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O75146

- HIP1R_HUMAN

UniProt

O75146 - HIP1R_HUMAN

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Protein

Huntingtin-interacting protein 1-related protein

Gene
HIP1R, HIP12, KIAA0655
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

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

GO - Biological processi

  1. receptor-mediated endocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:18415. HIP1R.

Subcellular locationi

Cytoplasmperinuclear region. Endomembrane system. Cytoplasmic vesicleclathrin-coated vesicle membrane
Note: Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region.2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

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

Organism-specific databases

PharmGKBiPA128394543.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO75146.
PaxDbiO75146.
PRIDEiO75146.

PTM databases

PhosphoSiteiO75146.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiO75146.
BgeeiO75146.
CleanExiHS_HIP1R.
GenevestigatoriO75146.

Organism-specific databases

HPAiCAB017187.
HPA038135.
HPA038136.

Interactioni

Subunit structurei

Interacts with actin. Does not interact with huntingtin By similarity. Interacts with CLTB and HIP1. Homodimer. Homodimerization promotes actin binding.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO75146.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 151129ENTHAdd
BLAST
Domaini771 – 1012242I/LWEQAdd
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili347 – 599253 Reviewed predictionAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the SLA2 family.
Contains 1 I/LWEQ domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

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

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

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

« Hide

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

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

Note: No experimental confirmation available.

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

Sequence cautioni

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

Natural variant

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei606 – 61510ESQEQGLRQR → VWPPQMQQHH in isoform 2. VSP_054238
Alternative sequencei616 – 1068453Missing in isoform 2. VSP_054239Add
BLAST

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSitei O75146.

Proteomic databases

MaxQBi O75146.
PaxDbi O75146.
PRIDEi O75146.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

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

Enzyme and pathway databases

Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

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

Publicationsi

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

Entry informationi

Entry nameiHIP1R_HUMAN
AccessioniPrimary (citable) accession number: O75146
Secondary accession number(s): A6NHQ6, Q6NXG8, Q9UED9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: September 3, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3

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