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Q9Y2Z0 (SUGT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Suppressor of G2 allele of SKP1 homolog
Alternative name(s):
Protein 40-6-3
Sgt1
Gene names
Name:SUGT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Probably associates with SCF (SKP1-CUL1-F-box protein) complex through interaction with SKP1. Interacts with S100A6. Interacts with HSP90. Ref.1 Ref.11 Ref.17 Ref.20

Subcellular location

Cytoplasm. Nucleus. Note: Translocates to the nucleus upon heat shock, requiring S100A6. Ref.17

Domain

The CS domain mediates interaction with HSP90.

Post-translational modification

Phosphorylated at Ser-281 and Ser-331, dephosphorylation promotes nuclear translocation, most likely due to disruption of the SUGT1-HSP90 complex. Ref.17

Sequence similarities

Belongs to the SUGT1 family.

Contains 1 CS domain.

Contains 1 SGS domain.

Contains 3 TPR repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRCH4O754272EBI-307008,EBI-718707

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2Z0-1)

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: Q9Y2Z0-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9 Ref.10
Chain2 – 365364Suppressor of G2 allele of SKP1 homolog
PRO_0000106332

Regions

Repeat11 – 4434TPR 1
Repeat45 – 7834TPR 2
Repeat79 – 11234TPR 3
Domain169 – 25890CS
Domain276 – 36590SGS

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.14 Ref.15 Ref.18 Ref.19
Modified residue2651Phosphothreonine Ref.15
Modified residue2811Phosphoserine Ref.17
Modified residue3311Phosphoserine Ref.15 Ref.17

Natural variations

Alternative sequence110 – 14233IETGF…AGITG → S in isoform 2.
VSP_013420

Experimental info

Sequence conflict1201A → V in AAQ01749. Ref.4

Secondary structure

....................... 365
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 4A5A413E70561D9A

FASTA36541,024
        10         20         30         40         50         60 
MAAAAAGTAT SQRFFQSFSD ALIDEDPQAA LEELTKALEQ KPDDAQYYCQ RAYCHILLGN 

        70         80         90        100        110        120 
YCVAVADAKK SLELNPNNST AMLRKGICEY HEKNYAAALE TFTEGQKLDI ETGFHRVGQA 

       130        140        150        160        170        180 
GLQLLTSSDP PALDSQSAGI TGADANFSVW IKRCQEAQNG SESEVWTHQS KIKYDWYQTE 

       190        200        210        220        230        240 
SQVVITLMIK NVQKNDVNVE FSEKELSALV KLPSGEDYNL KLELLHPIIP EQSTFKVLST 

       250        260        270        280        290        300 
KIEIKLKKPE AVRWEKLEGQ GDVPTPKQFV ADVKNLYPSS SPYTRNWDKL VGEIKEEEKN 

       310        320        330        340        350        360 
EKLEGDAALN RLFQQIYSDG SDEVKRAMNK SFMESGGTVL STNWSDVGKR KVEINPPDDM 


EWKKY 

« Hide

Isoform 2 [UniParc].

Checksum: 14DE069A1623DB53
Show »

FASTA33337,805

References

« Hide 'large scale' references
[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]Schmidt T.
Thesis (2001), University of Goettingen, Germany
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"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).
[4]Zou X., Mao Y., Xie Y.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"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.
[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].
[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].
Tissue: Cervix carcinoma.
[16]"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].
[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].
[19]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001124384.1. NM_001130912.1.
NP_006695.1. NM_006704.3.
UniGeneHs.281902.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RL1NMR-A167-276[»]
ProteinModelPortalQ9Y2Z0.
SMRQ9Y2Z0. Positions 30-111, 170-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116115. 54 interactions.
IntActQ9Y2Z0. 13 interactions.
MINTMINT-5005759.
STRING9606.ENSP00000367208.

PTM databases

PhosphoSiteQ9Y2Z0.

Polymorphism databases

DMDM62512186.

Proteomic databases

PaxDbQ9Y2Z0.
PRIDEQ9Y2Z0.

Protocols and materials databases

DNASU10910.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310528; ENSP00000308067; ENSG00000165416. [Q9Y2Z0-2]
ENST00000343788; ENSP00000367208; ENSG00000165416. [Q9Y2Z0-1]
GeneID10910.
KEGGhsa:10910.
UCSCuc001vhb.2. human. [Q9Y2Z0-2]
uc001vhc.2. human. [Q9Y2Z0-1]

Organism-specific databases

CTD10910.
GeneCardsGC13P053226.
H-InvDBHIX0026254.
HIX0201992.
HGNCHGNC:16987. SUGT1.
HPACAB015942.
HPA043949.
MIM604098. gene.
neXtProtNX_Q9Y2Z0.
PharmGKBPA134880121.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000248210.
HOVERGENHBG055080.
InParanoidQ9Y2Z0.
KOK12795.
OMASFIDEDP.
OrthoDBEOG7WX0B4.
PhylomeDBQ9Y2Z0.
TreeFamTF105979.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9Y2Z0.
BgeeQ9Y2Z0.
CleanExHS_SUGT1.
GenevestigatorQ9Y2Z0.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
2.60.40.790. 1 hit.
InterProIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007699. SGS.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF04969. CS. 1 hit.
PF05002. SGS. 1 hit.
[Graphical view]
SUPFAMSSF49764. SSF49764. 1 hit.
PROSITEPS51203. CS. 1 hit.
PS51048. SGS. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y2Z0.
GeneWikiSUGT1.
GenomeRNAi10910.
NextBio41435.
PROQ9Y2Z0.
SOURCESearch...

Entry information

Entry nameSUGT1_HUMAN
AccessionPrimary (citable) accession number: Q9Y2Z0
Secondary accession number(s): A2A303 expand/collapse secondary AC list , Q5JAK5, Q5TAM6, Q6VXY6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 133 of the entry and version 3 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 chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM