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P63208 (SKP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. 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 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 names
Name:SKP1
Synonyms:EMC19, OCP2, SKP1A, TCEB1L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length163 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.16 Ref.20 Ref.23

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.16 Ref.20

Sequence similarities

Belongs to the SKP1 family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
   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

Traceable author statement. Source: Reactome

Notch signaling pathway

Traceable author statement. Source: Reactome

SCF-dependent proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 15103331PubMed 20347421. Source: UniProtKB

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

Traceable author statement. Source: Reactome

histone H2A monoubiquitination

Inferred from direct assay PubMed 16943429. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein ubiquitination

Inferred from direct assay PubMed 15103331. Source: UniProtKB

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentCul7-RING ubiquitin ligase complex

Inferred from direct assay PubMed 21572988. Source: UniProtKB

SCF ubiquitin ligase complex

Inferred from direct assay PubMed 15103331Ref.10PubMed 20347421Ref.12PubMed 21572392PubMed 21725316PubMed 23263282. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionprotein binding

Inferred from physical interaction Ref.10PubMed 16943429Ref.11PubMed 19996097Ref.23PubMed 20347421. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay PubMed 20347421. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P63208-1)

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: P63208-2)

The sequence of this isoform differs from the canonical sequence as follows:
     154-163: RKENQWCEEK → GSTQFCL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 163162S-phase kinase-associated protein 1
PRO_0000187251

Regions

Region104 – 16360Interaction with the F-box domain of F-box proteins By similarity

Amino acid modifications

Modified residue1311Phosphothreonine Ref.13 Ref.15

Natural variations

Alternative sequence154 – 16310RKENQWCEEK → GSTQFCL in isoform 2.
VSP_007555
Natural variant141F → L.
Corresponds to variant rs11538034 [ dbSNP | Ensembl ].
VAR_051999

Secondary structure

.......................... 163
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 2.
Checksum: C794D62AFB75528A

FASTA16318,658
        10         20         30         40         50         60 
MPSIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV NAAILKKVIQ 

        70         80         90        100        110        120 
WCTHHKDDPP PPEDDENKEK RTDDIPVWDQ EFLKVDQGTL FELILAANYL DIKGLLDVTC 

       130        140        150        160 
KTVANMIKGK TPEEIRKTFN IKNDFTEEEE AQVRKENQWC EEK 

« Hide

Isoform 2 [UniParc] [UniParc].

Checksum: A376AA50007A3D2D
Show »

FASTA16018,063

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).
[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]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., Pasquali C., Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., Balant L., Hochstrasser D.F.
Submitted (FEB-1994) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11.
Tissue: Erythrocyte.
[6]"Related F-box proteins control cell death in Caenorhabditis elegans and human lymphoma."
Chiorazzi M., Rui L., Yang Y., Ceribelli M., Tishbi N., Maurer C.W., Ranuncolo S.M., Zhao H., Xu W., Chan W.C., Jaffe E.S., Gascoyne R.D., Campo E., Rosenwald A., Ott G., Delabie J., Rimsza L.M., Shaham S., Staudt L.M.
Proc. Natl. Acad. Sci. U.S.A. 110:3943-3948(2013) [PubMed] [Europe PMC] [Abstract]
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]"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].
[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]"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 THE SKP1-SKP2 COMPLEX.
[18]"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 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4171.1.
CCDS4172.1. [P63208-2]
PIRI39170.
RefSeqNP_008861.2. NM_006930.3. [P63208-2]
NP_733779.1. NM_170679.2. [P63208-1]
UniGeneHs.171626.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP63208.
SMRP63208. Positions 3-160.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112391. 152 interactions.
DIPDIP-31606N.
IntActP63208. 75 interactions.
MINTMINT-5001195.
STRING9606.ENSP00000231487.

PTM databases

PhosphoSiteP63208.

Polymorphism databases

DMDM52783797.

2D gel databases

SWISS-2DPAGEP63208.

Proteomic databases

MaxQBP63208.
PaxDbP63208.
PeptideAtlasP63208.
PRIDEP63208.

Protocols and materials databases

DNASU6500.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353411; ENSP00000231487; ENSG00000113558. [P63208-1]
ENST00000517625; ENSP00000429961; ENSG00000113558. [P63208-1]
ENST00000522552; ENSP00000429472; ENSG00000113558. [P63208-2]
ENST00000522855; ENSP00000429686; ENSG00000113558. [P63208-1]
GeneID6500.
KEGGhsa:6500.
UCSCuc003kzc.4. human.
uc003kzd.4. human. [P63208-2]

Organism-specific databases

CTD6500.
GeneCardsGC05M133521.
H-InvDBHIX0129723.
HGNCHGNC:10899. SKP1.
HPACAB012982.
HPA053745.
MIM601434. gene.
neXtProtNX_P63208.
PharmGKBPA162403424.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5201.
HOGENOMHOG000172184.
HOVERGENHBG057008.
InParanoidP63208.
KOK03094.
OMAVIQWCTY.
OrthoDBEOG7QVM4C.
PhylomeDBP63208.
TreeFamTF354233.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_24941. Circadian Clock.
REACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressP63208.
BgeeP63208.
CleanExHS_SKP1.
GenevestigatorP63208.

Family and domain databases

Gene3D3.30.710.10. 1 hit.
InterProIPR011333. BTB/POZ_fold.
IPR016897. E3_ubiquit_lig_SCF_Skp.
IPR001232. Skp1_comp.
IPR016072. Skp1_comp_dimer.
IPR016073. Skp1_comp_POZ.
[Graphical view]
PANTHERPTHR11165. PTHR11165. 1 hit.
PfamPF01466. Skp1. 1 hit.
PF03931. Skp1_POZ. 1 hit.
[Graphical view]
PIRSFPIRSF028729. E3_ubiquit_lig_SCF_Skp. 1 hit.
SMARTSM00512. Skp1. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
SSF81382. SSF81382. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSKP1. human.
EvolutionaryTraceP63208.
GeneWikiSKP1A.
GenomeRNAi6500.
NextBio25267.
PROP63208.
SOURCESearch...

Entry information

Entry nameSKP1_HUMAN
AccessionPrimary (citable) accession number: P63208
Secondary accession number(s): D3DQ97 expand/collapse secondary AC list , D3DQ98, P34991, Q8TAY2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 119 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