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O14964 (HGS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 132. 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:
Hepatocyte growth factor-regulated tyrosine kinase substrate
Alternative name(s):
Hrs
Protein pp110
Gene names
Name:HGS
Synonyms:HRS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length777 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation.

Subunit structure

Interacts with TRAK1. Interacts with TRAK2 By similarity. Interacts with TRAK1. Component of the ESCRT-0 complex composed of STAM or STAM2 and HGS. Part of a complex at least composed of HSG, STAM2 (or probably STAM) and EPS15. Interacts with STAM. Interacts with STAM2. Interacts with EPS15; the interaction is direct, calcium-dependent and inhibited by SNAP25. Interacts with NF2; the interaction is direct. Interacts with ubiquitin; the interaction is direct. Interacts with VPS37C. Interacts with SMAD1, SMAD2 and SMAD3. Interacts with TSG101; the interaction mediates the association with the ESCRT-I complex. Interacts with SNAP25; the interaction is direct and decreases with addition of increasing concentrations of free calcium. Interacts with SNX1; the interaction is direct. Component of a 550 kDa membrane complex at least composed of HGS and SNX1 but excluding EGFR. Component of the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and TRIM3. Ref.1 Ref.3 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14

Subcellular location

Cytoplasm. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Endosomemultivesicular body membrane; Peripheral membrane protein By similarity Ref.3 Ref.6.

Tissue specificity

Ubiquitous expression in adult and fetal tissues with higher expression in testis and peripheral blood leukocytes. Ref.1 Ref.2

Domain

Has a double-sided UIM that can bind 2 ubiquitin molecules, one on each side of the helix. Ref.3 Ref.17

The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate in membranes of early endosomes and penetrates bilayers. The FYVE domain insertion into PtdIns3P-enriched membranes is substantially increased in acidic conditions. Ref.3 Ref.17

Post-translational modification

Phosphorylated on Tyr-334. A minor site of phosphorylation on Tyr-329 is detected By similarity. Phosphorylation occurs in response to EGF, IL-2, GM-CSF and HGF.

Ubiquitinated by ITCH. Ref.7

Sequence similarities

Contains 1 FYVE-type zinc finger.

Contains 1 UIM (ubiquitin-interacting motif) repeat.

Contains 1 VHS domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Endosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendosomal transport

Non-traceable author statement Ref.3. Source: UniProtKB

endosome to lysosome transport

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

negative regulation of JAK-STAT cascade

Inferred from direct assay PubMed 12444102. Source: HGNC

negative regulation of cell proliferation

Traceable author statement Ref.1. Source: ProtInc

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

regulation of protein catabolic process

Traceable author statement PubMed 15611048. Source: HGNC

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

early endosome

Inferred from direct assay Ref.3. Source: HGNC

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

multivesicular body membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

secretory granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

sh3rf1Q6NRD33EBI-740220,EBI-7734031From a different organism.
UBBP0CG537EBI-740220,EBI-5333021From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14964-1)

Also known as: HRSi1;

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: O14964-2)

Also known as: HRSi2;

The sequence of this isoform differs from the canonical sequence as follows:
     518-604: Missing.
Note: Dubious isoform produced through aberrant splice sites.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 777777Hepatocyte growth factor-regulated tyrosine kinase substrate
PRO_0000098708

Regions

Domain15 – 143129VHS
Repeat258 – 27720UIM
Zinc finger160 – 22061FYVE-type
Region225 – 543319Interaction with SNX1 By similarity
Region445 – 54399Interaction with SNAP25 and TRAK2 By similarity
Region454 – 572119Interaction with STAM1 By similarity
Region480 – 777298Interaction with NF2
Compositional bias346 – 39449Pro-rich
Compositional bias505 – 772268Gln-rich

Amino acid modifications

Modified residue2071N6-acetyllysine Ref.18
Modified residue2161Phosphotyrosine Ref.11
Modified residue3081Phosphotyrosine By similarity
Modified residue3291Phosphotyrosine By similarity
Modified residue3341Phosphotyrosine By similarity
Modified residue5511N6-succinyllysine By similarity

Natural variations

Alternative sequence518 – 60487Missing in isoform 2.
VSP_036172
Natural variant71T → S. Ref.22
VAR_054154
Natural variant4001E → D.
Corresponds to variant rs34868130 [ dbSNP | Ensembl ].
VAR_052981
Natural variant7331A → S.
Corresponds to variant rs56058441 [ dbSNP | Ensembl ].
VAR_061991

Experimental info

Mutagenesis2661A → Q: Strongly reduced ubiquitin-binding. Reduced degradation of ubiquitinated EGFR. Ref.21
Mutagenesis2681A → Q: Strongly reduced ubiquitin-binding. Reduced degradation of ubiquitinated EGFR. Ref.21
Sequence conflict2361E → D in AAF82361. Ref.3

Secondary structure

.......................................... 777
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HRSi1) [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DD64167A19DCF030

FASTA77786,192
        10         20         30         40         50         60 
MGRGSGTFER LLDKATSQLL LETDWESILQ ICDLIRQGDT QAKYAVNSIK KKVNDKNPHV 

        70         80         90        100        110        120 
ALYALEVMES VVKNCGQTVH DEVANKQTME ELKDLLKRQV EVNVRNKILY LIQAWAHAFR 

       130        140        150        160        170        180 
NEPKYKVVQD TYQIMKVEGH VFPEFKESDA MFAAERAPDW VDAEECHRCR VQFGVMTRKH 

       190        200        210        220        230        240 
HCRACGQIFC GKCSSKYSTI PKFGIEKEVR VCEPCYEQLN RKAEGKATST TELPPEYLTS 

       250        260        270        280        290        300 
PLSQQSQLPP KRDETALQEE EELQLALALS QSEAEEKERL RQKSTYTSYP KAEPMPSASS 

       310        320        330        340        350        360 
APPASSLYSS PVNSSAPLAE DIDPELARYL NRNYWEKKQE EARKSPTPSA PVPLTEPAAQ 

       370        380        390        400        410        420 
PGEGHAAPTN VVENPLPETD SQPIPPSGGP FSEPQFHNGE SEESHEQFLK ALQNAVTTFV 

       430        440        450        460        470        480 
NRMKSNHMRG RSITNDSAVL SLFQSINGMH PQLLELLNQL DERRLYYEGL QDKLAQIRDA 

       490        500        510        520        530        540 
RGALSALREE HREKLRRAAE EAERQRQIQL AQKLEIMRQK KQEYLEVQRQ LAIQRLQEQE 

       550        560        570        580        590        600 
KERQMRLEQQ KQTVQMRAQM PAFPLPYAQL QAMPAAGGVL YQPSGPASFP STFSPAGSVE 

       610        620        630        640        650        660 
GSPMHGVYMS QPAPAAGPYP SMPSTAADPS MVSAYMYPAG ATGAQAAPQA QAGPTASPAY 

       670        680        690        700        710        720 
SSYQPTPTAG YQNVASQAPQ SLPAISQPPQ SSTMGYMGSQ SVSMGYQPYN MQNLMTTLPS 

       730        740        750        760        770 
QDASLPPQQP YIAGQQPMYQ QMAPSGGPPQ QQPPVAQQPQ AQGPPAQGSE AQLISFD 

« Hide

Isoform 2 (HRSi2) [UniParc].

Checksum: 9266F872DB03A3E6
Show »

FASTA69076,376

References

« Hide 'large scale' references
[1]"Hrs is associated with STAM, a signal-transducing adaptor molecule. Its suppressive effect on cytokine-induced cell growth."
Asao H., Sasaki Y., Arita T., Tanaka N., Endo K., Kasai H., Takeshita T., Endo Y., Fujita T., Sugamura K.
J. Biol. Chem. 272:32785-32791(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH STAM.
[2]"Human Hrs, a tyrosine kinase substrate in growth factor-stimulated cells: cDNA cloning and mapping of the gene to chromosome 17."
Lu L., Komada M., Kitamura N.
Gene 213:125-132(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Placenta.
[3]"The neurofibromatosis 2 tumor suppressor protein interacts with hepatocyte growth factor-regulated tyrosine kinase substrate."
Scoles D.R., Huynh D.P., Chen M.S., Burke S.P., Gutmann D.H., Pulst S.-M.
Hum. Mol. Genet. 9:1567-1574(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DOMAIN, INTERACTION WITH NF2, SUBCELLULAR LOCATION.
Tissue: Brain.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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 1).
Tissue: Skin.
[6]"Hrs, a tyrosine kinase substrate with a conserved double zinc finger domain, is localized to the cytoplasmic surface of early endosomes."
Komada M., Masaki R., Yamamoto A., Kitamura N.
J. Biol. Chem. 272:20538-20544(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4."
Marchese A., Raiborg C., Santini F., Keen J.H., Stenmark H., Benovic J.L.
Dev. Cell 5:709-722(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY ITCH.
[8]"STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes."
Bache K.G., Raiborg C., Mehlum A., Stenmark H.
J. Biol. Chem. 278:12513-12521(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STAM; STAM2 AND EPS15, IDENTIFICATION IN A COMPLEX WITH STAM2 AND EPS15.
[9]"HIV Gag mimics the Tsg101-recruiting activity of the human Hrs protein."
Pornillos O., Higginson D.S., Stray K.M., Fisher R.D., Garrus J.E., Payne M., He G.P., Wang H.E., Morham S.G., Sundquist W.I.
J. Cell Biol. 162:425-434(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 GAG AND HGS, SELF-ASSOCIATION.
[10]"Identification of human VPS37C, a component of endosomal sorting complex required for transport-I important for viral budding."
Eastman S.W., Martin-Serrano J., Chung W., Zang T., Bieniasz P.D.
J. Biol. Chem. 280:628-636(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VPS37C.
[11]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Hypertonia-associated protein Trak1 is a novel regulator of endosome-to-lysosome trafficking."
Webber E., Li L., Chin L.S.
J. Mol. Biol. 382:638-651(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAK1.
[14]"CART: an Hrs/actinin-4/BERP/myosin V protein complex required for efficient receptor recycling."
Yan Q., Sun W., Kujala P., Lotfi Y., Vida T.A., Bean A.J.
Mol. Biol. Cell 16:2470-2482(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CART COMPLEX.
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Membrane insertion of the FYVE domain is modulated by pH."
He J., Vora M., Haney R.M., Filonov G.S., Musselman C.A., Burd C.G., Kutateladze A.G., Verkhusha V.V., Stahelin R.V., Kutateladze T.G.
Proteins 76:852-860(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN FYVE-TYPE ZINC-FINGER.
[18]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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.
[20]"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].
[21]"Double-sided ubiquitin binding of Hrs-UIM in endosomal protein sorting."
Hirano S., Kawasaki M., Ura H., Kato R., Raiborg C., Stenmark H., Wakatsuki S.
Nat. Struct. Mol. Biol. 13:272-277(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 257-277 IN COMPLEX WITH UBIQUITIN, MUTAGENESIS OF ALA-266 AND ALA-268.
[22]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-7.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43895 mRNA. Translation: AAC51929.1.
D84064 mRNA. Translation: BAA23366.1.
AF260566 mRNA. Translation: AAF82361.1.
BT009754 mRNA. Translation: AAP88756.1.
BC003565 mRNA. Translation: AAH03565.1.
RefSeqNP_004703.1. NM_004712.4.
UniGeneHs.661056.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D3GX-ray1.70P257-277[»]
3F1IX-ray2.30H404-501[»]
3OBQX-ray1.40B346-354[»]
3ZYQX-ray1.48A1-225[»]
4AVXX-ray1.68A1-225[»]
ProteinModelPortalO14964.
SMRO14964. Positions 6-221, 404-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114593. 151 interactions.
DIPDIP-29050N.
IntActO14964. 49 interactions.
MINTMINT-234372.
STRING9606.ENSP00000331201.

PTM databases

PhosphoSiteO14964.

Proteomic databases

PaxDbO14964.
PeptideAtlasO14964.
PRIDEO14964.

Protocols and materials databases

DNASU9146.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329138; ENSP00000331201; ENSG00000185359. [O14964-1]
GeneID9146.
KEGGhsa:9146.
UCSCuc002kbg.3. human. [O14964-1]

Organism-specific databases

CTD9146.
GeneCardsGC17P079651.
HGNCHGNC:4897. HGS.
HPAHPA004872.
HPA007728.
MIM604375. gene.
neXtProtNX_O14964.
PharmGKBPA29271.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG257212.
HOGENOMHOG000044175.
HOVERGENHBG062917.
InParanoidO14964.
KOK12182.
OMAERMRQKS.
OrthoDBEOG7N37CN.
PhylomeDBO14964.
TreeFamTF314470.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
REACT_116125. Disease.
SignaLinkO14964.

Gene expression databases

ArrayExpressO14964.
BgeeO14964.
CleanExHS_HGS.
GenevestigatorO14964.

Family and domain databases

Gene3D1.25.40.90. 1 hit.
3.30.40.10. 1 hit.
InterProIPR008942. ENTH_VHS.
IPR027426. HGS.
IPR024641. HRS_helical.
IPR017073. Ubi-bd_Hrs_VPS27.
IPR003903. Ubiquitin-int_motif.
IPR002014. VHS.
IPR018205. VHS_subgr.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR13856:SF45. PTHR13856:SF45. 1 hit.
PfamPF01363. FYVE. 1 hit.
PF12210. Hrs_helical. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view]
PIRSFPIRSF036956. Hrs_Vps27. 1 hit.
SMARTSM00064. FYVE. 1 hit.
SM00726. UIM. 1 hit.
SM00288. VHS. 1 hit.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS50330. UIM. 1 hit.
PS50179. VHS. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHGS. human.
EvolutionaryTraceO14964.
GeneWikiHGS_(gene).
GenomeRNAi9146.
NextBio34307.
PROO14964.
SOURCESearch...

Entry information

Entry nameHGS_HUMAN
AccessionPrimary (citable) accession number: O14964
Secondary accession number(s): Q9NR36
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 1, 1998
Last modified: March 19, 2014
This is version 132 of the entry and version 1 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 17

Human chromosome 17: entries, gene names and cross-references to MIM