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P63208 (SKP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. 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
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
p19A
p19skp1
Gene names
Name:SKP1
Synonyms:EMC19, OCP2, SKP1A, TCEB1L
OrganismHomo sapiens (Human)
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. 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(Cyclin F) directs ubiquitination of CP110. Ref.16 Ref.19

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Component of an E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC. Part of a SCF(BTRC)-like complex lacking CUL1, which is associated with phosphorylated NFKBIA and RELA; RELA interacts directly with NFKBIA. Component of the SCF(FBXO44) complex, composed of SKP1, CUL1 and FBXO44. Identified in a complex with SKP2, CKS1B and CDKN1B. Interacts with the cyclin A/CDK2 complex. Part of a SCF-like complex consisting of CUL7, RBX1, SKP1 and FBXW8. Part of several SCF complexes containing SKP1 and one of the F-box proteins. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Interacts with FBXO2, FBXO4, FBXW7 and TRIM21. Interacts with FBXO45 By similarity. 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(Cyclin F) complex consisting of CUL1, RBX1, SKP1 and CCNF. Ref.7 Ref.8 Ref.9 Ref.10 Ref.16

Sequence similarities

Belongs to the SKP1 family.

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

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: 7553852] [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: 8530064] [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: 15489334] [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]"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: 9031623] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-163 (ISOFORM 1).
Tissue: Inner ear.
[7]"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: 12481031] [Abstract]
Cited for: INTERACTION WITH FBXW8, IDENTIFICATION IN SCF-LIKE COMPLEX.
[8]"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: 11389839] [Abstract]
Cited for: SUBUNIT OF A COMPLEX WITH SIAH1; CACYBP; UBE2D1; APC AND TBL1X.
[9]"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: 16880511] [Abstract]
Cited for: INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, INTERACTION WITH TRIM21.
[10]"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: 18203720] [Abstract]
Cited for: INTERACTION WITH FBXO44; FBXO17 AND FBXO27, IDENTIFICATION IN SCF-COMPLEX.
[11]"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: 20596027] [Abstract]
Cited for: IDENTIFICATION IN THE SCF(CYCLIN F) COMPLEX.
[12]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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: 11099048] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF THE SKP1-SKP2 COMPLEX.
[14]"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: 11961546] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH CUL1; RBX1 AND SKP2.
[15]"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: 12820959] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH 176-606 OF BTRC AND CTNNB1.
[16]"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: 16209941] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-159 IN COMPLEX WITH SKP2; CKS1B AND CDKN1B PHOSPHOPEPTIDE, SUBUNIT, FUNCTION.
[17]"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: 17434132] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FBXW7 AND CCNE PEPTIDE.
[18]"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: 17389369] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FBXO2.
[19]"Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase."
Li Y., Hao B.
J. Biol. Chem. 285:13896-13906(2010) [PubMed: 20181953] [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.
IPIIPI00172421.
IPI00301364.
PIRI39170.
RefSeqNP_008861.2. NM_006930.3.
NP_733779.1. NM_170679.2.
UniGeneHs.171626.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQVX-ray2.80B/D/F/H/J/L/N/P1-163[»]
1FS1X-ray1.80B/D1-147[»]
1FS2X-ray2.90B/D1-147[»]
1LDKX-ray3.10D2-140[»]
1P22X-ray2.95B1-163[»]
2ASSX-ray3.00A3-159[»]
2ASTX-ray2.30A3-159[»]
2E31X-ray2.40B1-163[»]
2E32X-ray3.52B/D1-163[»]
2OVPX-ray2.90A1-163[»]
2OVQX-ray2.60A1-163[»]
2OVRX-ray2.50A1-163[»]
3L2OX-ray2.80A3-163[»]
ProteinModelPortalP63208.
SMRP63208. Positions 3-160.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-17012N.
DIP-31606N.
IntActP63208. 41 interactions.
MINTMINT-5001195.
STRINGP63208.

PTM databases

PhosphoSiteP63208.

Polymorphism databases

DMDM52783797.

2D gel databases

SWISS-2DPAGEP63208.

Proteomic databases

PeptideAtlasP63208.
PRIDEP63208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353411; ENSP00000231487; ENSG00000113558.
GeneID6500.
KEGGhsa:6500.
UCSCuc003kzc.2. human.
uc003kzd.2. human.

Organism-specific databases

CTD6500.
GeneCardsGC05M133521.
H-InvDBHIX0200736.
HGNCHGNC:10899. SKP1.
HPACAB012982.
MIM601434. gene.
neXtProtNX_P63208.
PharmGKBPA162403424.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG20930.
HOGENOMHBG622018.
HOVERGENHBG057008.
InParanoidP63208.
OMASWDVEFL.
OrthoDBEOG498V26.
PhylomeDBP63208.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_152. Cell Cycle, Mitotic.
REACT_24941. Circadian Clock.
REACT_6185. HIV Infection.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP63208.
BgeeP63208.
CleanExHS_SKP1.
GenevestigatorP63208.
GermOnlineENSG00000113558. Homo sapiens.

Family and domain databases

InterProIPR011333. BTB/POZ_fold.
IPR016897. E3_ubiquit_lig_SCF_Skp.
IPR001232. Skp1_comp.
IPR016072. Skp1_comp_dimer.
IPR016073. Skp1_comp_POZ.
[Graphical view]
Gene3DG3DSA:3.30.710.10. BTB/POZ_fold. 1 hit.
KOK03094.
PANTHERPTHR11165. Skp1. 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. BTB/POZ_fold. 1 hit.
SSF81382. Skp1_comp_dimer. 1 hit.
ProtoNetSearch...

Other

NextBio25267.
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: January 25, 2012
This is version 92 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.

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

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families