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P63208

- SKP1_HUMAN

UniProt

P63208 - SKP1_HUMAN

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Protein

S-phase kinase-associated protein 1

Gene

SKP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) direct ubiquitination of TTI1 and TELO2. SCF(FBXO10) direct ubiquitination of BCL2.4 Publications

Pathwayi

GO - Molecular functioni

  1. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. G1/S transition of mitotic cell cycle Source: Reactome
  3. G2/M transition of mitotic cell cycle Source: Reactome
  4. histone H2A monoubiquitination Source: UniProtKB
  5. mitotic cell cycle Source: Reactome
  6. Notch signaling pathway Source: Reactome
  7. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  8. protein ubiquitination Source: UniProtKB
  9. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  10. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  11. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_115697. Prolactin receptor signaling.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_160305. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_206597. Degradation of GLI2 by the proteasome.
REACT_22442. Interleukin-1 signaling.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_24941. Circadian Clock.
REACT_267605. Degradation of GLI1 by the proteasome.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_821. Cyclin D associated events in G1.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
S-phase kinase-associated protein 1
Alternative name(s):
Cyclin-A/CDK2-associated protein p19
Short name:
p19A
Organ of Corti protein 2
Short name:
OCP-2
Organ of Corti protein II
Short name:
OCP-II
RNA polymerase II elongation factor-like protein
SIII
Transcription elongation factor B polypeptide 1-like
p19skp1
Gene namesi
Name:SKP1
Synonyms:EMC19, OCP2, SKP1A, TCEB1L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:10899. SKP1.

Subcellular locationi

GO - Cellular componenti

  1. Cul7-RING ubiquitin ligase complex Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. nucleoplasm Source: Reactome
  5. SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162403424.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 163162S-phase kinase-associated protein 1PRO_0000187251Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311Phosphothreonine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP63208.
PaxDbiP63208.
PeptideAtlasiP63208.
PRIDEiP63208.

2D gel databases

SWISS-2DPAGEP63208.

PTM databases

PhosphoSiteiP63208.

Expressioni

Gene expression databases

BgeeiP63208.
CleanExiHS_SKP1.
ExpressionAtlasiP63208. baseline and differential.
GenevestigatoriP63208.

Organism-specific databases

HPAiCAB012982.
HPA053745.

Interactioni

Subunit structurei

Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein as substrate-specific subunit. Component of the SCF(FBXW11) complex containing FBXW11. Component of the SCF(SKP2) complex containing SKP2, in which it interacts directly with SKP1, SKP2 and RBX1. Component of the SCF(FBXW2) complex containing FBXw2. Component of the SCF(FBXO32) complex containing FBXO32. Component of the probable SCF(FBXO7) complex containing FBXO7. Component of the SCF(FBXO10) complex containing FBXO10. Component of the SCF(FBXO11) complex containing FBXO11. Component of the SCF(FBXO25) complex containing FBXO25. Component of the SCF(FBXO33) complex containing FBXO33. Component of the probable SCF(FBXO4) complex containing FBXO4. Component of the SCF(FBXO44) complex, composed of SKP1, CUL1 and FBXO44. Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC. This complex binds phosphorylated NFKBIA. Part of a SCF complex consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Component of the SCF(FBXO17) complex, composed of SKP1, CUL1 and FBXO17. Component of the SCF(FBXO27) complex, composed of SKP1, CUL1 and FBXO27. Component of the SCF(CCNF) complex consisting of CUL1, RBX1, SKP1 and CCNF. Component of the SCF(FBXL3) complex composed of CUL1, SKP1, RBX1 and FBXL3. Component of the SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21. Component of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Component of the SCF(FBXW7) composed of CUL1, SKP1, RBX1 and FBXW7.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BTRCQ9Y2974EBI-307486,EBI-307461
CCNFP410026EBI-307486,EBI-1207574
CDKN1AP389363EBI-307486,EBI-375077
CTNNB1P352223EBI-307486,EBI-491549
CUL1Q136169EBI-307486,EBI-359390
ECDO959053EBI-307486,EBI-2557598
Fbxl21Q8BFZ43EBI-307486,EBI-6898235From a different organism.
Fbxl3Q8C4V43EBI-307486,EBI-1266589From a different organism.
FBXL8Q96CD03EBI-307486,EBI-2321097
FBXO11Q86XK22EBI-307486,EBI-1047804
FBXO3Q9UK992EBI-307486,EBI-2509901
FBXO46Q6PJ613EBI-307486,EBI-2322982
FBXO7Q9Y3I12EBI-307486,EBI-1161222
FBXW11Q9UKB14EBI-307486,EBI-355189
FBXW2Q9UKT83EBI-307486,EBI-914727
FBXW5Q969U63EBI-307486,EBI-741068
FBXW7Q969H05EBI-307486,EBI-359574
FBXW9Q5XUX13EBI-307486,EBI-2322729
MYCQ149012EBI-307486,EBI-7982457
PPP1CAP621363EBI-307486,EBI-357253
SKP2Q1330915EBI-307486,EBI-456291

Protein-protein interaction databases

BioGridi112391. 162 interactions.
DIPiDIP-31606N.
IntActiP63208. 81 interactions.
MINTiMINT-5001195.
STRINGi9606.ENSP00000231487.

Structurei

Secondary structure

1
163
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Beta strandi9 – 124Combined sources
Beta strandi13 – 175Combined sources
Helixi18 – 225Combined sources
Helixi25 – 339Combined sources
Beta strandi44 – 463Combined sources
Beta strandi47 – 504Combined sources
Helixi52 – 6514Combined sources
Helixi87 – 926Combined sources
Helixi97 – 11014Combined sources
Helixi113 – 12715Combined sources
Beta strandi128 – 1303Combined sources
Helixi132 – 1387Combined sources
Helixi149 – 1568Combined sources
Turni157 – 1593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQVX-ray2.80B/D/F/H/J/L/N/P1-69[»]
B/D/F/H/J/L/N/P83-163[»]
1FS1X-ray1.80B/D1-147[»]
1FS2X-ray2.90B/D1-147[»]
1LDKX-ray3.10D2-140[»]
1P22X-ray2.95B1-163[»]
2ASSX-ray3.00A2-160[»]
2ASTX-ray2.30A2-160[»]
2E31X-ray2.40B1-163[»]
2E32X-ray3.52B/D1-163[»]
2OVPX-ray2.90A1-69[»]
A82-149[»]
2OVQX-ray2.60A1-69[»]
A82-149[»]
2OVRX-ray2.50A1-69[»]
A82-149[»]
3L2OX-ray2.80A1-69[»]
A82-163[»]
4I6JX-ray2.70C1-163[»]
ProteinModelPortaliP63208.
SMRiP63208. Positions 3-160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63208.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni104 – 16360Interaction with the F-box domain of F-box proteinsBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the SKP1 family.Curated

Phylogenomic databases

eggNOGiCOG5201.
GeneTreeiENSGT00390000012652.
HOGENOMiHOG000172184.
HOVERGENiHBG057008.
InParanoidiP63208.
KOiK03094.
OMAiVIQWCTY.
OrthoDBiEOG7QVM4C.
PhylomeDBiP63208.
TreeFamiTF354233.

Family and domain databases

Gene3Di3.30.710.10. 1 hit.
InterProiIPR011333. BTB/POZ_fold.
IPR016897. E3_ubiquit_lig_SCF_Skp.
IPR001232. Skp1_comp.
IPR016072. Skp1_comp_dimer.
IPR016073. Skp1_comp_POZ.
[Graphical view]
PANTHERiPTHR11165. PTHR11165. 1 hit.
PfamiPF01466. Skp1. 1 hit.
PF03931. Skp1_POZ. 1 hit.
[Graphical view]
PIRSFiPIRSF028729. E3_ubiquit_lig_SCF_Skp. 1 hit.
SMARTiSM00512. Skp1. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
SSF81382. SSF81382. 1 hit.

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: P63208-1) [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

        10         20         30         40         50
MPSIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV
60 70 80 90 100
NAAILKKVIQ WCTHHKDDPP PPEDDENKEK RTDDIPVWDQ EFLKVDQGTL
110 120 130 140 150
FELILAANYL DIKGLLDVTC KTVANMIKGK TPEEIRKTFN IKNDFTEEEE
160
AQVRKENQWC EEK
Length:163
Mass (Da):18,658
Last modified:January 23, 2007 - v2
Checksum:iC794D62AFB75528A
GO
Isoform 2 (identifier: P63208-2) [UniParc] [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     154-163: RKENQWCEEK → GSTQFCL

Note: No experimental confirmation available.

Show »
Length:160
Mass (Da):18,063
Checksum:iA376AA50007A3D2D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141F → L.
Corresponds to variant rs11538034 [ dbSNP | Ensembl ].
VAR_051999

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei154 – 16310RKENQWCEEK → GSTQFCL in isoform 2. 1 PublicationVSP_007555

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33760 mRNA. Translation: AAC50241.1.
Z47087 mRNA. Translation: CAA87392.1.
CH471062 Genomic DNA. Translation: EAW62270.1.
CH471062 Genomic DNA. Translation: EAW62271.1.
CH471062 Genomic DNA. Translation: EAW62272.1.
CH471062 Genomic DNA. Translation: EAW62276.1.
BC009839 mRNA. Translation: AAH09839.1.
BC020798 mRNA. Translation: AAH20798.1.
BC025673 mRNA. Translation: AAH25673.1.
BC065730 mRNA. Translation: AAH65730.1.
U37558 mRNA. Translation: AAA79202.1.
CCDSiCCDS4171.1.
CCDS4172.1. [P63208-2]
PIRiI39170.
RefSeqiNP_008861.2. NM_006930.3. [P63208-2]
NP_733779.1. NM_170679.2. [P63208-1]
UniGeneiHs.171626.

Genome annotation databases

EnsembliENST00000353411; ENSP00000231487; ENSG00000113558. [P63208-1]
ENST00000517625; ENSP00000429961; ENSG00000113558. [P63208-1]
ENST00000522552; ENSP00000429472; ENSG00000113558. [P63208-2]
ENST00000522855; ENSP00000429686; ENSG00000113558. [P63208-1]
GeneIDi6500.
KEGGihsa:6500.
UCSCiuc003kzc.4. human.
uc003kzd.4. human. [P63208-2]

Polymorphism databases

DMDMi52783797.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33760 mRNA. Translation: AAC50241.1 .
Z47087 mRNA. Translation: CAA87392.1 .
CH471062 Genomic DNA. Translation: EAW62270.1 .
CH471062 Genomic DNA. Translation: EAW62271.1 .
CH471062 Genomic DNA. Translation: EAW62272.1 .
CH471062 Genomic DNA. Translation: EAW62276.1 .
BC009839 mRNA. Translation: AAH09839.1 .
BC020798 mRNA. Translation: AAH20798.1 .
BC025673 mRNA. Translation: AAH25673.1 .
BC065730 mRNA. Translation: AAH65730.1 .
U37558 mRNA. Translation: AAA79202.1 .
CCDSi CCDS4171.1.
CCDS4172.1. [P63208-2 ]
PIRi I39170.
RefSeqi NP_008861.2. NM_006930.3. [P63208-2 ]
NP_733779.1. NM_170679.2. [P63208-1 ]
UniGenei Hs.171626.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FQV X-ray 2.80 B/D/F/H/J/L/N/P 1-69 [» ]
B/D/F/H/J/L/N/P 83-163 [» ]
1FS1 X-ray 1.80 B/D 1-147 [» ]
1FS2 X-ray 2.90 B/D 1-147 [» ]
1LDK X-ray 3.10 D 2-140 [» ]
1P22 X-ray 2.95 B 1-163 [» ]
2ASS X-ray 3.00 A 2-160 [» ]
2AST X-ray 2.30 A 2-160 [» ]
2E31 X-ray 2.40 B 1-163 [» ]
2E32 X-ray 3.52 B/D 1-163 [» ]
2OVP X-ray 2.90 A 1-69 [» ]
A 82-149 [» ]
2OVQ X-ray 2.60 A 1-69 [» ]
A 82-149 [» ]
2OVR X-ray 2.50 A 1-69 [» ]
A 82-149 [» ]
3L2O X-ray 2.80 A 1-69 [» ]
A 82-163 [» ]
4I6J X-ray 2.70 C 1-163 [» ]
ProteinModelPortali P63208.
SMRi P63208. Positions 3-160.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112391. 162 interactions.
DIPi DIP-31606N.
IntActi P63208. 81 interactions.
MINTi MINT-5001195.
STRINGi 9606.ENSP00000231487.

PTM databases

PhosphoSitei P63208.

Polymorphism databases

DMDMi 52783797.

2D gel databases

SWISS-2DPAGE P63208.

Proteomic databases

MaxQBi P63208.
PaxDbi P63208.
PeptideAtlasi P63208.
PRIDEi P63208.

Protocols and materials databases

DNASUi 6500.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000353411 ; ENSP00000231487 ; ENSG00000113558 . [P63208-1 ]
ENST00000517625 ; ENSP00000429961 ; ENSG00000113558 . [P63208-1 ]
ENST00000522552 ; ENSP00000429472 ; ENSG00000113558 . [P63208-2 ]
ENST00000522855 ; ENSP00000429686 ; ENSG00000113558 . [P63208-1 ]
GeneIDi 6500.
KEGGi hsa:6500.
UCSCi uc003kzc.4. human.
uc003kzd.4. human. [P63208-2 ]

Organism-specific databases

CTDi 6500.
GeneCardsi GC05M133484.
H-InvDB HIX0129723.
HGNCi HGNC:10899. SKP1.
HPAi CAB012982.
HPA053745.
MIMi 601434. gene.
neXtProti NX_P63208.
PharmGKBi PA162403424.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5201.
GeneTreei ENSGT00390000012652.
HOGENOMi HOG000172184.
HOVERGENi HBG057008.
InParanoidi P63208.
KOi K03094.
OMAi VIQWCTY.
OrthoDBi EOG7QVM4C.
PhylomeDBi P63208.
TreeFami TF354233.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_115697. Prolactin receptor signaling.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_160305. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_206597. Degradation of GLI2 by the proteasome.
REACT_22442. Interleukin-1 signaling.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_24941. Circadian Clock.
REACT_267605. Degradation of GLI1 by the proteasome.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_821. Cyclin D associated events in G1.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.

Miscellaneous databases

ChiTaRSi SKP1. human.
EvolutionaryTracei P63208.
GeneWikii SKP1A.
GenomeRNAii 6500.
NextBioi 25267.
PROi P63208.
SOURCEi Search...

Gene expression databases

Bgeei P63208.
CleanExi HS_SKP1.
ExpressionAtlasi P63208. baseline and differential.
Genevestigatori P63208.

Family and domain databases

Gene3Di 3.30.710.10. 1 hit.
InterProi IPR011333. BTB/POZ_fold.
IPR016897. E3_ubiquit_lig_SCF_Skp.
IPR001232. Skp1_comp.
IPR016072. Skp1_comp_dimer.
IPR016073. Skp1_comp_POZ.
[Graphical view ]
PANTHERi PTHR11165. PTHR11165. 1 hit.
Pfami PF01466. Skp1. 1 hit.
PF03931. Skp1_POZ. 1 hit.
[Graphical view ]
PIRSFi PIRSF028729. E3_ubiquit_lig_SCF_Skp. 1 hit.
SMARTi SM00512. Skp1. 1 hit.
[Graphical view ]
SUPFAMi SSF54695. SSF54695. 1 hit.
SSF81382. SSF81382. 1 hit.
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).
  2. "A novel cDNA with homology to an RNA polymerase II elongation factors maps to human chromosome 5q31 (TCEB1L) and to mouse chromosome 11 (Tceb1l)."
    Sowden J., Morrison K., Schofield J., Putt W., Edwards Y.
    Genomics 29:145-151(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Lung, Skin and Uterus.
  5. Cited for: PROTEIN SEQUENCE OF 2-11.
    Tissue: Erythrocyte.
  6. Cited for: FUNCTION IN UBIQUITINATION OF BCL2, IDENTIFICATION IN THE SCF(FBXO10) COMPLEX.
  7. "Human inner ear OCP2 cDNA maps to 5q22-5q35.2 with related sequences on chromosomes 4p16.2-4p14, 5p13-5q22, 7pter-q22, 10 and 12p13-12qter."
    Liang Y., Chen H., Asher J.H. Jr., Chang C.-C., Friedman T.B.
    Gene 184:163-167(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-163 (ISOFORM 1).
    Tissue: Inner ear.
  8. "CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex."
    Dias D.C., Dolios G., Wang R., Pan Z.Q.
    Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBXW8, IDENTIFICATION IN SCF-LIKE COMPLEX.
  9. "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses."
    Matsuzawa S., Reed J.C.
    Mol. Cell 7:915-926(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT OF A COMPLEX WITH SIAH1; CACYBP; UBE2D1; APC AND TBL1X.
  10. "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.
  11. "Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases."
    Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.
    J. Biol. Chem. 283:12717-12729(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBXO44; FBXO17 AND FBXO27, IDENTIFICATION IN SCF-COMPLEX.
  12. "SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation."
    D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L., Washburn M.P., Dynlacht B., Pagano M.
    Nature 466:138-142(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SCF(CCNF) COMPLEX.
  13. "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 THR-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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 THR-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas."
    Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C., di Celle P.F., Chapuy B., Shipp M., Chiarle R., Pagano M.
    Nature 481:90-93(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF BCL6, IDENTIFICATION IN THE SCF(FBXO11) COMPLEX.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF THE SKP1-SKP2 COMPLEX.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH CUL1; RBX1 AND SKP2.
  19. "Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase."
    Wu G., Xu G., Schulman B.A., Jeffrey P.D., Harper J.W., Pavletich N.P.
    Mol. Cell 11:1445-1456(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH 176-606 OF BTRC AND CTNNB1.
  20. "Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase."
    Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M., Pavletich N.P.
    Mol. Cell 20:9-19(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-159 IN COMPLEX WITH SKP2; CKS1B AND CDKN1B PHOSPHOPEPTIDE, SUBUNIT, FUNCTION.
  21. "Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases."
    Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P.
    Mol. Cell 26:131-143(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FBXW7 AND CCNE1 PEPTIDE.
  22. "Structural basis for the selection of glycosylated substrates by SCF(Fbs1) ubiquitin ligase."
    Mizushima T., Yoshida Y., Kumanomidou T., Hasegawa Y., Suzuki A., Yamane T., Tanaka K.
    Proc. Natl. Acad. Sci. U.S.A. 104:5777-5781(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FBXO2.
  23. "Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase."
    Li Y., Hao B.
    J. Biol. Chem. 285:13896-13906(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FBXO4, FUNCTION.

Entry informationi

Entry nameiSKP1_HUMAN
AccessioniPrimary (citable) accession number: P63208
Secondary accession number(s): D3DQ97
, D3DQ98, P34991, Q8TAY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 123 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

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