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Q9Y2Z0

- SUGT1_HUMAN

UniProt

Q9Y2Z0 - SUGT1_HUMAN

Protein

Suppressor of G2 allele of SKP1 homolog

Gene

SUGT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. innate immune response Source: Reactome
    2. mitotic nuclear division Source: ProtInc
    3. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_75808. The NLRP3 inflammasome.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Suppressor of G2 allele of SKP1 homolog
    Alternative name(s):
    Protein 40-6-3
    Sgt1
    Gene namesi
    Name:SUGT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:16987. SUGT1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Translocates to the nucleus upon heat shock, requiring S100A6.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. kinetochore Source: ProtInc
    4. nucleus Source: HPA
    5. ubiquitin ligase complex Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134880121.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed6 Publications
    Chaini2 – 365364Suppressor of G2 allele of SKP1 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.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y2Z0.
    PaxDbiQ9Y2Z0.
    PRIDEiQ9Y2Z0.

    PTM databases

    PhosphoSiteiQ9Y2Z0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y2Z0.
    BgeeiQ9Y2Z0.
    CleanExiHS_SUGT1.
    GenevestigatoriQ9Y2Z0.

    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
    LRCH4O754272EBI-307008,EBI-718707

    Protein-protein interaction databases

    BioGridi116115. 54 interactions.
    DIPiDIP-53799N.
    IntActiQ9Y2Z0. 25 interactions.
    MINTiMINT-5005759.
    STRINGi9606.ENSP00000367208.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 SUGT1 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.
    HOGENOMiHOG000248210.
    HOVERGENiHBG055080.
    InParanoidiQ9Y2Z0.
    KOiK12795.
    OMAiSFIDEDP.
    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.
    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. Align

    Isoform 1 (identifier: Q9Y2Z0-1) [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

    MAAAAAGTAT SQRFFQSFSD ALIDEDPQAA LEELTKALEQ KPDDAQYYCQ    50
    RAYCHILLGN YCVAVADAKK SLELNPNNST AMLRKGICEY HEKNYAAALE 100
    TFTEGQKLDI ETGFHRVGQA GLQLLTSSDP PALDSQSAGI TGADANFSVW 150
    IKRCQEAQNG SESEVWTHQS KIKYDWYQTE SQVVITLMIK NVQKNDVNVE 200
    FSEKELSALV KLPSGEDYNL KLELLHPIIP EQSTFKVLST KIEIKLKKPE 250
    AVRWEKLEGQ GDVPTPKQFV ADVKNLYPSS SPYTRNWDKL VGEIKEEEKN 300
    EKLEGDAALN RLFQQIYSDG SDEVKRAMNK SFMESGGTVL STNWSDVGKR 350
    KVEINPPDDM EWKKY 365
    Length:365
    Mass (Da):41,024
    Last modified:January 23, 2007 - v3
    Checksum:i4A5A413E70561D9A
    GO
    Isoform 2 (identifier: Q9Y2Z0-2) [UniParc]FASTAAdd to Basket

    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. 1 PublicationCurated

    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:
    EMBL
    GenBank
    DDBJ
    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. [Q9Y2Z0-1]
    GeneIDi10910.
    KEGGihsa:10910.
    UCSCiuc001vhb.2. human. [Q9Y2Z0-2]
    uc001vhc.2. human. [Q9Y2Z0-1]

    Polymorphism databases

    DMDMi62512186.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS45050.1. [Q9Y2Z0-1 ]
    CCDS9436.1. [Q9Y2Z0-2 ]
    RefSeqi NP_001124384.1. NM_001130912.1. [Q9Y2Z0-1 ]
    NP_006695.1. NM_006704.3. [Q9Y2Z0-2 ]
    UniGenei Hs.281902.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RL1 NMR - A 167-276 [» ]
    ProteinModelPortali Q9Y2Z0.
    SMRi Q9Y2Z0. Positions 30-111, 170-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116115. 54 interactions.
    DIPi DIP-53799N.
    IntActi Q9Y2Z0. 25 interactions.
    MINTi MINT-5005759.
    STRINGi 9606.ENSP00000367208.

    PTM databases

    PhosphoSitei Q9Y2Z0.

    Polymorphism databases

    DMDMi 62512186.

    Proteomic databases

    MaxQBi Q9Y2Z0.
    PaxDbi Q9Y2Z0.
    PRIDEi Q9Y2Z0.

    Protocols and materials databases

    DNASUi 10910.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310528 ; ENSP00000308067 ; ENSG00000165416 . [Q9Y2Z0-2 ]
    ENST00000343788 ; ENSP00000367208 ; ENSG00000165416 . [Q9Y2Z0-1 ]
    GeneIDi 10910.
    KEGGi hsa:10910.
    UCSCi uc001vhb.2. human. [Q9Y2Z0-2 ]
    uc001vhc.2. human. [Q9Y2Z0-1 ]

    Organism-specific databases

    CTDi 10910.
    GeneCardsi GC13P053226.
    H-InvDB HIX0026254.
    HIX0201992.
    HGNCi HGNC:16987. SUGT1.
    HPAi CAB015942.
    HPA043949.
    MIMi 604098. gene.
    neXtProti NX_Q9Y2Z0.
    PharmGKBi PA134880121.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000248210.
    HOVERGENi HBG055080.
    InParanoidi Q9Y2Z0.
    KOi K12795.
    OMAi SFIDEDP.
    OrthoDBi EOG7WX0B4.
    PhylomeDBi Q9Y2Z0.
    TreeFami TF105979.

    Enzyme and pathway databases

    Reactomei REACT_75808. The NLRP3 inflammasome.

    Miscellaneous databases

    EvolutionaryTracei Q9Y2Z0.
    GeneWikii SUGT1.
    GenomeRNAii 10910.
    NextBioi 41435.
    PROi Q9Y2Z0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2Z0.
    Bgeei Q9Y2Z0.
    CleanExi HS_SUGT1.
    Genevestigatori Q9Y2Z0.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    2.60.40.790. 1 hit.
    InterProi IPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR007699. SGS.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF04969. CS. 1 hit.
    PF05002. SGS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49764. SSF49764. 1 hit.
    PROSITEi PS51203. CS. 1 hit.
    PS51048. SGS. 1 hit.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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].
    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. 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. 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.

    Entry informationi

    Entry nameiSUGT1_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: October 1, 2014
    This is version 138 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