Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13309 (SKP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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:
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 names
Name:SKP2
Synonyms:FBXL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.30

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.32

Subcellular location

Cytoplasm. Nucleus Ref.30.

Post-translational modification

Ubiquitinated by the APC/C complex, leading to its degradation by the proteasome. Deubiquitinated by USP13. Ref.28

Acetylation at Lys-68 and Lys-71 increases stability through impairment of APC/C-mediated proteolysis and promotes cytoplasmic retention. Deacetylated by SIRT3. Ref.30

Sequence similarities

Contains 1 F-box domain.

Contains 10 LRR (leucine-rich) repeats.

Sequence caution

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

The sequence BAB87202.1 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainLeucine-rich repeat
Repeat
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

cellular response to cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of intracellular estrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

protein polyubiquitination

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentSCF ubiquitin ligase complex

Inferred from direct assay Ref.20. Source: UniProtKB

aggresome

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionidentical protein binding

Inferred from physical interaction Ref.30. Source: IntAct

protein binding

Inferred from physical interaction PubMed 20134482. Source: IntAct

ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13309-1)

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.
Isoform 2 (identifier: Q13309-2)

Also known as: SKP2-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     355-424: ELGEIPTLKT...RLTLQKPSCL → LVTRAGVRIR...FYFYRLVLKQ
Isoform 3 (identifier: Q13309-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-169: Missing.
     180-224: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424S-phase kinase-associated protein 2
PRO_0000119954

Regions

Domain94 – 14047F-box
Repeat151 – 17626LRR 1
Repeat177 – 20428LRR 2
Repeat210 – 23425LRR 3
Repeat235 – 25723LRR 4
Repeat258 – 28427LRR 5
Repeat286 – 30823LRR 6
Repeat309 – 33022LRR 7
Repeat334 – 35623LRR 8
Repeat359 – 37820LRR 9
Repeat380 – 40122LRR 10
Motif67 – 737Nuclear localization signal Ref.30

Amino acid modifications

Modified residue641Phosphoserine Ref.18 Ref.24 Ref.25 Ref.26 Ref.29
Modified residue681N6-acetyllysine; by p300/EP300 Ref.30
Modified residue711N6-acetyllysine; by p300/EP300 Ref.30
Modified residue1791Phosphoserine Ref.23

Natural variations

Alternative sequence1 – 169169Missing in isoform 3.
VSP_044931
Alternative sequence180 – 22445Missing in isoform 3.
VSP_044932
Alternative sequence355 – 42470ELGEI…KPSCL → LVTRAGVRIRLDSDIGCPQT YRTSKLKSSHKLFCQHVRVI CIFVCDFYFYRLVLKQ in isoform 2.
VSP_008432
Natural variant851P → L.
Corresponds to variant rs3913486 [ dbSNP | Ensembl ].
VAR_016984
Natural variant871L → I.
Corresponds to variant rs3913487 [ dbSNP | Ensembl ].
VAR_016985

Experimental info

Sequence conflict1851H → D in AAC50242. Ref.1
Sequence conflict2151Missing in AAC50242. Ref.1
Sequence conflict2381S → P in AAC50242. Ref.1
Sequence conflict2411S → P in AAC50242. Ref.1
Sequence conflict244 – 2474SEFA → PKFP in AAC50242. Ref.1
Sequence conflict2511L → F in AAC50242. Ref.1
Sequence conflict2561S → P in AAC50242. Ref.1
Sequence conflict2681D → N in AAC50242. Ref.1
Sequence conflict2851I → M in AAC50242. Ref.1
Sequence conflict3191D → N in AAC50242. Ref.1
Sequence conflict3321F → S in AAC50242. Ref.1

Secondary structure

........................................................... 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SKP2-alpha) [UniParc].

Last modified October 3, 2003. Version 2.
Checksum: F29B7C338A7A37E9

FASTA42447,761
        10         20         30         40         50         60 
MHRKHLQEIP DLSSNVATSF TWGWDSSKTS ELLSGMGVSA LEKEEPDSEN IPQELLSNLG 

        70         80         90        100        110        120 
HPESPPRKRL KSKGSDKDFV IVRRPKLNRE NFPGVSWDSL PDELLLGIFS CLCLPELLKV 

       130        140        150        160        170        180 
SGVCKRWYRL ASDESLWQTL DLTGKNLHPD VTGRLLSQGV IAFRCPRSFM DQPLAEHFSP 

       190        200        210        220        230        240 
FRVQHMDLSN SVIEVSTLHG ILSQCSKLQN LSLEGLRLSD PIVNTLAKNS NLVRLNLSGC 

       250        260        270        280        290        300 
SGFSEFALQT LLSSCSRLDE LNLSWCFDFT EKHVQVAVAH VSETITQLNL SGYRKNLQKS 

       310        320        330        340        350        360 
DLSTLVRRCP NLVHLDLSDS VMLKNDCFQE FFQLNYLQHL SLSRCYDIIP ETLLELGEIP 

       370        380        390        400        410        420 
TLKTLQVFGI VPDGTLQLLK EALPHLQINC SHFTTIARPT IGNKKNQEIW GIKCRLTLQK 


PSCL 

« Hide

Isoform 2 (SKP2-beta) [UniParc].

Checksum: 8CB41CC9968695E3
Show »

FASTA41046,576
Isoform 3 [UniParc].

Checksum: 06BF227E9F6974C9
Show »

FASTA21023,763

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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].
[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]"Degradation of Tob1 mediated by SCFSkp2-dependent ubiquitination."
Hiramatsu Y., Kitagawa K., Suzuki T., Uchida C., Hattori T., Kikuchi H., Oda T., Hatakeyama S., Nakayama K.I., Yamamoto T., Konno H., Kitagawa M.
Cancer Res. 66:8477-8483(2006) [PubMed] [Europe PMC] [Abstract]
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]"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: 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]"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].
[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]"Acetylation-dependent regulation of Skp2 function."
Inuzuka H., Gao D., Finley L.W., Yang W., Wan L., Fukushima H., Chin Y.R., Zhai B., Shaik S., Lau A.W., Wang Z., Gygi S.P., Nakayama K., Teruya-Feldstein J., Toker A., Haigis M.C., Pandolfi P.P., Wei W.
Cell 150:179-193(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACETYLATION AT LYS-68 AND LYS-71, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION.
[31]"Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex."
Schulman B.A., Carrano A.C., Jeffrey P.D., Bowen Z., Kinnucan E.R.E., Finnin M.S., Elledge S.J., Harper J.W., Pagano M., Pavletich N.P.
Nature 408:381-386(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 101-153 IN COMPLEX WITH 1-147 OF SKP1.
[32]"Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase complex."
Zheng N., Schulman B.A., Song L., Miller J.J., Jeffrey P.D., Wang P., Chu C., Koepp D.M., Elledge S.J., Pagano M., Conaway R.C., Conaway J.W., Harper J.W., Pavletich N.P.
Nature 416:703-709(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CUL1; SKP1 AND RBX1, LEUCINE-RICH REPEATS, INTERACTION WITH CKS1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3915.1. [Q13309-2]
CCDS3916.1. [Q13309-1]
CCDS58944.1. [Q13309-4]
PIRI39171.
RefSeqNP_001230049.1. NM_001243120.1. [Q13309-4]
NP_005974.2. NM_005983.3. [Q13309-1]
NP_116026.1. NM_032637.3. [Q13309-2]
UniGeneHs.23348.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ13309.
SMRQ13309. Positions 95-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112393. 105 interactions.
DIPDIP-17011N.
IntActQ13309. 33 interactions.
MINTMINT-152160.
STRING9606.ENSP00000274255.

PTM databases

PhosphoSiteQ13309.

Polymorphism databases

DMDM37537922.

Proteomic databases

MaxQBQ13309.
PaxDbQ13309.
PRIDEQ13309.

Protocols and materials databases

DNASU6502.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274254; ENSP00000274254; ENSG00000145604. [Q13309-2]
ENST00000274255; ENSP00000274255; ENSG00000145604. [Q13309-1]
ENST00000546211; ENSP00000443492; ENSG00000145604. [Q13309-4]
GeneID6502.
KEGGhsa:6502.
UCSCuc003jkc.2. human. [Q13309-1]
uc003jkd.3. human. [Q13309-2]
uc011cou.2. human.

Organism-specific databases

CTD6502.
GeneCardsGC05P036103.
HGNCHGNC:10901. SKP2.
HPACAB013533.
HPA051196.
MIM601436. gene.
neXtProtNX_Q13309.
PharmGKBPA35801.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263321.
HOGENOMHOG000247037.
HOVERGENHBG047488.
KOK03875.
OMAEIWGIRC.
OrthoDBEOG7PGDRM.
PhylomeDBQ13309.
TreeFamTF352582.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ13309.
BgeeQ13309.
CleanExHS_SKP2.
GenevestigatorQ13309.

Family and domain databases

InterProIPR001810. F-box_dom.
[Graphical view]
PfamPF12937. F-box-like. 1 hit.
[Graphical view]
SMARTSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMSSF81383. SSF81383. 1 hit.
PROSITEPS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13309.
GeneWikiSKP2.
GenomeRNAi6502.
NextBio25275.
PROQ13309.
SOURCESearch...

Entry information

Entry nameSKP2_HUMAN
AccessionPrimary (citable) accession number: Q13309
Secondary accession number(s): A8K5E0 expand/collapse secondary AC list , B4DJT4, Q8TDZ0, Q8TDZ1, Q9BV69
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: July 9, 2014
This is version 146 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM