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S-phase kinase-associated protein 1 (Cyclin-A/CDK2-associated protein p19) (p19A) (Organ of Corti protein 2) (OCP-2) (Organ of Corti protein II) (OCP-II) (RNA polymerase II elongation factor-like protein) (SIII) (Transcription elongation factor B polypeptide 1-like) (p19skp1)

 SKP1_HUMAN              Reviewed;         163 AA.
P63208; D3DQ97; D3DQ98; P34991; Q8TAY2;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 154.
RecName: Full=S-phase kinase-associated protein 1;
AltName: Full=Cyclin-A/CDK2-associated protein p19;
Short=p19A;
AltName: Full=Organ of Corti protein 2;
Short=OCP-2;
AltName: Full=Organ of Corti protein II;
Short=OCP-II;
AltName: Full=RNA polymerase II elongation factor-like protein;
AltName: Full=SIII;
AltName: Full=Transcription elongation factor B polypeptide 1-like;
AltName: Full=p19skp1;
Name=SKP1; Synonyms=EMC19, OCP2, SKP1A, TCEB1L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7553852; DOI=10.1016/0092-8674(95)90271-6;
Zhang H., Kobayashi R., Galaktionov K., Beach D.;
"p19Skp1 and p45Skp2 are essential elements of the cyclin A-CDK2 S
phase kinase.";
Cell 82:915-925(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8530064; DOI=10.1006/geno.1995.1225;
Sowden J., Morrison K., Schofield J., Putt W., Edwards Y.;
"A novel cDNA with homology to an RNA polymerase II elongation factors
maps to human chromosome 5q31 (TCEB1L) and to mouse chromosome 11
(Tceb1l).";
Genomics 29:145-151(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-11.
TISSUE=Erythrocyte;
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.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[9]
FUNCTION IN UBIQUITINATION OF BCL2, AND IDENTIFICATION IN THE
SCF(FBXO10) COMPLEX.
PubMed=23431138; DOI=10.1073/pnas.1217271110;
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.;
"Related F-box proteins control cell death in Caenorhabditis elegans
and human lymphoma.";
Proc. Natl. Acad. Sci. U.S.A. 110:3943-3948(2013).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-163 (ISOFORM 1).
TISSUE=Inner ear;
PubMed=9031623; DOI=10.1016/S0378-1119(96)00590-2;
Liang Y., Chen H., Asher J.H. Jr., Chang C.-C., Friedman T.B.;
"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.";
Gene 184:163-167(1997).
[11]
INTERACTION WITH FBXW8, AND IDENTIFICATION IN SCF-LIKE COMPLEX.
PubMed=12481031; DOI=10.1073/pnas.252646399;
Dias D.C., Dolios G., Wang R., Pan Z.Q.;
"CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to
form an SCF-like complex.";
Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002).
[12]
SUBUNIT OF A COMPLEX WITH SIAH1; CACYBP; UBE2D1; APC AND TBL1X.
PubMed=11389839; DOI=10.1016/S1097-2765(01)00242-8;
Matsuzawa S., Reed J.C.;
"Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin
degradation linked to p53 responses.";
Mol. Cell 7:915-926(2001).
[13]
INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, AND INTERACTION WITH
TRIM21.
PubMed=16880511; DOI=10.1128/MCB.01630-05;
Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M.,
Krek W.;
"Regulation of p27 degradation and S-phase progression by Ro52 RING
finger protein.";
Mol. Cell. Biol. 26:5994-6004(2006).
[14]
INTERACTION WITH FBXO44; FBXO17 AND FBXO27, AND IDENTIFICATION IN
SCF-COMPLEX.
PubMed=18203720; DOI=10.1074/jbc.M709508200;
Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.;
"Diversity in tissue expression, substrate binding, and SCF complex
formation for a lectin family of ubiquitin ligases.";
J. Biol. Chem. 283:12717-12729(2008).
[15]
IDENTIFICATION IN THE SCF(CCNF) COMPLEX.
PubMed=20596027; DOI=10.1038/nature09140;
D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L.,
Washburn M.P., Dynlacht B., Pagano M.;
"SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity
through CP110 degradation.";
Nature 466:138-142(2010).
[16]
FUNCTION IN UBIQUITINATION OF BCL6, AND IDENTIFICATION IN THE
SCF(FBXO11) COMPLEX.
PubMed=22113614; DOI=10.1038/nature10688;
Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C.,
di Celle P.F., Chapuy B., Shipp M., Chiarle R., Pagano M.;
"FBXO11 targets BCL6 for degradation and is inactivated in diffuse
large B-cell lymphomas.";
Nature 481:90-93(2012).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[19]
FUNCTION.
PubMed=25704143; DOI=10.1016/j.ejcb.2015.01.004;
Man X., Megraw T.L., Lim Y.P.;
"Cep68 can be regulated by Nek2 and SCF complex.";
Eur. J. Cell Biol. 94:162-172(2015).
[20]
INTERACTION WITH CEP68.
PubMed=25503564; DOI=10.1038/ncb3076;
Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V.,
Florens L., Washburn M.P., Pagano M.;
"Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from
the PCM to allow centriole separation, disengagement and licensing.";
Nat. Cell Biol. 17:31-43(2015).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF THE SKP1-SKP2 COMPLEX.
PubMed=11099048; DOI=10.1038/35042620;
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.;
"Insights into SCF ubiquitin ligases from the structure of the Skp1-
Skp2 complex.";
Nature 408:381-386(2000).
[23]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH CUL1; RBX1
AND SKP2.
PubMed=11961546; DOI=10.1038/416703a;
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.;
"Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase
complex.";
Nature 416:703-709(2002).
[24]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH 176-606 OF BTRC
AND CTNNB1.
PubMed=12820959; DOI=10.1016/S1097-2765(03)00234-X;
Wu G., Xu G., Schulman B.A., Jeffrey P.D., Harper J.W.,
Pavletich N.P.;
"Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction
motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin
ligase.";
Mol. Cell 11:1445-1456(2003).
[25]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-159 IN COMPLEX WITH SKP2;
CKS1B AND CDKN1B PHOSPHOPEPTIDE, SUBUNIT, AND FUNCTION.
PubMed=16209941; DOI=10.1016/j.molcel.2005.09.003;
Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M.,
Pavletich N.P.;
"Structural basis of the Cks1-dependent recognition of p27(Kip1) by
the SCF(Skp2) ubiquitin ligase.";
Mol. Cell 20:9-19(2005).
[26]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FBXW7 AND CCNE1
PEPTIDE.
PubMed=17434132; DOI=10.1016/j.molcel.2007.02.022;
Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P.;
"Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated
substrate recognition by SCF ubiquitin ligases.";
Mol. Cell 26:131-143(2007).
[27]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FBXO2.
PubMed=17389369; DOI=10.1073/pnas.0610312104;
Mizushima T., Yoshida Y., Kumanomidou T., Hasegawa Y., Suzuki A.,
Yamane T., Tanaka K.;
"Structural basis for the selection of glycosylated substrates by
SCF(Fbs1) ubiquitin ligase.";
Proc. Natl. Acad. Sci. U.S.A. 104:5777-5781(2007).
[28]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FBXO4, AND
FUNCTION.
PubMed=20181953; DOI=10.1074/jbc.M110.111518;
Li Y., Hao B.;
"Structural basis of dimerization-dependent ubiquitination by the
SCF(Fbx4) ubiquitin ligase.";
J. Biol. Chem. 285:13896-13906(2010).
-!- 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, CEP68 and probably NFKB2 (PubMed:25704143). 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)
directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs
ubiquitination of BCL2. {ECO:0000269|PubMed:16209941,
ECO:0000269|PubMed:20181953, ECO:0000269|PubMed:22113614,
ECO:0000269|PubMed:23431138, ECO:0000269|PubMed:25704143}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: 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. Interacts with CEP68 (PubMed:25503564).
{ECO:0000269|PubMed:11389839, ECO:0000269|PubMed:12481031,
ECO:0000269|PubMed:12820959, ECO:0000269|PubMed:16209941,
ECO:0000269|PubMed:16880511, ECO:0000269|PubMed:17389369,
ECO:0000269|PubMed:17434132, ECO:0000269|PubMed:18203720,
ECO:0000269|PubMed:20181953, ECO:0000269|PubMed:20596027,
ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23431138,
ECO:0000269|PubMed:25503564}.
-!- INTERACTION:
Q6TVJ2:- (xeno); NbExp=2; IntAct=EBI-307497, EBI-15718764;
Q6TVJ4:- (xeno); NbExp=2; IntAct=EBI-307497, EBI-15718558;
Q6TVJ7:- (xeno); NbExp=2; IntAct=EBI-307497, EBI-15718586;
Q6TVW2:- (xeno); NbExp=5; IntAct=EBI-307497, EBI-15718527;
Q96IX9:ANKRD36BP1; NbExp=3; IntAct=EBI-307486, EBI-744859;
Q96GX9:APIP; NbExp=3; IntAct=EBI-307486, EBI-359248;
Q9Y297:BTRC; NbExp=6; IntAct=EBI-307486, EBI-307461;
P41002:CCNF; NbExp=6; IntAct=EBI-307486, EBI-1207574;
P38936:CDKN1A; NbExp=3; IntAct=EBI-307486, EBI-375077;
P35222:CTNNB1; NbExp=3; IntAct=EBI-307486, EBI-491549;
Q13616:CUL1; NbExp=10; IntAct=EBI-307486, EBI-359390;
Q9NXK8:FBXL12; NbExp=8; IntAct=EBI-307486, EBI-719790;
Q9UKC9:FBXL2; NbExp=5; IntAct=EBI-307486, EBI-724253;
Q96IG2:FBXL20; NbExp=3; IntAct=EBI-307486, EBI-8835647;
Q8BFZ4:Fbxl21 (xeno); NbExp=3; IntAct=EBI-307486, EBI-6898235;
Q8C4V4:Fbxl3 (xeno); NbExp=3; IntAct=EBI-307486, EBI-1266589;
Q9UKA1:FBXL5; NbExp=12; IntAct=EBI-307486, EBI-2692340;
Q96CD0:FBXL8; NbExp=14; IntAct=EBI-307486, EBI-2321097;
Q86XK2:FBXO11; NbExp=6; IntAct=EBI-307486, EBI-1047804;
Q96EF6:FBXO17; NbExp=14; IntAct=EBI-307486, EBI-2510157;
Q9UK22:FBXO2; NbExp=10; IntAct=EBI-307486, EBI-4287196;
Q80UW2:Fbxo2 (xeno); NbExp=4; IntAct=EBI-307497, EBI-2314714;
Q8NEZ5:FBXO22; NbExp=6; IntAct=EBI-307486, EBI-2510137;
Q8TCJ0-3:FBXO25; NbExp=3; IntAct=EBI-307486, EBI-6262578;
Q8NI29:FBXO27; NbExp=6; IntAct=EBI-307486, EBI-6425694;
Q9NVF7:FBXO28; NbExp=7; IntAct=EBI-307486, EBI-740282;
Q9UK99:FBXO3; NbExp=9; IntAct=EBI-307486, EBI-2509901;
Q7Z6M2:FBXO33; NbExp=2; IntAct=EBI-307486, EBI-8555452;
Q9UKT5:FBXO4; NbExp=9; IntAct=EBI-307486, EBI-960409;
Q9H4M3:FBXO44; NbExp=5; IntAct=EBI-307486, EBI-2322644;
Q9H4M3-2:FBXO44; NbExp=4; IntAct=EBI-307486, EBI-12104696;
Q6PJ61:FBXO46; NbExp=4; IntAct=EBI-307486, EBI-2322982;
Q5FWF7:FBXO48; NbExp=6; IntAct=EBI-307486, EBI-11961122;
Q9NRD1:FBXO6; NbExp=3; IntAct=EBI-307486, EBI-3938499;
Q9Y3I1:FBXO7; NbExp=7; IntAct=EBI-307486, EBI-1161222;
Q9UK97:FBXO9; NbExp=2; IntAct=EBI-307486, EBI-2869927;
Q9UKB1:FBXW11; NbExp=7; IntAct=EBI-307486, EBI-355189;
Q9UKT8:FBXW2; NbExp=4; IntAct=EBI-307486, EBI-914727;
P57775:FBXW4; NbExp=2; IntAct=EBI-307486, EBI-2372268;
Q969U6:FBXW5; NbExp=4; IntAct=EBI-307486, EBI-741068;
Q969U6-1:FBXW5; NbExp=3; IntAct=EBI-307497, EBI-16031873;
Q969H0:FBXW7; NbExp=5; IntAct=EBI-307486, EBI-359574;
Q8N3Y1:FBXW8; NbExp=2; IntAct=EBI-307486, EBI-914770;
Q5XUX1:FBXW9; NbExp=4; IntAct=EBI-307486, EBI-2322729;
Q7L273:KCTD9; NbExp=3; IntAct=EBI-307486, EBI-4397613;
Q9Y2K7:KDM2A; NbExp=2; IntAct=EBI-307486, EBI-765758;
Q8NHM5:KDM2B; NbExp=2; IntAct=EBI-307486, EBI-3955564;
P25791:LMO2; NbExp=3; IntAct=EBI-307486, EBI-739696;
Q13503:MED21; NbExp=5; IntAct=EBI-307497, EBI-394678;
Q14901:MYC; NbExp=2; IntAct=EBI-307486, EBI-7982457;
P62136:PPP1CA; NbExp=3; IntAct=EBI-307486, EBI-357253;
Q13309:SKP2; NbExp=13; IntAct=EBI-307486, EBI-456291;
Q13309-1:SKP2; NbExp=7; IntAct=EBI-307497, EBI-15490084;
Q9Y2Z0-2:SUGT1; NbExp=2; IntAct=EBI-307486, EBI-10768076;
A0A0B4J1Y2:TTC21A; NbExp=3; IntAct=EBI-307486, EBI-10220701;
Q8N5M4:TTC9C; NbExp=8; IntAct=EBI-307486, EBI-2851213;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P63208-1, P34991-1;
Sequence=Displayed;
Name=2;
IsoId=P63208-2, P34991-2;
Sequence=VSP_007555;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U33760; AAC50241.1; -; mRNA.
EMBL; Z47087; CAA87392.1; -; mRNA.
EMBL; CH471062; EAW62270.1; -; Genomic_DNA.
EMBL; CH471062; EAW62271.1; -; Genomic_DNA.
EMBL; CH471062; EAW62272.1; -; Genomic_DNA.
EMBL; CH471062; EAW62276.1; -; Genomic_DNA.
EMBL; BC009839; AAH09839.1; -; mRNA.
EMBL; BC020798; AAH20798.1; -; mRNA.
EMBL; BC025673; AAH25673.1; -; mRNA.
EMBL; BC065730; AAH65730.1; -; mRNA.
EMBL; U37558; AAA79202.1; -; mRNA.
CCDS; CCDS4171.1; -.
CCDS; CCDS4172.1; -. [P63208-2]
PIR; I39170; I39170.
RefSeq; NP_008861.2; NM_006930.3. [P63208-2]
RefSeq; NP_733779.1; NM_170679.2. [P63208-1]
UniGene; Hs.171626; -.
PDB; 1FQV; X-ray; 2.80 A; B/D/F/H/J/L/N/P=1-69, B/D/F/H/J/L/N/P=83-163.
PDB; 1FS1; X-ray; 1.80 A; B/D=1-147.
PDB; 1FS2; X-ray; 2.90 A; B/D=1-147.
PDB; 1LDK; X-ray; 3.10 A; D=2-140.
PDB; 1P22; X-ray; 2.95 A; B=1-163.
PDB; 2ASS; X-ray; 3.00 A; A=2-160.
PDB; 2AST; X-ray; 2.30 A; A=2-160.
PDB; 2E31; X-ray; 2.40 A; B=1-163.
PDB; 2E32; X-ray; 3.52 A; B/D=1-163.
PDB; 2OVP; X-ray; 2.90 A; A=1-69, A=82-149.
PDB; 2OVQ; X-ray; 2.60 A; A=1-69, A=82-149.
PDB; 2OVR; X-ray; 2.50 A; A=1-69, A=82-149.
PDB; 3L2O; X-ray; 2.80 A; A=1-69, A=82-163.
PDB; 3WSO; X-ray; 2.60 A; B=1-163.
PDB; 4I6J; X-ray; 2.70 A; C=1-163.
PDB; 5IBK; X-ray; 2.50 A; A/D=1-69, A/D=82-163.
PDB; 5JH5; X-ray; 2.55 A; B=2-163.
PDB; 5K35; X-ray; 2.85 A; B=1-163.
PDBsum; 1FQV; -.
PDBsum; 1FS1; -.
PDBsum; 1FS2; -.
PDBsum; 1LDK; -.
PDBsum; 1P22; -.
PDBsum; 2ASS; -.
PDBsum; 2AST; -.
PDBsum; 2E31; -.
PDBsum; 2E32; -.
PDBsum; 2OVP; -.
PDBsum; 2OVQ; -.
PDBsum; 2OVR; -.
PDBsum; 3L2O; -.
PDBsum; 3WSO; -.
PDBsum; 4I6J; -.
PDBsum; 5IBK; -.
PDBsum; 5JH5; -.
PDBsum; 5K35; -.
ProteinModelPortal; P63208; -.
SMR; P63208; -.
BioGrid; 112391; 252.
CORUM; P63208; -.
DIP; DIP-31606N; -.
IntAct; P63208; 174.
MINT; MINT-5001195; -.
STRING; 9606.ENSP00000231487; -.
DrugBank; DB06980; (2S)-2-(1H-indol-3-yl)hexanoic acid.
DrugBank; DB06981; (2S)-2-(1H-indol-3-yl)pentanoic acid.
DrugBank; DB06982; (2S)-8-[(tert-butoxycarbonyl)amino]-2-(1H-indol-3-yl)octanoic acid.
DrugBank; DB07950; 1H-INDOL-3-YLACETIC ACID.
DrugBank; DB01750; Naphthalen-1-Yl-Acetic Acid.
iPTMnet; P63208; -.
PhosphoSitePlus; P63208; -.
SwissPalm; P63208; -.
BioMuta; SKP1; -.
DMDM; 52783797; -.
SWISS-2DPAGE; P63208; -.
EPD; P63208; -.
MaxQB; P63208; -.
PaxDb; P63208; -.
PeptideAtlas; P63208; -.
PRIDE; P63208; -.
TopDownProteomics; P63208-1; -. [P63208-1]
DNASU; 6500; -.
Ensembl; ENST00000353411; ENSP00000231487; ENSG00000113558. [P63208-1]
Ensembl; ENST00000517625; ENSP00000429961; ENSG00000113558. [P63208-1]
Ensembl; ENST00000522552; ENSP00000429472; ENSG00000113558. [P63208-2]
Ensembl; ENST00000522855; ENSP00000429686; ENSG00000113558. [P63208-1]
GeneID; 6500; -.
KEGG; hsa:6500; -.
UCSC; uc003kzc.5; human.
CTD; 6500; -.
DisGeNET; 6500; -.
EuPathDB; HostDB:ENSG00000113558.18; -.
GeneCards; SKP1; -.
H-InvDB; HIX0129723; -.
HGNC; HGNC:10899; SKP1.
HPA; CAB012982; -.
HPA; HPA053745; -.
HPA; HPA058134; -.
MIM; 601434; gene.
neXtProt; NX_P63208; -.
OpenTargets; ENSG00000113558; -.
PharmGKB; PA162403424; -.
eggNOG; KOG1724; Eukaryota.
eggNOG; COG5201; LUCA.
GeneTree; ENSGT00390000012652; -.
HOGENOM; HOG000172184; -.
HOVERGEN; HBG057008; -.
InParanoid; P63208; -.
KO; K03094; -.
OMA; ENKWCEE; -.
OrthoDB; EOG091G0OU2; -.
PhylomeDB; P63208; -.
TreeFam; TF354233; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1170546; Prolactin receptor signaling.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2644607; Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-917937; Iron uptake and transport.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; P63208; -.
UniPathway; UPA00143; -.
ChiTaRS; SKP1; human.
EvolutionaryTrace; P63208; -.
GeneWiki; SKP1A; -.
GenomeRNAi; 6500; -.
PRO; PR:P63208; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113558; -.
CleanEx; HS_SKP1; -.
ExpressionAtlas; P63208; baseline and differential.
Genevisible; P63208; HS.
GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IDA:ParkinsonsUK-UCL.
GO; GO:0097602; F:cullin family protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
GO; GO:0051457; P:maintenance of protein location in nucleus; IPI:ParkinsonsUK-UCL.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0010265; P:SCF complex assembly; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
InterPro; IPR016897; SKP1.
InterPro; IPR001232; SKP1-like.
InterPro; IPR036296; SKP1-like_dim_sf.
InterPro; IPR011333; SKP1/BTB/POZ.
InterPro; IPR016072; Skp1_comp_dimer.
InterPro; IPR016073; Skp1_comp_POZ.
Pfam; PF01466; Skp1; 1.
Pfam; PF03931; Skp1_POZ; 1.
PIRSF; PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1.
SMART; SM00512; Skp1; 1.
SUPFAM; SSF54695; SSF54695; 1.
SUPFAM; SSF81382; SSF81382; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Isopeptide bond; Phosphoprotein;
Reference proteome; Ubl conjugation; Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.5}.
CHAIN 2 163 S-phase kinase-associated protein 1.
/FTId=PRO_0000187251.
REGION 104 163 Interaction with the F-box domain of F-
box proteins. {ECO:0000250}.
MOD_RES 131 131 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 142 142 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
VAR_SEQ 154 163 RKENQWCEEK -> GSTQFCL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_007555.
STRAND 3 7 {ECO:0000244|PDB:1FS1}.
STRAND 9 12 {ECO:0000244|PDB:4I6J}.
STRAND 13 17 {ECO:0000244|PDB:1FS1}.
HELIX 18 22 {ECO:0000244|PDB:1FS1}.
HELIX 25 33 {ECO:0000244|PDB:1FS1}.
STRAND 44 46 {ECO:0000244|PDB:1FS1}.
STRAND 47 50 {ECO:0000244|PDB:1LDK}.
HELIX 52 65 {ECO:0000244|PDB:1FS1}.
HELIX 87 92 {ECO:0000244|PDB:1FS1}.
HELIX 97 110 {ECO:0000244|PDB:1FS1}.
HELIX 113 127 {ECO:0000244|PDB:1FS1}.
STRAND 128 130 {ECO:0000244|PDB:1FQV}.
HELIX 132 138 {ECO:0000244|PDB:1FS1}.
HELIX 149 156 {ECO:0000244|PDB:2AST}.
TURN 157 159 {ECO:0000244|PDB:2AST}.
SEQUENCE 163 AA; 18658 MW; C794D62AFB75528A CRC64;
MPSIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV NAAILKKVIQ
WCTHHKDDPP PPEDDENKEK RTDDIPVWDQ EFLKVDQGTL FELILAANYL DIKGLLDVTC
KTVANMIKGK TPEEIRKTFN IKNDFTEEEE AQVRKENQWC EEK


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