Q13309 (SKP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-phase kinase-associated protein 2

Alternative name(s):
Cyclin-A/CDK2-associated protein p45
F-box protein Skp2
F-box/LRR-repeat protein 1
p45skp2

Gene names

Name:	SKP2
Synonyms:	FBXL1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1, CDT1, RBL2, MLL, CDK9, RAG2, FOXO1, UBP43, and probably MYC, TOB1 and TAL1. Degradation of TAL1 also requires STUB1. Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2. Promotes ubiquitination and destruction of CDH1 in a CK1-Dependent Manner, thereby regulating cell migration. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.30
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Part of a SCF(SKP2) complex consisting of CUL1, RBX1, SKP1 and SKP2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Interacts directly with CUL1 and SKP1. Interacts with CKS1. Interacts with the cyclin-A-CDK2 complex. Interacts with ORC1, phosphorylated CDT1, phosphorylated RBL2, ELF4, phosphorylated RAG2, FOXO1, UBP43, MYC, TOB1, TAL1 and MLL. Interacts with TRIM21. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.32
Subcellular location	Cytoplasm. Nucleus Ref.30.
Post-translational modification	Ubiquitinated by the APC/C complex, leading to its degradation by the proteasome. Deubiquitinated by USP13. Ref.28 Acetylation at Lys-68 and Lys-71 increases stability through impairment of APC/C-mediated proteolysis and promotes cytoplasmic retention. Deacetylated by SIRT3.
Sequence similarities	Contains 1 F-box domain. Contains 10 LRR (leucine-rich) repeats.
Sequence caution	The sequence AAC50242.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB87202.1 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Leucine-rich repeat Repeat
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G1 phase of mitotic cell cycle Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome G2/M transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara S phase of mitotic cell cycle Traceable author statement. Source: Reactome anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome cell proliferation Traceable author statement Ref.1. Source: ProtInc cellular response to cell-matrix adhesion Inferred from electronic annotation. Source: Compara positive regulation of intracellular estrogen receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara protein polyubiquitination Inferred from electronic annotation. Source: Compara regulation of cell cycle Inferred from electronic annotation. Source: Compara
Cellular_component	SCF ubiquitin ligase complex Inferred from direct assay Ref.20. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-456291,EBI-456291
Cdh1	P09803	2	EBI-456291,EBI-984420	From a different organism.
CDKN1B	P46527	2	EBI-456291,EBI-519280
CKS1B	P61024	3	EBI-456291,EBI-456371
CUL1	Q13616	8	EBI-456291,EBI-359390
DUSP1	P28562	3	EBI-456291,EBI-975493
EP300	Q09472	3	EBI-456291,EBI-447295
FZR1	Q9UM11	2	EBI-456291,EBI-724997
MYC	P01106	2	EBI-456291,EBI-447544
ORC1	Q13415	2	EBI-456291,EBI-374847
SIRT3	Q9NTG7	5	EBI-456291,EBI-724621
SKP1	P63208	6	EBI-456291,EBI-307486

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13309-1)

Also known as: SKP2-alpha;

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: Q13309-2)

Also known as: SKP2-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     355-424: ELGEIPTLKT...RLTLQKPSCL → LVTRAGVRIR...FYFYRLVLKQ

Isoform 3 (identifier: Q13309-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-169: Missing.
     180-224: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 424

424

S-phase kinase-associated protein 2

PRO_0000119954

Regions

Domain

94 – 140

47

F-box

Repeat

151 – 176

26

LRR 1

Repeat

177 – 204

28

LRR 2

Repeat

210 – 234

25

LRR 3

Repeat

235 – 257

23

LRR 4

Repeat

258 – 284

27

LRR 5

Repeat

286 – 308

23

LRR 6

Repeat

309 – 330

22

LRR 7

Repeat

334 – 356

23

LRR 8

Repeat

359 – 378

20

LRR 9

Repeat

380 – 401

22

LRR 10

Motif

67 – 73

7

Nuclear localization signal Ref.30

Amino acid modifications

Modified residue

64

1

Phosphoserine Ref.18 Ref.24 Ref.25 Ref.26 Ref.29

Modified residue

68

1

N6-acetyllysine; by p300/EP300 Ref.30

Modified residue

71

1

N6-acetyllysine; by p300/EP300 Ref.30

Modified residue

179

1

Phosphoserine Ref.23

Natural variations

Alternative sequence

1 – 169

169

Missing in isoform 3.

VSP_044931

Alternative sequence

180 – 224

45

Missing in isoform 3.

VSP_044932

Alternative sequence

355 – 424

70

ELGEI…KPSCL → LVTRAGVRIRLDSDIGCPQT YRTSKLKSSHKLFCQHVRVI CIFVCDFYFYRLVLKQ in isoform 2.

VSP_008432

Natural variant

85

1

P → L.
Corresponds to variant rs3913486 [ dbSNP | Ensembl ].

VAR_016984

Natural variant

87

1

L → I.
Corresponds to variant rs3913487 [ dbSNP | Ensembl ].

VAR_016985

Experimental info

Sequence conflict

185

1

H → D in AAC50242. Ref.1

Sequence conflict

215

1

Missing in AAC50242. Ref.1

Sequence conflict

238

1

S → P in AAC50242. Ref.1

Sequence conflict

241

1

S → P in AAC50242. Ref.1

Sequence conflict

244 – 247

4

SEFA → PKFP in AAC50242. Ref.1

Sequence conflict

251

1

L → F in AAC50242. Ref.1

Sequence conflict

256

1

S → P in AAC50242. Ref.1

Sequence conflict

268

1

D → N in AAC50242. Ref.1

Sequence conflict

285

1

I → M in AAC50242. Ref.1

Sequence conflict

319

1

D → N in AAC50242. Ref.1

Sequence conflict

332

1

F → S in AAC50242. Ref.1

Secondary structure

1

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424

Helix Strand Turn

Details...

Beta strand

97 – 100

4

Helix

102 – 109

8

Helix

114 – 116

3

Helix

117 – 121

5

Helix

125 – 131

7

Helix

134 – 136

3

Beta strand

137 – 141

5

Helix

149 – 157

9

Beta strand

161 – 164

4

Beta strand

180 – 182

3

Beta strand

185 – 187

3

Helix

195 – 202

8

Beta strand

209 – 212

4

Helix

220 – 226

7

Beta strand

233 – 236

4

Helix

245 – 254

10

Beta strand

260 – 262

3

Helix

271 – 280

10

Beta strand

287 – 289

3

Helix

294 – 296

3

Helix

299 – 308

10

Beta strand

313 – 316

4

Helix

325 – 333

9

Beta strand

339 – 341

3

Helix

350 – 358

9

Beta strand

364 – 366

3

Helix

376 – 382

7

Beta strand

386 – 389

4

Beta strand

402 – 404

3

Beta strand

415 – 417

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SKP2-alpha) [UniParc]. Last modified October 3, 2003. Version 2. Checksum: F29B7C338A7A37E9	FASTA	424	47,761
	10 20 30 40 50 60 MHRKHLQEIP DLSSNVATSF TWGWDSSKTS ELLSGMGVSA LEKEEPDSEN IPQELLSNLG 70 80 90 100 110 120 HPESPPRKRL KSKGSDKDFV IVRRPKLNRE NFPGVSWDSL PDELLLGIFS CLCLPELLKV 130 140 150 160 170 180 SGVCKRWYRL ASDESLWQTL DLTGKNLHPD VTGRLLSQGV IAFRCPRSFM DQPLAEHFSP 190 200 210 220 230 240 FRVQHMDLSN SVIEVSTLHG ILSQCSKLQN LSLEGLRLSD PIVNTLAKNS NLVRLNLSGC 250 260 270 280 290 300 SGFSEFALQT LLSSCSRLDE LNLSWCFDFT EKHVQVAVAH VSETITQLNL SGYRKNLQKS 310 320 330 340 350 360 DLSTLVRRCP NLVHLDLSDS VMLKNDCFQE FFQLNYLQHL SLSRCYDIIP ETLLELGEIP 370 380 390 400 410 420 TLKTLQVFGI VPDGTLQLLK EALPHLQINC SHFTTIARPT IGNKKNQEIW GIKCRLTLQK PSCL
	Isoform 2 (SKP2-beta) [UniParc]. Checksum: 8CB41CC9968695E3	FASTA	410	46,576
	10 20 30 40 50 60 MHRKHLQEIP DLSSNVATSF TWGWDSSKTS ELLSGMGVSA LEKEEPDSEN IPQELLSNLG 70 80 90 100 110 120 HPESPPRKRL KSKGSDKDFV IVRRPKLNRE NFPGVSWDSL PDELLLGIFS CLCLPELLKV 130 140 150 160 170 180 SGVCKRWYRL ASDESLWQTL DLTGKNLHPD VTGRLLSQGV IAFRCPRSFM DQPLAEHFSP 190 200 210 220 230 240 FRVQHMDLSN SVIEVSTLHG ILSQCSKLQN LSLEGLRLSD PIVNTLAKNS NLVRLNLSGC 250 260 270 280 290 300 SGFSEFALQT LLSSCSRLDE LNLSWCFDFT EKHVQVAVAH VSETITQLNL SGYRKNLQKS 310 320 330 340 350 360 DLSTLVRRCP NLVHLDLSDS VMLKNDCFQE FFQLNYLQHL SLSRCYDIIP ETLLLVTRAG 370 380 390 400 410 VRIRLDSDIG CPQTYRTSKL KSSHKLFCQH VRVICIFVCD FYFYRLVLKQ
	Isoform 3 [UniParc]. Checksum: 06BF227E9F6974C9	FASTA	210	23,763
	10 20 30 40 50 60 MDQPLAEHFS TLAKNSNLVR LNLSGCSGFS EFALQTLLSS CSRLDELNLS WCFDFTEKHV 70 80 90 100 110 120 QVAVAHVSET ITQLNLSGYR KNLQKSDLST LVRRCPNLVH LDLSDSVMLK NDCFQEFFQL 130 140 150 160 170 180 NYLQHLSLSR CYDIIPETLL ELGEIPTLKT LQVFGIVPDG TLQLLKEALP HLQINCSHFT 190 200 210 TIARPTIGNK KNQEIWGIKC RLTLQKPSCL

References

	« Hide 'large scale' referencesShow '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), PROTEIN SEQUENCE OF 6-19; 31-58; 80-86 AND 365-372, INTERACTION WITH CYCLIN A-CDK2 COMPLEX.
[2]	"Human SKP2-like protein." Yamaguchi T. Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Liver.
[3]	"Androgenic regulation of Skp2 in androgen-dependent and -independent LNCaP human prostate tumor cells." Kokontis J.M., Fukuchi J., Liao S. Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Prostatic carcinoma.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Thalamus.
[5]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORM 2). Tissue: Placenta.
[8]	"The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2)." Tedesco D., Lukas J., Reed S.I. Genes Dev. 16:2946-2957(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RBL2, FUNCTION IN UBIQUITINATION OF RBL2.
[9]	"Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication." Mendez J., Zou-Yang X.H., Kim S.Y., Hidaka M., Tansey W.P., Stillman B. Mol. Cell 9:481-491(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ORC1, FUNCTION IN UBIQUITINATION OF ORC1.
[10]	"The SCF(Skp2) ubiquitin ligase complex interacts with the human replication licensing factor Cdt1 and regulates Cdt1 degradation." Li X., Zhao Q., Liao R., Sun P., Wu X. J. Biol. Chem. 278:30854-30858(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDT1, FUNCTION IN UBIQUITINATION OF CDT1.
[11]	"The F-box protein Skp2 participates in c-Myc proteosomal degradation and acts as a cofactor for c-Myc-regulated transcription." von der Lehr N., Johansson S., Wu S., Bahram F., Castell A., Cetinkaya C., Hydbring P., Weidung I., Nakayama K., Nakayama K.I., Soderberg O., Kerppola T.K., Larsson L.G. Mol. Cell 11:1189-1200(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYC, FUNCTION IN UBIQUITINATION OF MYC.
[12]	"The ISG15 isopeptidase UBP43 is regulated by proteolysis via the SCFSkp2 ubiquitin ligase." Tokarz S., Berset C., La Rue J., Friedman K., Nakayama K., Nakayama K., Zhang D.E., Lanker S. J. Biol. Chem. 279:46424-46430(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UBP43, FUNCTION IN UBIQUITINATION OF UBP43.
[13]	"Ubiquitination of p21Cip1/WAF1 by SCFSkp2: substrate requirement and ubiquitination site selection." Wang W., Nacusi L., Sheaff R.J., Liu X. Biochemistry 44:14553-14564(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN UBIQUITINATION OF CDKN1A.
[14]	"Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J recombinase to the cell cycle." Jiang H., Chang F.C., Ross A.E., Lee J., Nakayama K., Nakayama K., Desiderio S. Mol. Cell 18:699-709(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAG2, FUNCTION IN UBIQUITINATION OF RAG2.
[15]	"Ubiquitylation of Cdk9 by Skp2 facilitates optimal Tat transactivation." Barboric M., Zhang F., Besenicar M., Plemenitas A., Peterlin B.M. J. Virol. 79:11135-11141(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN UBIQUITINATION OF CDK9.
[16]	"Skp2 inhibits FOXO1 in tumor suppression through ubiquitin-mediated degradation." Huang H., Regan K.M., Wang F., Wang D., Smith D.I., van Deursen J.M., Tindall D.J. Proc. Natl. Acad. Sci. U.S.A. 102:1649-1654(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FOXO1, FUNCTION IN UBIQUITINATION OF FOXO1.
[17]	"Degradation of Tob1 mediated by SCFSkp2-dependent ubiquitination." Hiramatsu Y., Kitagawa K., Suzuki T., Uchida C., Hattori T., Kikuchi H., Oda T., Hatakeyama S., Nakayama K.I., Yamamoto T., Konno H., Kitagawa M. Cancer Res. 66:8477-8483(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TOB1, FUNCTION IN UBIQUITINATION OF TOB1.
[18]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"The ETS protein MEF is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCFSkp2." Liu Y., Hedvat C.V., Mao S., Zhu X.H., Yao J., Nguyen H., Koff A., Nimer S.D. Mol. Cell. Biol. 26:3114-3123(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ELF4, FUNCTION IN UBIQUITINATION OF ELF4.
[20]	"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.
[21]	"Bimodal degradation of MLL by SCFSkp2 and APCCdc20 assures cell cycle execution: a critical regulatory circuit lost in leukemogenic MLL fusions." Liu H., Cheng E.H., Hsieh J.J. Genes Dev. 21:2385-2398(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MLL, FUNCTION IN UBIQUITINATION OF MLL.
[22]	"Ubiquitination and degradation of Tal1/SCL are induced by Notch signaling and depend on Skp2 and CHIP." Nie L., Wu H., Sun X.H. J. Biol. Chem. 283:684-692(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TAL1, FUNCTION IN UBIQUITINATION OF TAL1.
[23]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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 SER-64, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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].
[28]	"Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control." Chen M., Gutierrez G.J., Ronai Z.A. Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011) [PubMed] [Europe PMC] [Abstract] Cited for: DEUBIQUITINATION BY USP13.
[29]	"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 SER-64, MASS SPECTROMETRY.
[30]	"Acetylation-dependent regulation of Skp2 function." Inuzuka H., Gao D., Finley L.W., Yang W., Wan L., Fukushima H., Chin Y.R., Zhai B., Shaik S., Lau A.W., Wang Z., Gygi S.P., Nakayama K., Teruya-Feldstein J., Toker A., Haigis M.C., Pandolfi P.P., Wei W. Cell 150:179-193(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ACETYLATION AT LYS-68 AND LYS-71, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION.
[31]	"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 101-153 IN COMPLEX WITH 1-147 OF SKP1.
[32]	"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 COMPLEX WITH CUL1; SKP1 AND RBX1, LEUCINE-RICH REPEATS, INTERACTION WITH CKS1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U33761 mRNA. Translation: AAC50242.1. Different initiation.
AB050979 mRNA. Translation: BAB87200.1.
AB050980 mRNA. Translation: BAB87201.1.
AB050981 mRNA. Translation: BAB87202.1. Sequence problems.
AY029177 mRNA. Translation: AAK31593.1.
AK291255 mRNA. Translation: BAF83944.1.
AK296223 mRNA. Translation: BAG58946.1.
AC008942 Genomic DNA. No translation available.
CH471119 Genomic DNA. Translation: EAW55936.1.
BC001441 mRNA. Translation: AAH01441.1.
BC007441 mRNA. Translation: AAH07441.1.

IPI

IPI00013294.
IPI00178899.
IPI01012086.

PIR

I39171.

RefSeq

NP_001230049.1. NM_001243120.1.
NP_005974.2. NM_005983.3.
NP_116026.1. NM_032637.3.

UniGene

Hs.23348.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FQV	X-ray	2.80	A/C/E/G/I/K/M/O	89-424	[»]
1FS1	X-ray	1.80	A/C	89-141	[»]
1FS2	X-ray	2.90	A/C	89-398	[»]
1LDK	X-ray	3.10	E	97-137	[»]
2ASS	X-ray	3.00	B	89-424	[»]
2AST	X-ray	2.30	B	89-424	[»]

ProteinModelPortal

Q13309.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17011N.
DIP-17017N.
DIP-31091N.

IntAct

Q13309. 22 interactions.

MINT

MINT-152160.

STRING

9606.ENSP00000274255.

PTM databases

PhosphoSite

Q13309.

Polymorphism databases

DMDM

37537922.

Proteomic databases

PaxDb

Q13309.

PRIDE

Q13309.

Protocols and materials databases

DNASU

6502.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000274254; ENSP00000274254; ENSG00000145604.
ENST00000274255; ENSP00000274255; ENSG00000145604.
ENST00000546211; ENSP00000443492; ENSG00000145604.

GeneID

6502.

KEGG

hsa:6502.

UCSC

uc003jkc.2. human.
uc003jkd.3. human.

Organism-specific databases

CTD

6502.

GeneCards

GC05P036103.

HGNC

HGNC:10901. SKP2.

HPA

CAB013533.

MIM

601436. gene.

neXtProt

NX_Q13309.

PharmGKB

PA35801.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG263321.

HOGENOM

HOG000247037.

HOVERGEN

HBG047488.

KO

K03875.

OMA

TIARPTV.

Enzyme and pathway databases

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.
foxopathway. FoxO family signaling.

Reactome

REACT_115566. Cell Cycle.
REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q13309.

Bgee

Q13309.

CleanEx

HS_SKP2.

Genevestigator

Q13309.

GermOnline

ENSG00000145604. Homo sapiens.

Family and domain databases

InterPro

IPR001810. F-box_dom_cyclin-like.
[Graphical view]

SMART

SM00256. FBOX. 1 hit.
[Graphical view]

SUPFAM

SSF81383. F-box_dom_Skp2-like. 1 hit.

PROSITE

PS50181. FBOX. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q13309.

GenomeRNAi

6502.

NextBio

25275.

SOURCE

Search...

Entry information

Entry name

SKP2_HUMAN

Accession

Primary (citable) accession number: Q13309
Secondary accession number(s): A8K5E0 , B4DJT4, Q8TDZ0, Q8TDZ1, Q9BV69

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	October 3, 2003
Last modified:	May 1, 2013
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.