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Q13309

- SKP2_HUMAN

UniProt

Q13309 - SKP2_HUMAN

Protein

S-phase kinase-associated protein 2

Gene

SKP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (03 Oct 2003)
      Previous versions | rss
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    Functioni

    Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, FOXO1, UBP43, and probably MYC, TOB1 and TAL1. Degradation of TAL1 also requires STUB1. Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2. Promotes ubiquitination and destruction of CDH1 in a CK1-Dependent Manner, thereby regulating cell migration.14 Publications

    Pathwayi

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: IntAct
    3. ubiquitin-protein transferase activity Source: Ensembl

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. cell proliferation Source: ProtInc
    3. cellular response to cell-matrix adhesion Source: Ensembl
    4. G1/S transition of mitotic cell cycle Source: Reactome
    5. G2/M transition of mitotic cell cycle Source: Ensembl
    6. mitotic cell cycle Source: Reactome
    7. positive regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
    8. positive regulation of smooth muscle cell proliferation Source: Ensembl
    9. protein polyubiquitination Source: Ensembl
    10. regulation of cell cycle Source: Ensembl

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_821. Cyclin D associated events in G1.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-phase kinase-associated protein 2
    Alternative name(s):
    Cyclin-A/CDK2-associated protein p45
    F-box protein Skp2
    F-box/LRR-repeat protein 1
    p45skp2
    Gene namesi
    Name:SKP2
    Synonyms:FBXL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:10901. SKP2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. aggresome Source: HPA
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. nucleolus Source: HPA
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA
    7. SCF ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35801.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 424424S-phase kinase-associated protein 2PRO_0000119954Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei64 – 641Phosphoserine5 Publications
    Modified residuei68 – 681N6-acetyllysine; by p300/EP3001 Publication
    Modified residuei71 – 711N6-acetyllysine; by p300/EP3001 Publication
    Modified residuei179 – 1791Phosphoserine1 Publication

    Post-translational modificationi

    Ubiquitinated by the APC/C complex, leading to its degradation by the proteasome. Deubiquitinated by USP13.1 Publication
    Acetylation at Lys-68 and Lys-71 increases stability through impairment of APC/C-mediated proteolysis and promotes cytoplasmic retention. Deacetylated by SIRT3.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ13309.
    PaxDbiQ13309.
    PRIDEiQ13309.

    PTM databases

    PhosphoSiteiQ13309.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13309.
    BgeeiQ13309.
    CleanExiHS_SKP2.
    GenevestigatoriQ13309.

    Organism-specific databases

    HPAiCAB013533.
    HPA051196.

    Interactioni

    Subunit structurei

    Part of a SCF(SKP2) complex consisting of CUL1, RBX1, SKP1 and SKP2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Interacts directly with CUL1 and SKP1. Interacts with CKS1. Interacts with the cyclin-A-CDK2 complex. Interacts with ORC1, phosphorylated CDT1, phosphorylated RBL2, ELF4, phosphorylated RAG2, FOXO1, UBP43, MYC, TOB1, TAL1 and KMT2A/MLL1. Interacts with TRIM21.15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-456291,EBI-456291
    Q4AE163EBI-456291,EBI-7418293From a different organism.
    CDH1A5D8W42EBI-456291,EBI-7793316
    Cdh1P098032EBI-456291,EBI-984420From a different organism.
    CDKN1AP389362EBI-456291,EBI-375077
    CDKN1BP465274EBI-456291,EBI-519280
    CKS1BP610246EBI-456291,EBI-456371
    CUL1Q136169EBI-456291,EBI-359390
    DUSP1P285623EBI-456291,EBI-975493
    EP300Q094723EBI-456291,EBI-447295
    FZR1Q9UM112EBI-456291,EBI-724997
    MYCP011062EBI-456291,EBI-447544
    ORC1Q134152EBI-456291,EBI-374847
    PHBP352322EBI-7791408,EBI-354213
    RBX1P628773EBI-456291,EBI-398523
    SIRT3Q9NTG75EBI-456291,EBI-724621
    SKP1P6320815EBI-456291,EBI-307486

    Protein-protein interaction databases

    BioGridi112393. 105 interactions.
    DIPiDIP-17011N.
    IntActiQ13309. 46 interactions.
    MINTiMINT-152160.
    STRINGi9606.ENSP00000274255.

    Structurei

    Secondary structure

    1
    424
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi97 – 1004
    Helixi102 – 1098
    Helixi114 – 1163
    Helixi117 – 1215
    Helixi125 – 1317
    Helixi134 – 1363
    Beta strandi137 – 1415
    Helixi149 – 1579
    Beta strandi161 – 1644
    Beta strandi180 – 1823
    Beta strandi185 – 1873
    Helixi195 – 2028
    Beta strandi209 – 2124
    Helixi220 – 2267
    Beta strandi233 – 2364
    Helixi245 – 25410
    Beta strandi260 – 2623
    Helixi271 – 28010
    Beta strandi287 – 2893
    Helixi294 – 2963
    Helixi299 – 30810
    Beta strandi313 – 3164
    Helixi325 – 3339
    Beta strandi339 – 3413
    Helixi350 – 3589
    Beta strandi364 – 3663
    Helixi376 – 3827
    Beta strandi386 – 3894
    Beta strandi402 – 4043
    Beta strandi415 – 4173

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FQVX-ray2.80A/C/E/G/I/K/M/O89-424[»]
    1FS1X-ray1.80A/C89-141[»]
    1FS2X-ray2.90A/C89-398[»]
    1LDKX-ray3.10E97-137[»]
    2ASSX-ray3.00B89-424[»]
    2ASTX-ray2.30B89-424[»]
    ProteinModelPortaliQ13309.
    SMRiQ13309. Positions 95-419.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13309.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini94 – 14047F-boxPROSITE-ProRule annotationAdd
    BLAST
    Repeati151 – 17626LRR 11 PublicationAdd
    BLAST
    Repeati177 – 20428LRR 21 PublicationAdd
    BLAST
    Repeati210 – 23425LRR 31 PublicationAdd
    BLAST
    Repeati235 – 25723LRR 41 PublicationAdd
    BLAST
    Repeati258 – 28427LRR 51 PublicationAdd
    BLAST
    Repeati286 – 30823LRR 61 PublicationAdd
    BLAST
    Repeati309 – 33022LRR 71 PublicationAdd
    BLAST
    Repeati334 – 35623LRR 81 PublicationAdd
    BLAST
    Repeati359 – 37820LRR 91 PublicationAdd
    BLAST
    Repeati380 – 40122LRR 101 PublicationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi67 – 737Nuclear localization signal1 Publication

    Sequence similaritiesi

    Contains 1 F-box domain.PROSITE-ProRule annotation
    Contains 10 LRR (leucine-rich) repeats.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG263321.
    HOGENOMiHOG000247037.
    HOVERGENiHBG047488.
    KOiK03875.
    OMAiEIWGIRC.
    OrthoDBiEOG7PGDRM.
    PhylomeDBiQ13309.
    TreeFamiTF352582.

    Family and domain databases

    InterProiIPR001810. F-box_dom.
    [Graphical view]
    PfamiPF12937. F-box-like. 1 hit.
    [Graphical view]
    SMARTiSM00256. FBOX. 1 hit.
    [Graphical view]
    SUPFAMiSSF81383. SSF81383. 1 hit.
    PROSITEiPS50181. FBOX. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13309-1) [UniParc]FASTAAdd to Basket

    Also known as: SKP2-alpha

    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

    MHRKHLQEIP DLSSNVATSF TWGWDSSKTS ELLSGMGVSA LEKEEPDSEN    50
    IPQELLSNLG HPESPPRKRL KSKGSDKDFV IVRRPKLNRE NFPGVSWDSL 100
    PDELLLGIFS CLCLPELLKV SGVCKRWYRL ASDESLWQTL DLTGKNLHPD 150
    VTGRLLSQGV IAFRCPRSFM DQPLAEHFSP FRVQHMDLSN SVIEVSTLHG 200
    ILSQCSKLQN LSLEGLRLSD PIVNTLAKNS NLVRLNLSGC SGFSEFALQT 250
    LLSSCSRLDE LNLSWCFDFT EKHVQVAVAH VSETITQLNL SGYRKNLQKS 300
    DLSTLVRRCP NLVHLDLSDS VMLKNDCFQE FFQLNYLQHL SLSRCYDIIP 350
    ETLLELGEIP TLKTLQVFGI VPDGTLQLLK EALPHLQINC SHFTTIARPT 400
    IGNKKNQEIW GIKCRLTLQK PSCL 424
    Length:424
    Mass (Da):47,761
    Last modified:October 3, 2003 - v2
    Checksum:iF29B7C338A7A37E9
    GO
    Isoform 2 (identifier: Q13309-2) [UniParc]FASTAAdd to Basket

    Also known as: SKP2-beta

    The sequence of this isoform differs from the canonical sequence as follows:
         355-424: ELGEIPTLKT...RLTLQKPSCL → LVTRAGVRIR...FYFYRLVLKQ

    Show »
    Length:410
    Mass (Da):46,576
    Checksum:i8CB41CC9968695E3
    GO
    Isoform 3 (identifier: Q13309-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-169: Missing.
         180-224: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:210
    Mass (Da):23,763
    Checksum:i06BF227E9F6974C9
    GO

    Sequence cautioni

    The sequence BAB87202.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAC50242.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti185 – 1851H → D in AAC50242. (PubMed:7553852)Curated
    Sequence conflicti215 – 2151Missing in AAC50242. (PubMed:7553852)Curated
    Sequence conflicti238 – 2381S → P in AAC50242. (PubMed:7553852)Curated
    Sequence conflicti241 – 2411S → P in AAC50242. (PubMed:7553852)Curated
    Sequence conflicti244 – 2474SEFA → PKFP in AAC50242. (PubMed:7553852)Curated
    Sequence conflicti251 – 2511L → F in AAC50242. (PubMed:7553852)Curated
    Sequence conflicti256 – 2561S → P in AAC50242. (PubMed:7553852)Curated
    Sequence conflicti268 – 2681D → N in AAC50242. (PubMed:7553852)Curated
    Sequence conflicti285 – 2851I → M in AAC50242. (PubMed:7553852)Curated
    Sequence conflicti319 – 3191D → N in AAC50242. (PubMed:7553852)Curated
    Sequence conflicti332 – 3321F → S in AAC50242. (PubMed:7553852)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti85 – 851P → L.
    Corresponds to variant rs3913486 [ dbSNP | Ensembl ].
    VAR_016984
    Natural varianti87 – 871L → I.
    Corresponds to variant rs3913487 [ dbSNP | Ensembl ].
    VAR_016985

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 169169Missing in isoform 3. 1 PublicationVSP_044931Add
    BLAST
    Alternative sequencei180 – 22445Missing in isoform 3. 1 PublicationVSP_044932Add
    BLAST
    Alternative sequencei355 – 42470ELGEI…KPSCL → LVTRAGVRIRLDSDIGCPQT YRTSKLKSSHKLFCQHVRVI CIFVCDFYFYRLVLKQ in isoform 2. 2 PublicationsVSP_008432Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33761 mRNA. Translation: AAC50242.1. Different initiation.
    AB050979 mRNA. Translation: BAB87200.1.
    AB050980 mRNA. Translation: BAB87201.1.
    AB050981 mRNA. Translation: BAB87202.1. Sequence problems.
    AY029177 mRNA. Translation: AAK31593.1.
    AK291255 mRNA. Translation: BAF83944.1.
    AK296223 mRNA. Translation: BAG58946.1.
    AC008942 Genomic DNA. No translation available.
    CH471119 Genomic DNA. Translation: EAW55936.1.
    BC001441 mRNA. Translation: AAH01441.1.
    BC007441 mRNA. Translation: AAH07441.1.
    CCDSiCCDS3915.1. [Q13309-2]
    CCDS3916.1. [Q13309-1]
    CCDS58944.1. [Q13309-4]
    PIRiI39171.
    RefSeqiNP_001230049.1. NM_001243120.1. [Q13309-4]
    NP_005974.2. NM_005983.3. [Q13309-1]
    NP_116026.1. NM_032637.3. [Q13309-2]
    UniGeneiHs.23348.

    Genome annotation databases

    EnsembliENST00000274254; ENSP00000274254; ENSG00000145604. [Q13309-2]
    ENST00000274255; ENSP00000274255; ENSG00000145604. [Q13309-1]
    ENST00000546211; ENSP00000443492; ENSG00000145604. [Q13309-4]
    GeneIDi6502.
    KEGGihsa:6502.
    UCSCiuc003jkc.2. human. [Q13309-1]
    uc003jkd.3. human. [Q13309-2]
    uc011cou.2. human.

    Polymorphism databases

    DMDMi37537922.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33761 mRNA. Translation: AAC50242.1 . Different initiation.
    AB050979 mRNA. Translation: BAB87200.1 .
    AB050980 mRNA. Translation: BAB87201.1 .
    AB050981 mRNA. Translation: BAB87202.1 . Sequence problems.
    AY029177 mRNA. Translation: AAK31593.1 .
    AK291255 mRNA. Translation: BAF83944.1 .
    AK296223 mRNA. Translation: BAG58946.1 .
    AC008942 Genomic DNA. No translation available.
    CH471119 Genomic DNA. Translation: EAW55936.1 .
    BC001441 mRNA. Translation: AAH01441.1 .
    BC007441 mRNA. Translation: AAH07441.1 .
    CCDSi CCDS3915.1. [Q13309-2 ]
    CCDS3916.1. [Q13309-1 ]
    CCDS58944.1. [Q13309-4 ]
    PIRi I39171.
    RefSeqi NP_001230049.1. NM_001243120.1. [Q13309-4 ]
    NP_005974.2. NM_005983.3. [Q13309-1 ]
    NP_116026.1. NM_032637.3. [Q13309-2 ]
    UniGenei Hs.23348.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FQV X-ray 2.80 A/C/E/G/I/K/M/O 89-424 [» ]
    1FS1 X-ray 1.80 A/C 89-141 [» ]
    1FS2 X-ray 2.90 A/C 89-398 [» ]
    1LDK X-ray 3.10 E 97-137 [» ]
    2ASS X-ray 3.00 B 89-424 [» ]
    2AST X-ray 2.30 B 89-424 [» ]
    ProteinModelPortali Q13309.
    SMRi Q13309. Positions 95-419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112393. 105 interactions.
    DIPi DIP-17011N.
    IntActi Q13309. 46 interactions.
    MINTi MINT-152160.
    STRINGi 9606.ENSP00000274255.

    PTM databases

    PhosphoSitei Q13309.

    Polymorphism databases

    DMDMi 37537922.

    Proteomic databases

    MaxQBi Q13309.
    PaxDbi Q13309.
    PRIDEi Q13309.

    Protocols and materials databases

    DNASUi 6502.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274254 ; ENSP00000274254 ; ENSG00000145604 . [Q13309-2 ]
    ENST00000274255 ; ENSP00000274255 ; ENSG00000145604 . [Q13309-1 ]
    ENST00000546211 ; ENSP00000443492 ; ENSG00000145604 . [Q13309-4 ]
    GeneIDi 6502.
    KEGGi hsa:6502.
    UCSCi uc003jkc.2. human. [Q13309-1 ]
    uc003jkd.3. human. [Q13309-2 ]
    uc011cou.2. human.

    Organism-specific databases

    CTDi 6502.
    GeneCardsi GC05P036103.
    HGNCi HGNC:10901. SKP2.
    HPAi CAB013533.
    HPA051196.
    MIMi 601436. gene.
    neXtProti NX_Q13309.
    PharmGKBi PA35801.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263321.
    HOGENOMi HOG000247037.
    HOVERGENi HBG047488.
    KOi K03875.
    OMAi EIWGIRC.
    OrthoDBi EOG7PGDRM.
    PhylomeDBi Q13309.
    TreeFami TF352582.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_821. Cyclin D associated events in G1.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.

    Miscellaneous databases

    EvolutionaryTracei Q13309.
    GeneWikii SKP2.
    GenomeRNAii 6502.
    NextBioi 25275.
    PROi Q13309.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13309.
    Bgeei Q13309.
    CleanExi HS_SKP2.
    Genevestigatori Q13309.

    Family and domain databases

    InterProi IPR001810. F-box_dom.
    [Graphical view ]
    Pfami PF12937. F-box-like. 1 hit.
    [Graphical view ]
    SMARTi SM00256. FBOX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81383. SSF81383. 1 hit.
    PROSITEi PS50181. FBOX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "p19Skp1 and p45Skp2 are essential elements of the cyclin A-CDK2 S phase kinase."
      Zhang H., Kobayashi R., Galaktionov K., Beach D.
      Cell 82:915-925(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 6-19; 31-58; 80-86 AND 365-372, INTERACTION WITH CYCLIN A-CDK2 COMPLEX.
    2. "Human SKP2-like protein."
      Yamaguchi T.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Liver.
    3. "Androgenic regulation of Skp2 in androgen-dependent and -independent LNCaP human prostate tumor cells."
      Kokontis J.M., Fukuchi J., Liao S.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Prostatic carcinoma.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Thalamus.
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Placenta.
    8. "The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2)."
      Tedesco D., Lukas J., Reed S.I.
      Genes Dev. 16:2946-2957(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBL2, FUNCTION IN UBIQUITINATION OF RBL2.
    9. "Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication."
      Mendez J., Zou-Yang X.H., Kim S.Y., Hidaka M., Tansey W.P., Stillman B.
      Mol. Cell 9:481-491(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ORC1, FUNCTION IN UBIQUITINATION OF ORC1.
    10. "The SCF(Skp2) ubiquitin ligase complex interacts with the human replication licensing factor Cdt1 and regulates Cdt1 degradation."
      Li X., Zhao Q., Liao R., Sun P., Wu X.
      J. Biol. Chem. 278:30854-30858(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDT1, FUNCTION IN UBIQUITINATION OF CDT1.
    11. "The F-box protein Skp2 participates in c-Myc proteosomal degradation and acts as a cofactor for c-Myc-regulated transcription."
      von der Lehr N., Johansson S., Wu S., Bahram F., Castell A., Cetinkaya C., Hydbring P., Weidung I., Nakayama K., Nakayama K.I., Soderberg O., Kerppola T.K., Larsson L.G.
      Mol. Cell 11:1189-1200(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYC, FUNCTION IN UBIQUITINATION OF MYC.
    12. "The ISG15 isopeptidase UBP43 is regulated by proteolysis via the SCFSkp2 ubiquitin ligase."
      Tokarz S., Berset C., La Rue J., Friedman K., Nakayama K., Nakayama K., Zhang D.E., Lanker S.
      J. Biol. Chem. 279:46424-46430(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBP43, FUNCTION IN UBIQUITINATION OF UBP43.
    13. "Ubiquitination of p21Cip1/WAF1 by SCFSkp2: substrate requirement and ubiquitination site selection."
      Wang W., Nacusi L., Sheaff R.J., Liu X.
      Biochemistry 44:14553-14564(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF CDKN1A.
    14. "Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J recombinase to the cell cycle."
      Jiang H., Chang F.C., Ross A.E., Lee J., Nakayama K., Nakayama K., Desiderio S.
      Mol. Cell 18:699-709(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAG2, FUNCTION IN UBIQUITINATION OF RAG2.
    15. "Ubiquitylation of Cdk9 by Skp2 facilitates optimal Tat transactivation."
      Barboric M., Zhang F., Besenicar M., Plemenitas A., Peterlin B.M.
      J. Virol. 79:11135-11141(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF CDK9.
    16. "Skp2 inhibits FOXO1 in tumor suppression through ubiquitin-mediated degradation."
      Huang H., Regan K.M., Wang F., Wang D., Smith D.I., van Deursen J.M., Tindall D.J.
      Proc. Natl. Acad. Sci. U.S.A. 102:1649-1654(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FOXO1, FUNCTION IN UBIQUITINATION OF FOXO1.
    17. Cited for: INTERACTION WITH TOB1, FUNCTION IN UBIQUITINATION OF TOB1.
    18. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "The ETS protein MEF is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCFSkp2."
      Liu Y., Hedvat C.V., Mao S., Zhu X.H., Yao J., Nguyen H., Koff A., Nimer S.D.
      Mol. Cell. Biol. 26:3114-3123(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ELF4, FUNCTION IN UBIQUITINATION OF ELF4.
    20. "Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein."
      Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M., Krek W.
      Mol. Cell. Biol. 26:5994-6004(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, INTERACTION WITH TRIM21.
    21. "Bimodal degradation of MLL by SCFSkp2 and APCCdc20 assures cell cycle execution: a critical regulatory circuit lost in leukemogenic MLL fusions."
      Liu H., Cheng E.H., Hsieh J.J.
      Genes Dev. 21:2385-2398(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KMT2A/MLL1, FUNCTION IN UBIQUITINATION OF KMT2A/MLL1.
    22. "Ubiquitination and degradation of Tal1/SCL are induced by Notch signaling and depend on Skp2 and CHIP."
      Nie L., Wu H., Sun X.H.
      J. Biol. Chem. 283:684-692(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAL1, FUNCTION IN UBIQUITINATION OF TAL1.
    23. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control."
      Chen M., Gutierrez G.J., Ronai Z.A.
      Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEUBIQUITINATION BY USP13.
    29. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: FUNCTION, ACETYLATION AT LYS-68 AND LYS-71, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION.
    31. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 101-153 IN COMPLEX WITH 1-147 OF SKP1.
    32. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CUL1; SKP1 AND RBX1, LEUCINE-RICH REPEATS, INTERACTION WITH CKS1.

    Entry informationi

    Entry nameiSKP2_HUMAN
    AccessioniPrimary (citable) accession number: Q13309
    Secondary accession number(s): A8K5E0
    , B4DJT4, Q8TDZ0, Q8TDZ1, Q9BV69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: October 3, 2003
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 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 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3