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Protein

Hepatocyte growth factor-regulated tyrosine kinase substrate

Gene

Hgs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri160 – 22061FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • protein domain specific binding Source: MGI
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Hepatocyte growth factor-regulated tyrosine kinase substrate
Gene namesi
Name:Hgs
Synonyms:Hrs
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:104681. Hgs.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice show a defect in ventral folding morphogenesis, exhibiting two bilateral heart tubes and absence of foregut, and died around embryonic day 11. Significantly enlarged endosomes were also detected in cells of the endoderm.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi183 – 1831R → A: 100-fold loss of affinity for PIP3 and accumulation in the cytosol. 1 Publication
Mutagenesisi215 – 2151C → S: Accumulation in proteinaceous aggregates devoid of membranes and no interaction with PI3P. 1 Publication
Mutagenesisi269 – 2691L → A: Loss of protein phosphorylation at Y-329 and Y-334; when associated with A-270. 1 Publication
Mutagenesisi270 – 2701S → A: Loss of protein phosphorylation at Y-329 and Y-334; when associated with A-269. 2 Publications
Mutagenesisi270 – 2701S → E: No interaction with ubiquitin. 2 Publications
Mutagenesisi329 – 3291Y → F: No change in the phosphorylation level. Loss of protein phosphorylation; when associated with F-334. 1 Publication
Mutagenesisi334 – 3341Y → F: No change in the phosphorylation level. Loss of protein phosphorylation; when associated with F-329. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 775775Hepatocyte growth factor-regulated tyrosine kinase substratePRO_0000098709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei207 – 2071N6-acetyllysineBy similarity
Modified residuei216 – 2161PhosphotyrosineCombined sources
Modified residuei308 – 3081PhosphotyrosineCombined sources
Modified residuei329 – 3291Phosphotyrosine1 Publication
Modified residuei334 – 3341Phosphotyrosine1 Publication
Modified residuei549 – 5491N6-succinyllysineCombined sources

Post-translational modificationi

Phosphorylated on Tyr-334. This phosphorylation occurs in response to EGF. A minor site of phosphorylation on Tyr-329 is detected. Protein phosphorylation may also be triggered in response to IL-2, GM-CSF and HGF.1 Publication
Ubiquitinated by ITCH.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ99LI8.
MaxQBiQ99LI8.
PaxDbiQ99LI8.
PRIDEiQ99LI8.

PTM databases

iPTMnetiQ99LI8.
PhosphoSiteiQ99LI8.

Expressioni

Tissue specificityi

Ubiquitous expression in adult and fetal tissues with higher expression in testis.2 Publications

Gene expression databases

BgeeiQ99LI8.
CleanExiMM_HGS.

Interactioni

Subunit structurei

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 (PubMed:10651905). 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 (PubMed:11094085). Interacts with TSG101; the interaction mediates the association with the ESCRT-I complex (PubMed:12802020). 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. Interacts with TRAK1 and TRAK2. Interacts with ARRDC3. Identified in a complex containing at least ARRDC4, V2R and HGS (By similarity). Interacts (via UIM domain) with UBQLN1 (via ubiquitin-like domain) (PubMed:16159959).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TSG101Q998163EBI-2119135,EBI-346882From a different organism.

GO - Molecular functioni

  • protein domain specific binding Source: MGI
  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi200296. 7 interactions.
DIPiDIP-29102N.
IntActiQ99LI8. 7 interactions.
MINTiMINT-267768.
STRINGi10090.ENSMUSP00000026900.

Structurei

3D structure databases

ProteinModelPortaliQ99LI8.
SMRiQ99LI8. Positions 6-221, 402-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 143129VHSPROSITE-ProRule annotationAdd
BLAST
Domaini258 – 27720UIMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni225 – 541317Interaction with SNX1By similarityAdd
BLAST
Regioni443 – 54199Interaction with SNAP25 and TRAK2By similarityAdd
BLAST
Regioni452 – 570119Interaction with STAM1 PublicationAdd
BLAST
Regioni478 – 775298Interaction with NF2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi503 – 55856Gln-richAdd
BLAST
Compositional biasi559 – 763205Pro-richAdd
BLAST

Domaini

Has a double-sided UIM that can bind 2 ubiquitin molecules, one on each side of the helix.By similarity
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 (By similarity).By similarity

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
Contains 1 UIM (ubiquitin-interacting motif) domain.PROSITE-ProRule annotation
Contains 1 VHS domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri160 – 22061FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1818. Eukaryota.
ENOG410XNRF. LUCA.
HOVERGENiHBG062917.
InParanoidiQ99LI8.
KOiK12182.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR008942. ENTH_VHS.
IPR024641. HRS_helical.
IPR017073. Ubi-bd_Hrs_VPS27.
IPR003903. UIM_dom.
IPR002014. VHS_dom.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF12210. Hrs_helical. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view]
PIRSFiPIRSF036956. Hrs_Vps27. 1 hit.
SMARTiSM00064. FYVE. 1 hit.
SM00288. VHS. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50330. UIM. 1 hit.
PS50179. VHS. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99LI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRGSGTFER LLDKATSQLL LETDWESILQ ICDLIRQGDT QAKYAVNSIK
60 70 80 90 100
KKVNDKNPHV ALYALEVMES VVKNCGQTVH DEVANKQTME ELKELLKRQV
110 120 130 140 150
EVNVRNKILY LIQAWAHAFR NEPKYKVVQD TYQIMKVEGH VFPEFKESDA
160 170 180 190 200
MFAAERAPDW VDAEECHRCR VQFGVVTRKH HCRACGQIFC GKCSSKYSTI
210 220 230 240 250
PKFGIEKEVR VCEPCYEQLN KKAEGKASST TELPPEYLTS PLSQQSQLPP
260 270 280 290 300
KRDETALQEE EELQLALALS QSEAEEKERM RQKTTYTAHP KAEPTPLASS
310 320 330 340 350
APPAGSLYSS PVNSSAPLAE DIDPELARYL NRNYWEKKQE EARKSPTPSA
360 370 380 390 400
PVPLTEPAAQ PGEGHTAPNS MAEAPLPETD SQPITPCSGP FSEYQNGESE
410 420 430 440 450
ESHEQFLKAL QNAVSTFVNR MKSNHMRGRS ITNDSAVLSL FQSINTMHPQ
460 470 480 490 500
LLELLNQLDE RRLYYEGLQD KLAQIRDARG ALSALREEHR EKLRRAAEEA
510 520 530 540 550
ERQRQIQLAQ KLEIMRQKKQ EYLEVQRQLA IQRLQEQEKE RQMRLEQQKQ
560 570 580 590 600
TVQMRAQMPA FPLPYAQLQA MPTAGGVLYQ PSGPTSFPAT FSPAGSVEGS
610 620 630 640 650
PMHGVYMSQP APATGPYPSM PGTTADPSMV SAYMYPTGAP GAQAAPQAQA
660 670 680 690 700
GPTTSPAYSS YQPTPTPGYQ SVASQAPQSL PAISQPPQTS NIGYMGSQPM
710 720 730 740 750
SMGYQPYNMQ NLMTALPGQD ASLPAQQPYI PGQQPLYQQM APSTGPPQQQ
760 770
PPVAQPAPTQ GPPAQGSEAQ LISFD
Length:775
Mass (Da):86,015
Last modified:July 19, 2005 - v2
Checksum:i0E68BF5AB514865B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231T → S in AAH03239 (PubMed:15489334).Curated
Sequence conflicti584 – 5841P → S in BAC32676 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50050 mRNA. Translation: BAA08768.1.
AK046299 mRNA. Translation: BAC32676.1.
BC003239 mRNA. Translation: AAH03239.1.
PIRiI49759.
RefSeqiNP_001152800.1. NM_001159328.1.
NP_032270.3. NM_008244.3.
UniGeneiMm.7919.

Genome annotation databases

GeneIDi15239.
KEGGimmu:15239.
UCSCiuc007msx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50050 mRNA. Translation: BAA08768.1.
AK046299 mRNA. Translation: BAC32676.1.
BC003239 mRNA. Translation: AAH03239.1.
PIRiI49759.
RefSeqiNP_001152800.1. NM_001159328.1.
NP_032270.3. NM_008244.3.
UniGeneiMm.7919.

3D structure databases

ProteinModelPortaliQ99LI8.
SMRiQ99LI8. Positions 6-221, 402-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200296. 7 interactions.
DIPiDIP-29102N.
IntActiQ99LI8. 7 interactions.
MINTiMINT-267768.
STRINGi10090.ENSMUSP00000026900.

PTM databases

iPTMnetiQ99LI8.
PhosphoSiteiQ99LI8.

Proteomic databases

EPDiQ99LI8.
MaxQBiQ99LI8.
PaxDbiQ99LI8.
PRIDEiQ99LI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi15239.
KEGGimmu:15239.
UCSCiuc007msx.2. mouse.

Organism-specific databases

CTDi9146.
MGIiMGI:104681. Hgs.

Phylogenomic databases

eggNOGiKOG1818. Eukaryota.
ENOG410XNRF. LUCA.
HOVERGENiHBG062917.
InParanoidiQ99LI8.
KOiK12182.

Miscellaneous databases

NextBioi287839.
PROiQ99LI8.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LI8.
CleanExiMM_HGS.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR008942. ENTH_VHS.
IPR024641. HRS_helical.
IPR017073. Ubi-bd_Hrs_VPS27.
IPR003903. UIM_dom.
IPR002014. VHS_dom.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF12210. Hrs_helical. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view]
PIRSFiPIRSF036956. Hrs_Vps27. 1 hit.
SMARTiSM00064. FYVE. 1 hit.
SM00288. VHS. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50330. UIM. 1 hit.
PS50179. VHS. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Growth factor-induced tyrosine phosphorylation of Hrs, a novel 115-kilodalton protein with a structurally-conserved putative zinc finger domain."
    Komada M., Kitamura N.
    Mol. Cell. Biol. 15:6213-6221(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "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: INTERACTION WITH STAM, DOMAIN.
  5. "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: TISSUE SPECIFICITY.
  6. "Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis."
    Komada M., Soriano P.
    Genes Dev. 13:1475-1485(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. "A hrs binding protein having a Src homology 3 domain is involved in intracellular degradation of growth factors and their receptors."
    Takata H., Kato M., Denda K., Kitamura N.
    Genes Cells 5:57-69(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STAM2, SUBCELLULAR LOCATION.
  8. "Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling through cooperation with SARA."
    Miura S., Takeshita T., Asao H., Kimura Y., Murata K., Sasaki Y., Hanai J., Beppu H., Tsukazaki T., Wrana J.L., Miyazono K., Sugamura K.
    Mol. Cell. Biol. 20:9346-9355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMAD1; SMAD2 AND SMAD3, DISRUPTION PHENOTYPE, FUNCTION.
  9. "FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes."
    Raiborg C., Bremnes B., Mehlum A., Gillooly D.J., D'Arrigo A., Stang E., Stenmark H.
    J. Cell Sci. 114:2255-2263(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-183 AND CYS-215, SUBCELLULAR LOCATION.
  10. "Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes."
    Raiborg C., Bache K.G., Gillooly D.J., Madshus I.H., Stang E., Stenmark H.
    Nat. Cell Biol. 4:394-398(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBIQUITIN, MUTAGENESIS OF SER-270.
  11. "The UIM domain of Hrs couples receptor sorting to vesicle formation."
    Urbe S., Sachse M., Row P.E., Preisinger C., Barr F.A., Strous G., Klumperman J., Clague M.J.
    J. Cell Sci. 116:4169-4179(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-329 AND TYR-334, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LEU-269; SER-270; TYR-329 AND TYR-334, SUBCELLULAR LOCATION.
  12. "TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation."
    Lu Q., Hope L.W., Brasch M., Reinhard C., Cohen S.N.
    Proc. Natl. Acad. Sci. U.S.A. 100:7626-7631(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TSG101.
  13. Cited for: INTERACTION WITH UBQLN1.
  14. "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].
  15. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  16. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  17. "Hybrid structural model of the complete human ESCRT-0 complex."
    Ren X., Kloer D.P., Kim Y.C., Ghirlando R., Saidi L.F., Hummer G., Hurley J.H.
    Structure 17:406-416(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STAM.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  19. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-549, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHGS_MOUSE
AccessioniPrimary (citable) accession number: Q99LI8
Secondary accession number(s): Q61691, Q8BQW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: May 11, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.