Reviewed, UniProtKB/Swiss-Prot Q13309 (SKP2_HUMAN)

Names and origin

Protein names

Recommended name:
    S-phase kinase-associated protein 2
Alternative name(s):
    F-box protein Skp2
    Cyclin A/CDK2-associated protein p45
    p45skp2
    F-box/LRR-repeat protein 1

Gene names

Name:	SKP2
Synonyms:	FBXL1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 ORC1L, CDT1, RBL2, MLL, CDK9, RAG2, FOXO1A, UBP43, and probably MYC, TOB1 and TAL1. Degradation of TAL1 also requires STUB1. Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Part of the SCF(SKP2) complex consisting of CUL1, RBX1, SKP1 and SKP2. Interacts directly with CUL1 and SKP1. Interacts with CKS1. Interacts with the cyclin A-CDK2 complex. Interacts with ORC1L, phosphorylated CDT1, phosphorylated RBL2, ELF4, phosphorylated RAG2, FOXO1A, UBP43, MYC, TOB1, TAL1 and MLL. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.1 Ref.27
Sequence similarities	Contains 1 F-box domain. Contains 8 LRR (leucine-rich) repeats.
Sequence caution	The sequence BAB87202.1 differs from that shown. Reason: Miscellaneous discrepancy. Probable cloning artifact.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Leucine-rich repeat Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	G1/S transition of mitotic cell cycle Ref.1 Traceable author statement. Source: ProtInc cell proliferation Ref.1 Traceable author statement. Source: ProtInc modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Ref.8 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CKS1B	P61024	2	EBI-456291,EBI-456371
CUL1	Q13616	2	EBI-456291,EBI-359390
DUSP1	P28562	1	EBI-456291,EBI-975493
MYC	P01106	2	EBI-456291,EBI-447544
ORC1L	Q13415	2	EBI-456291,EBI-374847

Alternative products

This entry describes 2 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

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

180 – 204

25

LRR 1

Repeat

210 – 234

25

LRR 2

Repeat

258 – 284

27

LRR 3

Repeat

286 – 308

23

LRR 4

Repeat

309 – 330

22

LRR 5

Repeat

334 – 356

23

LRR 6

Repeat

359 – 378

20

LRR 7

Repeat

380 – 403

24

LRR 8

Amino acid modifications

Modified residue

64

1

Phosphoserine Ref.17 Ref.22 Ref.23 Ref.25

Modified residue

179

1

Phosphoserine Ref.21

Natural variations

Alternative sequence

355 – 424

70

ELGEI…KPSCL → LVTRAGVRIRLDSDIGCPQT YRTSKLKSSHKLFCQHVRVI CIFVCDFYFYRLVLKQ in isoform 2.

VSP_008432

Natural variant

85

1

P → L: dbSNP rs3913486.

VAR_016984

Natural variant

87

1

L → I: dbSNP rs3913487.

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...

Helix

102 – 109

8

Helix

114 – 116

3

Helix

117 – 121

5

Helix

125 – 131

7

Helix

134 – 136

3

Beta strand

138 – 141

4

Helix

149 – 157

9

Beta strand

161 – 164

4

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

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). 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

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: 7553852] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	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].
[6]	"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] (ISOFORM 2). Tissue: Placenta.
[7]	"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: 12435635] [Abstract] Cited for: INTERACTION WITH RBL2, FUNCTION IN UBIQUITINATION OF RBL2.
[8]	"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: 11931757] [Abstract] Cited for: INTERACTION WITH ORC1L, FUNCTION IN UBIQUITINATION OF ORC1L.
[9]	"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: 12840033] [Abstract] Cited for: INTERACTION WITH CDT1, FUNCTION IN UBIQUITINATION OF CDT1.
[10]	"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: 12769844] [Abstract] Cited for: INTERACTION WITH MYC, FUNCTION IN UBIQUITINATION OF MYC.
[11]	"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: 15342634] [Abstract] Cited for: INTERACTION WITH UBP43, FUNCTION IN UBIQUITINATION OF UBP43.
[12]	"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: 16262255] [Abstract] Cited for: FUNCTION IN UBIQUITINATION OF CDKN1A.
[13]	"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: 15949444] [Abstract] Cited for: INTERACTION WITH RAG2, FUNCTION IN UBIQUITINATION OF RAG2.
[14]	"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: 16103164] [Abstract] Cited for: FUNCTION IN UBIQUITINATION OF CDK9.
[15]	"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: 15668399] [Abstract] Cited for: INTERACTION WITH FOXO1A, FUNCTION IN UBIQUITINATION OF FOXO1A.
[16]	"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: 16951159] [Abstract] Cited for: INTERACTION WITH TOB1, FUNCTION IN UBIQUITINATION OF TOB1.
[17]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"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: 16581786] [Abstract] Cited for: INTERACTION WITH ELF4, FUNCTION IN UBIQUITINATION OF ELF4.
[19]	"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: 17908926] [Abstract] Cited for: INTERACTION WITH MLL, FUNCTION IN UBIQUITINATION OF MLL.
[20]	"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: 17962192] [Abstract] Cited for: INTERACTION WITH TAL1, FUNCTION IN UBIQUITINATION OF TAL1.
[21]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, MASS SPECTROMETRY.
[22]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY.
[23]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY.
[24]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[25]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY. Tissue: T-cell.
[26]	"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 101-153 IN COMPLEX WITH 1-147 OF SKP1.
[27]	"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 COMPLEX WITH CUL1; SKP1 AND RBX1, 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.
CH471119 Genomic DNA. Translation: EAW55936.1.
BC001441 mRNA. Translation: AAH01441.1.
BC007441 mRNA. Translation: AAH07441.1.

IPI

IPI00013294.
IPI00178899.

PIR

I39171.

RefSeq

NP_005974.2.
NP_116026.1.

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17011N.
DIP-17017N.

IntAct

Q13309. 8 interactions.

STRING

Q13309.

PTM databases

PhosphoSite

Q13309.

Proteomic databases

PRIDE

Q13309.

Genome annotation databases

Ensembl

ENST00000274255; ENSP00000274255; ENSG00000145604; Homo sapiens. [Genome view]

GeneID

6502.

KEGG

hsa:6502.

UCSC

uc003jkc.1. human.
uc003jkd.1. human.

Organism-specific databases

CTD

6502.

GeneCards

GC05P036187.

H-InvDB

HIX0004811.

HGNC

HGNC:10901. SKP2.

HPA

CAB013533.

MIM

601436. gene.

PharmGKB

PA35801.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16734.

HOVERGEN

Q13309.

OMA

ARPTVGN.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.

Gene expression databases

ArrayExpress

Q13309.

Bgee

Q13309.

CleanEx

HS_SKP2.

Genevestigator

Q13309.

GermOnline

ENSG00000145604. Homo sapiens.

Family and domain databases

InterPro

IPR001810. F-box.
[Graphical view]

Pfam

PF00646. F-box. 1 hit.
[Graphical view]

SMART

SM00256. FBOX. 1 hit.
[Graphical view]

PROSITE

PS50181. FBOX. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

25275.

SOURCE

Search...

Entry information

Entry name

SKP2_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	October 3, 2003
Last modified:	February 9, 2010
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.