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Q9WTX5 (SKP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
S-phase kinase-associated protein 1A
p19A
p19skp1
Gene names
Name:Skp1
Synonyms:Skp1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity. Ref.1 Ref.4 Ref.6

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.1 Ref.4 Ref.5 Ref.6 Ref.7

Sequence similarities

Belongs to the SKP1 family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 163162S-phase kinase-associated protein 1
PRO_0000187252

Regions

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

Amino acid modifications

Modified residue1311Phosphothreonine By similarity

Experimental info

Sequence conflict411D → N in BAC37220. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9WTX5 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AE184C00BE6556DB

FASTA16318,672
        10         20         30         40         50         60 
MPTIKLQSSD 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

References

« Hide 'large scale' references
[1]"Ubiquitin-dependent degradation of IkappaBalpha is mediated by a ubiquitin ligase Skp1/Cul 1/F-box protein FWD1."
Hatakeyama S., Kitagawa M., Nakayama K., Shirane M., Matsumoto M., Hattori K., Higashi H., Nakano H., Okumura K., Onoe K., Good R.A., Nakayama K.
Proc. Natl. Acad. Sci. U.S.A. 96:3859-3863(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL1; PHOSPHORYLATED NFKBIA AND BTRC.
Strain: C57BL/6J.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Brain, Head, Kidney, Olfactory bulb and Thymus.
[3]"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].
Strain: FVB/N.
Tissue: Mammary tumor.
[4]"Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP."
Spencer E., Jiang J., Chen Z.J.
Genes Dev. 13:284-294(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH PHOSPHORYLATED NFKBIA; BTRC AND RELA.
[5]"Characterization of a mouse gene (Fbxw6) that encodes a homologue of Caenorhabditis elegans SEL-10."
Maruyama S., Hatakeyama S., Nakayama K., Ishida N., Kawakami K., Nakayama K.
Genomics 78:214-222(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH BTRC AND CUL1.
[6]"E3 ubiquitin ligase that recognizes sugar chains."
Yoshida Y., Chiba T., Tokunaga F., Kawasaki H., Iwai K., Suzuki T., Ito Y., Matsuoka K., Yoshida M., Tanaka K., Tai T.
Nature 418:438-442(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Fbxo45, a novel ubiquitin ligase, regulates synaptic activity."
Tada H., Okano H.J., Takagi H., Shibata S., Yao I., Matsumoto M., Saiga T., Nakayama K.I., Kashima H., Takahashi T., Setou M., Okano H.
J. Biol. Chem. 285:3840-3849(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBXO45.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF083214 mRNA. Translation: AAD16036.1.
AK002983 mRNA. Translation: BAB22496.1.
AK010628 mRNA. Translation: BAB27074.1.
AK012498 mRNA. Translation: BAB28281.1.
AK014245 mRNA. Translation: BAB29222.1.
AK027909 mRNA. Translation: BAC25660.1.
AK078330 mRNA. Translation: BAC37220.1.
AK088339 mRNA. Translation: BAC40292.1.
BC002115 mRNA. Translation: AAH02115.1.
CCDSCCDS24669.1.
RefSeqNP_035673.3. NM_011543.4.
XP_006532849.1. XM_006532786.1.
UniGeneMm.42944.

3D structure databases

ProteinModelPortalQ9WTX5.
SMRQ9WTX5. Positions 3-160.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203998. 29 interactions.
DIPDIP-38596N.
IntActQ9WTX5. 11 interactions.
MINTMINT-4134768.

PTM databases

PhosphoSiteQ9WTX5.

2D gel databases

REPRODUCTION-2DPAGEQ9WTX5.

Proteomic databases

MaxQBQ9WTX5.
PaxDbQ9WTX5.
PRIDEQ9WTX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037324; ENSMUSP00000038744; ENSMUSG00000036309.
ENSMUST00000109072; ENSMUSP00000104700; ENSMUSG00000036309.
GeneID21402.
KEGGmmu:21402.
UCSCuc007ivf.2. mouse.

Organism-specific databases

CTD21402.
MGIMGI:103575. Skp1a.

Phylogenomic databases

eggNOGCOG5201.
GeneTreeENSGT00390000012652.
HOGENOMHOG000172184.
HOVERGENHBG057008.
InParanoidQ9WTX5.
KOK03094.
OMAVIQWCTY.
PhylomeDBQ9WTX5.
TreeFamTF354233.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9WTX5.
BgeeQ9WTX5.
CleanExMM_SKP1A.
GenevestigatorQ9WTX5.

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. mouse.
NextBio300668.
PROQ9WTX5.
SOURCESearch...

Entry information

Entry nameSKP1_MOUSE
AccessionPrimary (citable) accession number: Q9WTX5
Secondary accession number(s): Q8C5H6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot