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Q13309

- SKP2_HUMAN

UniProt

Q13309 - SKP2_HUMAN

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ13309.
CleanExiHS_SKP2.
ExpressionAtlasiQ13309. baseline and differential.
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. 111 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.
GeneTreeiENSGT00390000007918.
HOGENOMiHOG000247037.
HOVERGENiHBG047488.
InParanoidiQ13309.
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) [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

        10         20         30         40         50
MHRKHLQEIP DLSSNVATSF TWGWDSSKTS ELLSGMGVSA LEKEEPDSEN
60 70 80 90 100
IPQELLSNLG HPESPPRKRL KSKGSDKDFV IVRRPKLNRE NFPGVSWDSL
110 120 130 140 150
PDELLLGIFS CLCLPELLKV SGVCKRWYRL ASDESLWQTL DLTGKNLHPD
160 170 180 190 200
VTGRLLSQGV IAFRCPRSFM DQPLAEHFSP FRVQHMDLSN SVIEVSTLHG
210 220 230 240 250
ILSQCSKLQN LSLEGLRLSD PIVNTLAKNS NLVRLNLSGC SGFSEFALQT
260 270 280 290 300
LLSSCSRLDE LNLSWCFDFT EKHVQVAVAH VSETITQLNL SGYRKNLQKS
310 320 330 340 350
DLSTLVRRCP NLVHLDLSDS VMLKNDCFQE FFQLNYLQHL SLSRCYDIIP
360 370 380 390 400
ETLLELGEIP TLKTLQVFGI VPDGTLQLLK EALPHLQINC SHFTTIARPT
410 420
IGNKKNQEIW GIKCRLTLQK PSCL
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]
ENST00000620197; ENSP00000478031; 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. 111 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 ]
ENST00000620197 ; ENSP00000478031 ; 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.
GeneTreei ENSGT00390000007918.
HOGENOMi HOG000247037.
HOVERGENi HBG047488.
InParanoidi Q13309.
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

Bgeei Q13309.
CleanExi HS_SKP2.
ExpressionAtlasi Q13309. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 149 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