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Protein

Protein SGT1 homolog

Gene

SUGT1

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

Functioni

May play a role in ubiquitination and subsequent proteasomal degradation of target proteins.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_75808. The NLRP3 inflammasome.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SGT1 homologBy similarity
Alternative name(s):
Protein 40-6-3Imported
Sgt11 Publication
Suppressor of G2 allele of SKP1 homologBy similarity
Gene namesi
Name:SUGT1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:16987. SUGT1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • kinetochore Source: ProtInc
  • nucleus Source: HPA
  • ubiquitin ligase complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134880121.

Polymorphism and mutation databases

BioMutaiSUGT1.
DMDMi62512186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed6 Publications
Chaini2 – 365364Protein SGT1 homologPRO_0000106332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei265 – 2651Phosphothreonine1 Publication
Modified residuei281 – 2811Phosphoserine1 Publication
Modified residuei331 – 3311Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated at Ser-281 and Ser-331, dephosphorylation promotes nuclear translocation, most likely due to disruption of the SUGT1-HSP90 complex.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y2Z0.
PaxDbiQ9Y2Z0.
PRIDEiQ9Y2Z0.

PTM databases

PhosphoSiteiQ9Y2Z0.

Expressioni

Gene expression databases

BgeeiQ9Y2Z0.
CleanExiHS_SUGT1.
GenevisibleiQ9Y2Z0. HS.

Organism-specific databases

HPAiCAB015942.
HPA043949.

Interactioni

Subunit structurei

Probably associates with SCF (SKP1-CUL1-F-box protein) complex through interaction with SKP1. Interacts with S100A6. Interacts with HSP90.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-10768076,EBI-352572
LRCH4O754272EBI-307008,EBI-718707
SKP1P632082EBI-10768076,EBI-307486

Protein-protein interaction databases

BioGridi116115. 70 interactions.
DIPiDIP-53799N.
IntActiQ9Y2Z0. 29 interactions.
MINTiMINT-5005759.
STRINGi9606.ENSP00000367208.

Structurei

Secondary structure

1
365
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi174 – 1785Combined sources
Beta strandi180 – 1878Combined sources
Helixi194 – 1963Combined sources
Beta strandi197 – 2004Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi206 – 2116Combined sources
Beta strandi215 – 2228Combined sources
Beta strandi224 – 2263Combined sources
Helixi230 – 2323Combined sources
Beta strandi233 – 2375Combined sources
Beta strandi239 – 2479Combined sources
Beta strandi255 – 2584Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RL1NMR-A167-276[»]
ProteinModelPortaliQ9Y2Z0.
SMRiQ9Y2Z0. Positions 30-111, 170-261.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y2Z0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati11 – 4434TPR 1Add
BLAST
Repeati45 – 7834TPR 2Add
BLAST
Repeati79 – 11234TPR 3Add
BLAST
Domaini169 – 25890CSPROSITE-ProRule annotationAdd
BLAST
Domaini276 – 36590SGSPROSITE-ProRule annotationAdd
BLAST

Domaini

The CS domain mediates interaction with HSP90.

Sequence similaritiesi

Belongs to the SGT1 family.Curated
Contains 1 CS domain.PROSITE-ProRule annotation
Contains 1 SGS domain.PROSITE-ProRule annotation
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00390000013700.
HOGENOMiHOG000248210.
HOVERGENiHBG055080.
InParanoidiQ9Y2Z0.
KOiK12795.
OMAiMAKNVPK.
OrthoDBiEOG7WX0B4.
PhylomeDBiQ9Y2Z0.
TreeFamiTF105979.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007699. SGS.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF04969. CS. 1 hit.
PF05002. SGS. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
PS51048. SGS. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y2Z0-1) [UniParc]FASTAAdd to basket

Also known as: SGT1B1 Publication

, SUGT1B1 Publication, SGT1.21 Publication

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

        10         20         30         40         50
MAAAAAGTAT SQRFFQSFSD ALIDEDPQAA LEELTKALEQ KPDDAQYYCQ
60 70 80 90 100
RAYCHILLGN YCVAVADAKK SLELNPNNST AMLRKGICEY HEKNYAAALE
110 120 130 140 150
TFTEGQKLDI ETGFHRVGQA GLQLLTSSDP PALDSQSAGI TGADANFSVW
160 170 180 190 200
IKRCQEAQNG SESEVWTHQS KIKYDWYQTE SQVVITLMIK NVQKNDVNVE
210 220 230 240 250
FSEKELSALV KLPSGEDYNL KLELLHPIIP EQSTFKVLST KIEIKLKKPE
260 270 280 290 300
AVRWEKLEGQ GDVPTPKQFV ADVKNLYPSS SPYTRNWDKL VGEIKEEEKN
310 320 330 340 350
EKLEGDAALN RLFQQIYSDG SDEVKRAMNK SFMESGGTVL STNWSDVGKR
360
KVEINPPDDM EWKKY
Length:365
Mass (Da):41,024
Last modified:January 23, 2007 - v3
Checksum:i4A5A413E70561D9A
GO
Isoform 2 (identifier: Q9Y2Z0-2) [UniParc]FASTAAdd to basket

Also known as: SGT1A, SUGT1A1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     110-142: IETGFHRVGQAGLQLLTSSDPPALDSQSAGITG → S

Show »
Length:333
Mass (Da):37,805
Checksum:i14DE069A1623DB53
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201A → V in AAQ01749 (PubMed:15346769).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei110 – 14233IETGF…AGITG → S in isoform 2. 4 PublicationsVSP_013420Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132856 mRNA. Translation: AAD30062.1.
AJ344097 mRNA. Translation: CAC51433.1.
AY321358 mRNA. Translation: AAQ76039.1.
AY271314 mRNA. Translation: AAQ01749.1.
BT009798 mRNA. Translation: AAP88800.1.
AL139089 Genomic DNA. Translation: CAI17072.1.
AL139089 Genomic DNA. Translation: CAM23909.1.
CH471124 Genomic DNA. Translation: EAW52045.1.
BC000911 mRNA. Translation: AAH00911.1.
CCDSiCCDS45050.1. [Q9Y2Z0-1]
CCDS9436.1. [Q9Y2Z0-2]
RefSeqiNP_001124384.1. NM_001130912.1. [Q9Y2Z0-1]
NP_006695.1. NM_006704.3. [Q9Y2Z0-2]
UniGeneiHs.281902.

Genome annotation databases

EnsembliENST00000310528; ENSP00000308067; ENSG00000165416. [Q9Y2Z0-2]
ENST00000343788; ENSP00000367208; ENSG00000165416.
GeneIDi10910.
KEGGihsa:10910.
UCSCiuc001vhb.2. human. [Q9Y2Z0-2]
uc001vhc.2. human. [Q9Y2Z0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132856 mRNA. Translation: AAD30062.1.
AJ344097 mRNA. Translation: CAC51433.1.
AY321358 mRNA. Translation: AAQ76039.1.
AY271314 mRNA. Translation: AAQ01749.1.
BT009798 mRNA. Translation: AAP88800.1.
AL139089 Genomic DNA. Translation: CAI17072.1.
AL139089 Genomic DNA. Translation: CAM23909.1.
CH471124 Genomic DNA. Translation: EAW52045.1.
BC000911 mRNA. Translation: AAH00911.1.
CCDSiCCDS45050.1. [Q9Y2Z0-1]
CCDS9436.1. [Q9Y2Z0-2]
RefSeqiNP_001124384.1. NM_001130912.1. [Q9Y2Z0-1]
NP_006695.1. NM_006704.3. [Q9Y2Z0-2]
UniGeneiHs.281902.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RL1NMR-A167-276[»]
ProteinModelPortaliQ9Y2Z0.
SMRiQ9Y2Z0. Positions 30-111, 170-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116115. 70 interactions.
DIPiDIP-53799N.
IntActiQ9Y2Z0. 29 interactions.
MINTiMINT-5005759.
STRINGi9606.ENSP00000367208.

PTM databases

PhosphoSiteiQ9Y2Z0.

Polymorphism and mutation databases

BioMutaiSUGT1.
DMDMi62512186.

Proteomic databases

MaxQBiQ9Y2Z0.
PaxDbiQ9Y2Z0.
PRIDEiQ9Y2Z0.

Protocols and materials databases

DNASUi10910.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310528; ENSP00000308067; ENSG00000165416. [Q9Y2Z0-2]
ENST00000343788; ENSP00000367208; ENSG00000165416.
GeneIDi10910.
KEGGihsa:10910.
UCSCiuc001vhb.2. human. [Q9Y2Z0-2]
uc001vhc.2. human. [Q9Y2Z0-1]

Organism-specific databases

CTDi10910.
GeneCardsiGC13P053226.
H-InvDBHIX0026254.
HIX0201992.
HGNCiHGNC:16987. SUGT1.
HPAiCAB015942.
HPA043949.
MIMi604098. gene.
neXtProtiNX_Q9Y2Z0.
PharmGKBiPA134880121.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00390000013700.
HOGENOMiHOG000248210.
HOVERGENiHBG055080.
InParanoidiQ9Y2Z0.
KOiK12795.
OMAiMAKNVPK.
OrthoDBiEOG7WX0B4.
PhylomeDBiQ9Y2Z0.
TreeFamiTF105979.

Enzyme and pathway databases

ReactomeiREACT_75808. The NLRP3 inflammasome.

Miscellaneous databases

ChiTaRSiSUGT1. human.
EvolutionaryTraceiQ9Y2Z0.
GeneWikiiSUGT1.
GenomeRNAii10910.
NextBioi41435.
PROiQ9Y2Z0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2Z0.
CleanExiHS_SUGT1.
GenevisibleiQ9Y2Z0. HS.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007699. SGS.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF04969. CS. 1 hit.
PF05002. SGS. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
PS51048. SGS. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex."
    Kitagawa K., Skowyra D., Elledge S.J., Harper J.W., Hieter P.
    Mol. Cell 4:21-33(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBUNIT.
  2. "Identification of a novel splice variant: human SGT1B (SUGT1B)."
    Niikura Y., Kitagawa K.
    DNA Seq. 14:436-441(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Molecular cloning and characterization of SGT1.2, a novel splice variant of Homo sapiens SGT1."
    Zou X., Ji C., Wang L., Wu M., Zheng H., Xu J., Jin F., Gu S., Ying K., Xie Y., Mao Y.
    DNA Seq. 15:140-143(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. Schmidt T.
    Thesis (2001), University of Goettingen, Germany
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  5. "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 2).
  6. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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).
    Tissue: Cervix.
  9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Tissue: Platelet.
  10. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 195-204; 222-236 AND 312-326, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hepatoma.
  11. "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins."
    Nowotny M., Spiechowicz M., Jastrzebska B., Filipek A., Kitagawa K., Kuznicki J.
    J. Biol. Chem. 278:26923-26928(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH S100A6.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265 AND SER-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Nuclear translocation of Sgt1 depends on its phosphorylation state."
    Prus W., Zabka M., Bieganowski P., Filipek A.
    Int. J. Biochem. Cell Biol. 43:1747-1753(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-281 AND SER-331, SUBCELLULAR LOCATION, INTERACTION WITH S100A6.
  18. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain."
    Lee Y.-T., Jacob J., Michowski W., Nowotny M., Kuznicki J., Chazin W.J.
    J. Biol. Chem. 279:16511-16517(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 167-276, INTERACTION WITH HSP90.

Entry informationi

Entry nameiSGT1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2Z0
Secondary accession number(s): A2A303
, Q5JAK5, Q5TAM6, Q6VXY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 145 of the entry and version 3 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 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.