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O75146 (HIP1R_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Huntingtin-interacting protein 1-related protein

Short name=HIP1-related protein
Alternative name(s):
Huntingtin-interacting protein 12
Short name=HIP-12
Gene names
Name:HIP1R
Synonyms:HIP12, KIAA0655
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1068 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7

Subunit structure

Interacts with actin. Does not interact with huntingtin By similarity. Interacts with CLTB and HIP1. Homodimer. Homodimerization promotes actin binding. Ref.6 Ref.8 Ref.13

Subcellular location

Cytoplasmperinuclear region. Endomembrane system. Cytoplasmic vesicleclathrin-coated vesicle membrane. Note: Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region. Ref.6 Ref.7

Tissue specificity

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

Domain

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

Sequence similarities

Belongs to the SLA2 family.

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

Contains 1 I/LWEQ domain.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q53HG75EBI-4402639,EBI-7285164

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75146-1)

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 2 (identifier: O75146-2)

The sequence of this isoform differs from the canonical sequence as follows:
     606-615: ESQEQGLRQR → VWPPQMQQHH
     616-1068: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10681068Huntingtin-interacting protein 1-related protein
PRO_0000083984

Regions

Domain23 – 151129ENTH
Domain771 – 1012242I/LWEQ
Region867 – 92458Important for actin binding
Coiled coil347 – 599253 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12
Modified residue10171Phosphoserine Ref.9

Natural variations

Alternative sequence606 – 61510ESQEQGLRQR → VWPPQMQQHH in isoform 2.
VSP_054238
Alternative sequence616 – 1068453Missing in isoform 2.
VSP_054239
Natural variant3451N → S. Ref.4
Corresponds to variant rs149504879 [ dbSNP | Ensembl ].
VAR_070814
Natural variant4041K → Q.
Corresponds to variant rs7972242 [ dbSNP | Ensembl ].
VAR_051029
Natural variant5161K → Q.
Corresponds to variant rs7972242 [ dbSNP | Ensembl ].
VAR_051030
Natural variant7821V → M.
Corresponds to variant rs2271051 [ dbSNP | Ensembl ].
VAR_020043
Natural variant9431N → S.
Corresponds to variant rs3736414 [ dbSNP | Ensembl ].
VAR_051031

Experimental info

Mutagenesis8671R → D: Reduced acting binding. Ref.13
Mutagenesis8711G → D: Reduced acting binding. Ref.13
Mutagenesis8751A → D: Reduced acting binding. Ref.13
Mutagenesis922 – 9243KVK → DDD: Strongly reduced actin binding. Ref.13

Secondary structure

............... 1068
Helix Strand Turn

Details...

Sequences

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

Last modified April 27, 2001. Version 2.
Checksum: 3CBC7CF1191BFF8F

FASTA1,068119,388
        10         20         30         40         50         60 
MNSIKNVPAR VLSRRPGHSL EAEREQFDKT QAISISKAIN TQEAPVKEKH ARRIILGTHH 

        70         80         90        100        110        120 
EKGAFTFWSY AIGLPLPSSS ILSWKFCHVL HKVLRDGHPN VLHDCQRYRS NIREIGDLWG 

       130        140        150        160        170        180 
HLHDRYGQLV NVYTKLLLTK ISFHLKHPQF PAGLEVTDEV LEKAAGTDVN NIFQLTVEMF 

       190        200        210        220        230        240 
DYMDCELKLS ESVFRQLNTA IAVSQMSSGQ CRLAPLIQVI QDCSHLYHYT VKLLFKLHSC 

       250        260        270        280        290        300 
LPADTLQGHR DRFHEQFHSL RNFFRRASDM LYFKRLIQIP RLPEGPPNFL RASALAEHIK 

       310        320        330        340        350        360 
PVVVIPEEAP EDEEPENLIE ISTGPPAGEP VVVADLFDQT FGPPNGSVKD DRDLQIESLK 

       370        380        390        400        410        420 
REVEMLRSEL EKIKLEAQRY IAQLKSQVNA LEGELEEQRK QKQKALVDNE QLRHELAQLR 

       430        440        450        460        470        480 
AAQLEGERSQ GLREEAERKA SATEARYNKL KEKHSELVHV HAELLRKNAD TAKQLTVTQQ 

       490        500        510        520        530        540 
SQEEVARVKE QLAFQVEQVK RESELKLEEK SDQLEKLKRE LEAKAGELAR AQEALSHTEQ 

       550        560        570        580        590        600 
SKSELSSRLD TLSAEKDALS GAVRQREADL LAAQSLVRET EAALSREQQR SSQEQGELQG 

       610        620        630        640        650        660 
RLAERESQEQ GLRQRLLDEQ FAVLRGAAAE AAGILQDAVS KLDDPLHLRC TSSPDYLVSR 

       670        680        690        700        710        720 
AQEALDAVST LEEGHAQYLT SLADASALVA ALTRFSHLAA DTIINGGATS HLAPTDPADR 

       730        740        750        760        770        780 
LIDTCRECGA RALELMGQLQ DQQALRHMQA SLVRTPLQGI LQLGQELKPK SLDVRQEELG 

       790        800        810        820        830        840 
AVVDKEMAAT SAAIEDAVRR IEDMMNQARH ASSGVKLEVN ERILNSCTDL MKAIRLLVTT 

       850        860        870        880        890        900 
STSLQKEIVE SGRGAATQQE FYAKNSRWTE GLISASKAVG WGATQLVEAA DKVVLHTGKY 

       910        920        930        940        950        960 
EELIVCSHEI AASTAQLVAA SKVKANKHSP HLSRLQECSR TVNERAANVV ASTKSGQEQI 

       970        980        990       1000       1010       1020 
EDRDTMDFSG LSLIKLKKQE METQVRVLEL EKTLEAERMR LGELRKQHYV LAGASGSPGE 

      1030       1040       1050       1060 
EVAIRPSTAP RSVTTKKPPL AQKPSVAPRQ DHQLDKKDGI YPAQLVNY 

« Hide

Isoform 2 [UniParc].

Checksum: 8C8EA2E9117EE27E
Show »

FASTA61570,288

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"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].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB014555 mRNA. Translation: BAA31630.1. Different initiation.
AC027290 Genomic DNA. No translation available.
BC067085 mRNA. Translation: AAH67085.1.
AB013384 mRNA. Translation: BAA33713.1.
RefSeqNP_003950.1. NM_003959.1.
UniGeneHs.524815.
Hs.714965.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R0DX-ray1.90A/B/D/E/F/G/H/I771-971[»]
ProteinModelPortalO75146.
SMRO75146. Positions 349-451, 461-559, 773-966.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114493. 9 interactions.
DIPDIP-17042N.
IntActO75146. 4 interactions.
MINTMINT-2797489.
STRING9606.ENSP00000253083.

PTM databases

PhosphoSiteO75146.

Proteomic databases

PaxDbO75146.
PRIDEO75146.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253083; ENSP00000253083; ENSG00000130787.
GeneID9026.
KEGGhsa:9026.
UCSCuc001udi.1. human.

Organism-specific databases

CTD9026.
GeneCardsGC12P123319.
HGNCHGNC:18415. HIP1R.
HPACAB017187.
HPA038135.
HPA038136.
MIM605613. gene.
neXtProtNX_O75146.
PharmGKBPA128394543.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG280957.
HOGENOMHOG000020612.
HOVERGENHBG005968.
InParanoidO75146.
OMAVNTWRSK.
OrthoDBEOG72JWFF.
PhylomeDBO75146.
TreeFamTF316860.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressO75146.
BgeeO75146.
CleanExHS_HIP1R.
GenevestigatorO75146.

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

ChiTaRSHIP1R. human.
EvolutionaryTraceO75146.
GeneWikiHIP1R.
GenomeRNAi9026.
NextBio33819.
PROO75146.
SOURCESearch...

Entry information

Entry nameHIP1R_HUMAN
AccessionPrimary (citable) accession number: O75146
Secondary accession number(s): A6NHQ6, Q6NXG8, Q9UED9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: April 16, 2014
This is version 124 of the entry and version 2 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 12

Human chromosome 12: entries, gene names and cross-references to MIM