAYLASLE EEGSLENADS TAMRNCLSKI KAIGEELLPR GLDIKQEELG 

       790        800        810        820        830        840 
DLVDKEMAAT SAAIETATAR IEEMLSKSRA GDTGVKLEVN ERILGCCTSL MQAIQVLIVA 

       850        860        870        880        890        900 
SKDLQREIVE SGRGTASPKE FYAKNSRWTE GLISASKAVG WGATVMVDAA DLVVQGRGKF 

       910        920        930        940        950        960 
EELMVCSHEI AASTAQLVAA SKVKADKDSP NLAQLQQASR GVNQATAGVV ASTISGKSQI 

       970        980        990       1000       1010       1020 
EETDNMDFSS MTLTQIKRQE MDSQVRVLEL ENELQKERQK LGELRKKHYE LAGVAEGWEE 

      1030 
GTEASPPTLQ EVVTEKE 

« Hide

Isoform HIP1-2 (Sequence not available).
Isoform 3 [UniParc].

Checksum: C09BAD680242941A
Show »

FASTA986110,663

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Huntingtin interacting protein 1 induces apoptosis via a novel caspase-dependent death effector domain."
Hackam A.S., Yassa A.S., Singaraja R., Metzler M., Gutekunst C.-A., Gan L., Warby S., Wellington C.L., Vaillancourt J., Chen N., Gervais F.G., Raymond L., Nicholson D.W., Hayden M.R.
J. Biol. Chem. 275:41299-41308(2000) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34669.1. [O00291-1]
CCDS59060.1. [O00291-3]
RefSeqNP_001230127.1. NM_001243198.2. [O00291-3]
NP_005329.3. NM_005338.6. [O00291-1]
UniGeneHs.329266.
Hs.619089.
Hs.674397.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NO2X-ray2.80A482-586[»]
2QA7X-ray2.80A/B/C/D370-481[»]
3I00X-ray2.30A/B361-480[»]
ProteinModelPortalO00291.
SMRO00291. Positions 371-472, 481-581, 773-966.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109339. 15 interactions.
DIPDIP-17041N.
IntActO00291. 11 interactions.
MINTMINT-208214.
STRING9606.ENSP00000336747.

PTM databases

PhosphoSiteO00291.

Proteomic databases

MaxQBO00291.
PaxDbO00291.
PRIDEO00291.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336926; ENSP00000336747; ENSG00000127946. [O00291-1]
ENST00000434438; ENSP00000410300; ENSG00000127946. [O00291-3]
ENST00000575057; ENSP00000460815; ENSG00000263334. [O00291-1]
ENST00000576304; ENSP00000459517; ENSG00000263334. [O00291-3]
GeneID3092.
KEGGhsa:3092.
UCSCuc003uds.2. human. [O00291-1]

Organism-specific databases

CTD3092.
GeneCardsGC07M075162.
HGNCHGNC:4913. HIP1.
HPACAB015334.
CAB016402.
HPA013606.
HPA017964.
MIM601767. gene.
neXtProtNX_O00291.
PharmGKBPA29289.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG280957.
HOGENOMHOG000020612.
HOVERGENHBG005968.
InParanoidO00291.
KOK04559.
OMAGRGKFEE.
PhylomeDBO00291.
TreeFamTF316860.

Gene expression databases

ArrayExpressO00291.
BgeeO00291.
CleanExHS_HIP1.
GenevestigatorO00291.

Family and domain databases

Gene3D1.20.1410.10. 1 hit.
1.25.40.90. 1 hit.
InterProIPR011417. ANTH_dom.
IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR002558. ILWEQ_dom.
[Graphical view]
PfamPF07651. ANTH. 1 hit.
PF01608. I_LWEQ. 1 hit.
[Graphical view]
ProDomPD011820. ILWEQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00273. ENTH. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view]
SUPFAMSSF109885. SSF109885. 1 hit.
SSF48464. SSF48464. 1 hit.
PROSITEPS50942. ENTH. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHip1. human.
EvolutionaryTraceO00291.
GenomeRNAi3092.
NextBio12271.
PROO00291.
SOURCESearch...

Entry information

Entry nameHIP1_HUMAN
AccessionPrimary (citable) accession number: O00291
Secondary accession number(s): B4E3I7 expand/collapse secondary AC list , E7ES17, O00328, Q2TB58, Q8TDL4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 148 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM