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Protein

S-phase kinase-associated protein 1

Gene

Skp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_289448. Cyclin D associated events in G1.
REACT_289947. Prolactin receptor signaling.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_334977. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_337033. Interleukin-1 signaling.
REACT_341044. SCF-beta-TrCP mediated degradation of Emi1.
REACT_342086. SCF(Skp2)-mediated degradation of p27/p21.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_345278. Regulation of PLK1 Activity at G2/M Transition.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.
REACT_359269. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_359387. Degradation of GLI1 by the proteasome.
REACT_360804. CLEC7A (Dectin-1) signaling.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Skp1
Synonyms:Skp1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:103575. Skp1a.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: CACAO
  • Cul7-RING ubiquitin ligase complex Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: MGI
  • SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 163162S-phase kinase-associated protein 1PRO_0000187252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9WTX5.
PaxDbiQ9WTX5.
PRIDEiQ9WTX5.

2D gel databases

REPRODUCTION-2DPAGEQ9WTX5.

PTM databases

PhosphoSiteiQ9WTX5.

Expressioni

Gene expression databases

BgeeiQ9WTX5.
CleanExiMM_SKP1A.
ExpressionAtlasiQ9WTX5. baseline and differential.
GenevisibleiQ9WTX5. MM.

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 FBXW7.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ppp1caP621372EBI-1202363,EBI-357187
Rnf2Q9CQJ44EBI-1202363,EBI-927321

Protein-protein interaction databases

BioGridi203998. 30 interactions.
DIPiDIP-38596N.
IntActiQ9WTX5. 11 interactions.
MINTiMINT-4134768.
STRINGi10090.ENSMUSP00000038744.

Structurei

3D structure databases

ProteinModelPortaliQ9WTX5.
SMRiQ9WTX5. Positions 3-160.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ9WTX5.
KOiK03094.
OMAiICSWDAE.
PhylomeDBiQ9WTX5.
TreeFamiTF354233.

Family and domain databases

InterProiIPR011333. BTB/POZ_fold.
IPR016897. SKP1.
IPR001232. SKP1-like.
IPR016072. Skp1_comp_dimer.
IPR016073. Skp1_comp_POZ.
[Graphical view]
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.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WTX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTIKLQSSD 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):18,672
Last modified:January 23, 2007 - v3
Checksum:iAE184C00BE6556DB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411D → N in BAC37220 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS24669.1.
RefSeqiNP_035673.3. NM_011543.4.
XP_006532849.1. XM_006532786.2.
UniGeneiMm.42944.

Genome annotation databases

EnsembliENSMUST00000037324; ENSMUSP00000038744; ENSMUSG00000036309.
ENSMUST00000109072; ENSMUSP00000104700; ENSMUSG00000036309.
GeneIDi21402.
KEGGimmu:21402.
UCSCiuc007ivf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS24669.1.
RefSeqiNP_035673.3. NM_011543.4.
XP_006532849.1. XM_006532786.2.
UniGeneiMm.42944.

3D structure databases

ProteinModelPortaliQ9WTX5.
SMRiQ9WTX5. Positions 3-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203998. 30 interactions.
DIPiDIP-38596N.
IntActiQ9WTX5. 11 interactions.
MINTiMINT-4134768.
STRINGi10090.ENSMUSP00000038744.

PTM databases

PhosphoSiteiQ9WTX5.

2D gel databases

REPRODUCTION-2DPAGEQ9WTX5.

Proteomic databases

MaxQBiQ9WTX5.
PaxDbiQ9WTX5.
PRIDEiQ9WTX5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037324; ENSMUSP00000038744; ENSMUSG00000036309.
ENSMUST00000109072; ENSMUSP00000104700; ENSMUSG00000036309.
GeneIDi21402.
KEGGimmu:21402.
UCSCiuc007ivf.2. mouse.

Organism-specific databases

CTDi21402.
MGIiMGI:103575. Skp1a.

Phylogenomic databases

eggNOGiCOG5201.
GeneTreeiENSGT00390000012652.
HOGENOMiHOG000172184.
HOVERGENiHBG057008.
InParanoidiQ9WTX5.
KOiK03094.
OMAiICSWDAE.
PhylomeDBiQ9WTX5.
TreeFamiTF354233.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_289448. Cyclin D associated events in G1.
REACT_289947. Prolactin receptor signaling.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_334977. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_337033. Interleukin-1 signaling.
REACT_341044. SCF-beta-TrCP mediated degradation of Emi1.
REACT_342086. SCF(Skp2)-mediated degradation of p27/p21.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_345278. Regulation of PLK1 Activity at G2/M Transition.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.
REACT_359269. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_359387. Degradation of GLI1 by the proteasome.
REACT_360804. CLEC7A (Dectin-1) signaling.

Miscellaneous databases

NextBioi300668.
PROiQ9WTX5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WTX5.
CleanExiMM_SKP1A.
ExpressionAtlasiQ9WTX5. baseline and differential.
GenevisibleiQ9WTX5. MM.

Family and domain databases

InterProiIPR011333. BTB/POZ_fold.
IPR016897. SKP1.
IPR001232. SKP1-like.
IPR016072. Skp1_comp_dimer.
IPR016073. Skp1_comp_POZ.
[Graphical view]
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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  7. Cited for: INTERACTION WITH FBXO45.

Entry informationi

Entry nameiSKP1_MOUSE
AccessioniPrimary (citable) accession number: Q9WTX5
Secondary accession number(s): Q8C5H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.