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Reviewed, UniProtKB/Swiss-Prot O00291 (HIP1_HUMAN)

Last modified November 3, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length1037 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.6 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17

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.6 Ref.10 Ref.13 Ref.17 Ref.3 Ref.5 Ref.16 Ref.18

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.10 Ref.12 Ref.13 Ref.17 Ref.11

Tissue specificity

Ubiquitously expressed with the highest level in brain. Expression is up-regulated in prostate and colon cancer. Ref.6 Ref.14 Ref.5

Domain

The pseudo DED region (pDED) mediates the interaction with IFT57. Ref.3

Binds F-actin via the talin-like I/LWEQ domain. Ref.3

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.

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
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processactivation of caspase activity Ref.3

Inferred from direct assay. Source: MGI

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin coat assembly Ref.12 Ref.13

Inferred from direct assay. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

induction of apoptosis Ref.8

Inferred from direct assay. Source: UniProtKB

positive regulation of receptor-mediated endocytosis Ref.10 Ref.12

Inferred from mutant phenotype. Source: UniProtKB

regulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentGolgi apparatus Ref.3

Inferred from direct assay. Source: MGI

clathrin coated vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton Ref.6

Traceable author statement. Source: ProtInc

membrane fraction Ref.6

Traceable author statement. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin binding Ref.12

Inferred from direct assay. Source: MGI

phosphoinositide binding Ref.15

Inferred from direct assay. Source: UniProtKB

structural constituent of cytoskeleton Ref.5

Traceable author statement. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [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.

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

Amino acid modifications

Modified residue1541Phosphothreonine By similarity

Natural variations

Natural variant2631M → K: dbSNP rs17149023.
VAR_051032

Experimental info

Mutagenesis561K → E: Abolishes 3-phosphoinositide-binding; when associated with GLU-58. Ref.17
Mutagenesis581K → E: Abolishes 3-phosphoinositide-binding; when associated with GLU-56. Ref.17
Mutagenesis4321F → G: Abolishes HIP1-induced cell death. Ref.8
Mutagenesis10051R → E: Reduces AR-induced nuclear translocation. Ref.17
Sequence conflict891A → P in AAC33564. Ref.3
Sequence conflict245 – 2517KLHSCLP → EFAAAST in CAA70574. Ref.6
Sequence conflict639 – 6446LNQLEE → STRPRI in CAA70574. Ref.6
Sequence conflict6881L → F in AAL87037. Ref.3

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). FASTA

References

« Hide 'large scale' references
[1]"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: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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: 11788820] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-1037, INTERACTION WITH IFT57, SUBUNIT, DOMAIN.
[4]"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.
[5]"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: 9140394] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-1037, INTERACTION WITH HTT, TISSUE SPECIFICITY.
[6]"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: 9147654] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-644, FUNCTION, INTERACTION WITH HTT, TISSUE SPECIFICITY.
Tissue: Brain.
[7]"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: 9616134] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION.
[8]"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: 11007801] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF PHE-432.
[9]"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: 11063258] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[10]"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: 11532990] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AP2A1; AP2A2 AND CLTC, SUBCELLULAR LOCATION.
[11]"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: 11517213] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"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: 11577110] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]"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: 11889126] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CLTB AND HIP1R, SUBCELLULAR LOCATION.
[14]"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: 12163454] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[15]"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: 14732715] [Abstract]
Cited for: FUNCTION.
[16]"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: 15533940] [Abstract]
Cited for: INTERACTION WITH CLTB.
[17]"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: 16027218] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AR, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-56; LYS-58 AND ARG-1005.
[18]"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: 18790740] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH F-ACTIN.
[19]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]"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: 17257618] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 474-579.
[21]"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: 18155047] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 362-474.
+Additional computationally mapped references.

Cross-references

Sequence databases

AC004491 Genomic DNA. No translation available.
AC018720 Genomic DNA. No translation available.
BC110545 mRNA. Translation: AAI10546.1.
AF365404 mRNA. Translation: AAL87037.1.
AF052288 expand/collapse EMBL AC list , AF052261, AF052262, AF052263, AF052264, AF052265, AF052266, AF052267, AF052268, AF052269, AF052270, AF052271, AF052272, AF052273, AF052274, AF052275, AF052276, AF052277, AF052278, AF052279, AF052280, AF052281, AF052282, AF052283, AF052284, AF052285, AF052286, AF052287 Genomic DNA. Translation: AAC33564.1.
U79734 mRNA. Translation: AAC51257.1. Different initiation.
Y09420 mRNA. Translation: CAA70574.1.
IPIIPI00782965.
RefSeqNP_005329.3.
UniGeneHs.329266
Hs.619089

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2NO2X-ray2.80A482-586[»]
2QA7X-ray2.80A/B/C/D370-481[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:17041N.
IntActO00291. 4 interactions.
STRINGO00291.

Proteomic databases

PRIDEO00291.

Genome annotation databases

EnsemblENST00000336926; ENSP00000336747; ENSG00000127946; Homo sapiens. [Genome view]
ENST00000404944; ENSP00000385314; ENSG00000127946; Homo sapiens. [Genome view]
ENST00000420909; ENSP00000414280; ENSG00000127946; Homo sapiens. [Genome view]
ENST00000434438; ENSP00000410300; ENSG00000127946; Homo sapiens. [Genome view]
GeneID3092.
KEGGhsa:3092.
UCSCuc003uds.1. human.

Organism-specific databases

CTD3092.
GeneCardsGC07M075001.
H-InvDBHIX0006779.
HGNCHGNC:4913. HIP1.
HPACAB015334.
CAB016402.
HPA013606.
HPA017964.
MIM601767. gene.
PharmGKBPA29289.
GenAtlasSearch...

Phylogenomic databases

HOVERGENO00291.
OMAKQELATS.

Enzyme and pathway databases

Pathway_Interaction_DBar_pathway. Coregulation of Androgen receptor activity.

Gene expression databases

ArrayExpressO00291.
BgeeO00291.
CleanExHS_HIP1.
GenevestigatorO00291.
GermOnlineENSG00000127946. Homo sapiens.

Family and domain databases

InterProIPR011417. ANTH.
IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR002558. ILWEQ.
[Graphical view]
Gene3DG3DSA:1.25.40.90. ENTH_VHS. 1 hit.
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]
PROSITEPS50942. ENTH. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameHIP1_HUMAN
AccessionPrimary (citable) accession number: O00291
Secondary accession number(s): O00328, Q2TB58, Q8TDL4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: September 23, 2008
Last modified: November 3, 2009
This is version 100 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 7

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents