P63208 (SKP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-phase kinase-associated protein 1

Alternative name(s):
Cyclin-A/CDK2-associated protein p19
Organ of Corti protein 2
Short name=OCP-2
Organ of Corti protein II
Short name=OCP-II
RNA polymerase II elongation factor-like protein
SIII
Transcription elongation factor B
p19A
p19skp1

Gene names

Name:	SKP1
Synonyms:	EMC19, OCP2, SKP1A, TCEB1L

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	163 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) 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. Ref.18 Ref.21
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein as substrate-specific subunit. Component of the SCF(FBXW11) complex containing FBXW11. Component of the SCF(SKP2) complex containing SKP2, in which it interacts directly with SKP1, SKP2 and RBX1. Component of the SCF(FBXW2) complex containing FBXw2. Component of the SCF(FBXO32) complex containing FBXO32. Component of the probable SCF(FBXO7) complex containing FBXO7. Component of the SCF(FBXO11) complex containing FBXO11. Component of the SCF(FBXO25) complex containing FBXO25. Component of the SCF(FBXO33) complex containing FBXO33. Component of the probable SCF(FBXO4) complex containing FBXO4. Component of the SCF(FBXO44) complex, composed of SKP1, CUL1 and FBXO44. Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC. This complex binds phosphorylated NFKBIA. Part of a SCF complex consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Component of the SCF(FBXO17) complex, composed of SKP1, CUL1 and FBXO17. Component of the SCF(FBXO27) complex, composed of SKP1, CUL1 and FBXO27. Component of the SCF(CCNF) complex consisting of CUL1, RBX1, SKP1 and CCNF. Component of the SCF(FBXL3) complex composed of CUL1, SKP1, RBX1 and FBXL3. Component of the SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21. Component of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Component of the SCF(FBXW7) composed of CUL1, SKP1, RBX1 and FBXW7. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.18
Sequence similarities	Belongs to the SKP1 family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
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 Notch signaling pathway Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay PubMed 15103331PubMed 20347421. Source: UniProtKB anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome histone H2A monoubiquitination Inferred from direct assay PubMed 16943429. Source: UniProtKB positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	SCF ubiquitin ligase complex Inferred from direct assay PubMed 15103331Ref.9PubMed 20347421Ref.11PubMed 21572392PubMed 21725316PubMed 23263282. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ubiquitin-protein ligase activity Inferred from direct assay PubMed 20347421. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BTRC	Q9Y297	4	EBI-307486,EBI-307461
CCNF	P41002	6	EBI-307486,EBI-1207574
CUL1	Q13616	6	EBI-307486,EBI-359390
FBXL8	Q96CD0	3	EBI-307486,EBI-2321097
FBXO11	Q86XK2	2	EBI-307486,EBI-1047804
FBXO46	Q6PJ61	3	EBI-307486,EBI-2322982
FBXO7	Q9Y3I1	2	EBI-307486,EBI-1161222
FBXW11	Q9UKB1	4	EBI-307486,EBI-355189
FBXW2	Q9UKT8	2	EBI-307486,EBI-914727
FBXW5	Q969U6	3	EBI-307486,EBI-741068
FBXW9	Q5XUX1	3	EBI-307486,EBI-2322729
PPP1CA	P62136	3	EBI-307486,EBI-357253
SKP2	Q13309	6	EBI-307486,EBI-456291

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P63208-1)

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: P63208-2)

The sequence of this isoform differs from the canonical sequence as follows:
     154-163: RKENQWCEEK → GSTQFCL

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 163

162

S-phase kinase-associated protein 1

PRO_0000187251

Regions

Region

104 – 163

60

Interaction with the F-box domain of F-box proteins By similarity

Amino acid modifications

Modified residue

131

1

Phosphothreonine Ref.12 Ref.14

Natural variations

Alternative sequence

154 – 163

10

RKENQWCEEK → GSTQFCL in isoform 2.

VSP_007555

Natural variant

14

1

F → L.
Corresponds to variant rs11538034 [ dbSNP | Ensembl ].

VAR_051999

Secondary structure

1

.

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163

Helix Strand Turn

Details...

Beta strand

3 – 7

5

Beta strand

13 – 17

5

Helix

18 – 22

5

Helix

25 – 33

9

Beta strand

43 – 46

4

Beta strand

47 – 50

4

Helix

52 – 65

14

Beta strand

81 – 83

3

Helix

87 – 92

6

Helix

97 – 110

14

Helix

113 – 127

15

Beta strand

128 – 130

3

Helix

132 – 138

7

Helix

149 – 156

8

Turn

157 – 159

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: C794D62AFB75528A	FASTA	163	18,658
	10 20 30 40 50 60 MPSIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV NAAILKKVIQ 70 80 90 100 110 120 WCTHHKDDPP PPEDDENKEK RTDDIPVWDQ EFLKVDQGTL FELILAANYL DIKGLLDVTC 130 140 150 160 KTVANMIKGK TPEEIRKTFN IKNDFTEEEE AQVRKENQWC EEK
	Isoform 2 [UniParc] [UniParc]. Checksum: A376AA50007A3D2D	FASTA	160	18,063
	10 20 30 40 50 60 MPSIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV NAAILKKVIQ 70 80 90 100 110 120 WCTHHKDDPP PPEDDENKEK RTDDIPVWDQ EFLKVDQGTL FELILAANYL DIKGLLDVTC 130 140 150 160 KTVANMIKGK TPEEIRKTFN IKNDFTEEEE AQVGSTQFCL

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).
[2]	"A novel cDNA with homology to an RNA polymerase II elongation factors maps to human chromosome 5q31 (TCEB1L) and to mouse chromosome 11 (Tceb1l)." Sowden J., Morrison K., Schofield J., Putt W., Edwards Y. Genomics 29:145-151(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] (ISOFORMS 1 AND 2). Tissue: Lung, Skin and Uterus.
[5]	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 Cited for: PROTEIN SEQUENCE OF 2-11. Tissue: Erythrocyte.
[6]	"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." Liang Y., Chen H., Asher J.H. Jr., Chang C.-C., Friedman T.B. Gene 184:163-167(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-163 (ISOFORM 1). Tissue: Inner ear.
[7]	"CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex." Dias D.C., Dolios G., Wang R., Pan Z.Q. Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FBXW8, IDENTIFICATION IN SCF-LIKE COMPLEX.
[8]	"Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses." Matsuzawa S., Reed J.C. Mol. Cell 7:915-926(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT OF A COMPLEX WITH SIAH1; CACYBP; UBE2D1; APC AND TBL1X.
[9]	"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.
[10]	"Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases." Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L. J. Biol. Chem. 283:12717-12729(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FBXO44; FBXO17 AND FBXO27, IDENTIFICATION IN SCF-COMPLEX.
[11]	"SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation." D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L., Washburn M.P., Dynlacht B., Pagano M. Nature 466:138-142(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SCF(CCNF) COMPLEX.
[12]	"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 THR-131, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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].
[14]	"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 THR-131, MASS SPECTROMETRY.
[15]	"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 THE SKP1-SKP2 COMPLEX.
[16]	"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 SCF COMPLEX WITH CUL1; RBX1 AND SKP2.
[17]	"Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase." Wu G., Xu G., Schulman B.A., Jeffrey P.D., Harper J.W., Pavletich N.P. Mol. Cell 11:1445-1456(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH 176-606 OF BTRC AND CTNNB1.
[18]	"Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase." Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M., Pavletich N.P. Mol. Cell 20:9-19(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-159 IN COMPLEX WITH SKP2; CKS1B AND CDKN1B PHOSPHOPEPTIDE, SUBUNIT, FUNCTION.
[19]	"Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases." Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P. Mol. Cell 26:131-143(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FBXW7 AND CCNE PEPTIDE.
[20]	"Structural basis for the selection of glycosylated substrates by SCF(Fbs1) ubiquitin ligase." Mizushima T., Yoshida Y., Kumanomidou T., Hasegawa Y., Suzuki A., Yamane T., Tanaka K. Proc. Natl. Acad. Sci. U.S.A. 104:5777-5781(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FBXO2.
[21]	"Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase." Li Y., Hao B. J. Biol. Chem. 285:13896-13906(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FBXO4, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U33760 mRNA. Translation: AAC50241.1.
Z47087 mRNA. Translation: CAA87392.1.
CH471062 Genomic DNA. Translation: EAW62270.1.
CH471062 Genomic DNA. Translation: EAW62271.1.
CH471062 Genomic DNA. Translation: EAW62272.1.
CH471062 Genomic DNA. Translation: EAW62276.1.
BC009839 mRNA. Translation: AAH09839.1.
BC020798 mRNA. Translation: AAH20798.1.
BC025673 mRNA. Translation: AAH25673.1.
BC065730 mRNA. Translation: AAH65730.1.
U37558 mRNA. Translation: AAA79202.1.

IPI

IPI00172421.
IPI00301364.

PIR

I39170.

RefSeq

NP_008861.2. NM_006930.3.
NP_733779.1. NM_170679.2.

UniGene

Hs.171626.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FQV	X-ray	2.80	B/D/F/H/J/L/N/P	1-163	[»]
1FS1	X-ray	1.80	B/D	1-147	[»]
1FS2	X-ray	2.90	B/D	1-147	[»]
1LDK	X-ray	3.10	D	2-140	[»]
1P22	X-ray	2.95	B	1-163	[»]
2ASS	X-ray	3.00	A	3-159	[»]
2AST	X-ray	2.30	A	3-159	[»]
2E31	X-ray	2.40	B	1-163	[»]
2E32	X-ray	3.52	B/D	1-163	[»]
2OVP	X-ray	2.90	A	1-163	[»]
2OVQ	X-ray	2.60	A	1-163	[»]
2OVR	X-ray	2.50	A	1-163	[»]
3L2O	X-ray	2.80	A	3-163	[»]
4I6J	X-ray	2.70	C	1-163	[»]

ProteinModelPortal

P63208.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31606N.

IntAct

P63208. 52 interactions.

MINT

MINT-5001195.

STRING

9606.ENSP00000231487.

PTM databases

PhosphoSite

P63208.

Polymorphism databases

DMDM

52783797.

2D gel databases

SWISS-2DPAGE

P63208.

Proteomic databases

PaxDb

P63208.

PeptideAtlas

P63208.

PRIDE

P63208.

Protocols and materials databases

DNASU

6500.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000353411; ENSP00000231487; ENSG00000113558.
ENST00000517625; ENSP00000429961; ENSG00000113558.
ENST00000522552; ENSP00000429472; ENSG00000113558.
ENST00000522855; ENSP00000429686; ENSG00000113558.

GeneID

6500.

KEGG

hsa:6500.

UCSC

uc003kzc.4. human.
uc003kzd.4. human.

Organism-specific databases

CTD

6500.

GeneCards

GC05M133521.

H-InvDB

HIX0129723.

HGNC

HGNC:10899. SKP1.

HPA

CAB012982.

MIM

601434. gene.

neXtProt

NX_P63208.

PharmGKB

PA162403424.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5201.

HOGENOM

HOG000172184.

HOVERGEN

HBG057008.

InParanoid

P63208.

KO

K03094.

OMA

VIQWCTY.

OrthoDB

EOG498V26.

PhylomeDB

P63208.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_24941. Circadian Clock.
REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

P63208.

Bgee

P63208.

CleanEx

HS_SKP1.

Genevestigator

P63208.

GermOnline

ENSG00000113558. Homo sapiens.

Family and domain databases

Gene3D

3.30.710.10. 1 hit.

InterPro

IPR011333. BTB/POZ_fold.
IPR016897. E3_ubiquit_lig_SCF_Skp.
IPR001232. Skp1_comp.
IPR016072. Skp1_comp_dimer.
IPR016073. Skp1_comp_POZ.
[Graphical view]

PANTHER

PTHR11165. PTHR11165. 1 hit.

Pfam

PF01466. Skp1. 1 hit.
PF03931. Skp1_POZ. 1 hit.
[Graphical view]

PIRSF

PIRSF028729. E3_ubiquit_lig_SCF_Skp. 1 hit.

SMART

SM00512. Skp1. 1 hit.
[Graphical view]

SUPFAM

SSF54695. BTB/POZ_fold. 1 hit.
SSF81382. Skp1_comp_dimer. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

SKP1. human.

EvolutionaryTrace

P63208.

GenomeRNAi

6500.

NextBio

25267.

SOURCE

Search...

Entry information

Entry name

SKP1_HUMAN

Accession

Primary (citable) accession number: P63208
Secondary accession number(s): D3DQ97 , D3DQ98, P34991, Q8TAY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 105 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.