Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13098 (CSN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
COP9 signalosome complex subunit 1

Short name=SGN1
Short name=Signalosome subunit 1
Alternative name(s):
G protein pathway suppressor 1
Short name=GPS-1
JAB1-containing signalosome subunit 1
Protein MFH
Gene names
Name:GPS1
Synonyms:COPS1, CSN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Suppresses G-protein- and mitogen-activated protein kinase-mediated signal transduction. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

Subunit structure

Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COP6, COPS7 (COPS7A or COPS7B) and COPS8. In the complex, it probably interacts directly with COPS2, COPS3, COPS4 and CSN5. Interacts directly with inositol kinase ITPK1. Interacts with CAPN8 By similarity. Ref.8 Ref.10 Ref.15

Subcellular location

Cytoplasm. Nucleus Ref.6.

Tissue specificity

Widely expressed. Ref.1

Domain

The PCI domain is necessary and sufficient for the interactions with other CSN subunits of the complex. Mediates the interaction with CAPN8 By similarity. Ref.8

The N-terminal part (1-216), which is not required for deneddylating activity and CSN complex formation, is nevertheless essential for other aspects of CSN complex function, such as repression of c-fos/FOS expression. Ref.8

Sequence similarities

Belongs to the CSN1 family.

Contains 1 PCI domain.

Sequence caution

The sequence AAC50906.2 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

COPS5Q929053EBI-725197,EBI-594661

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13098-4)

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 4 (identifier: Q13098-5)

The sequence of this isoform differs from the canonical sequence as follows:
     103-106: Missing.
Isoform 3 (identifier: Q13098-6)

The sequence of this isoform differs from the canonical sequence as follows:
     12-109: GAVEPMQIDV...EATRSSLREL → PASSVSGSGG...QIDVDPQEDP
     471-491: REGSQGELTPANSQSRMSTNM → TSTDLGPPGG...VRCRQVGGVH
Note: No experimental confirmation available.
Isoform 2 (identifier: Q13098-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MPLPVQVFNLQ → MRDSSAPSSASSSVTDLYCTPHSSRSDLVLPGTAGDFSLSASLSACTLLYE
     103-106: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 491490COP9 signalosome complex subunit 1
PRO_0000120959

Regions

Domain324 – 428105PCI

Amino acid modifications

Modified residue4681Phosphoserine Ref.15 Ref.21
Modified residue4741Phosphoserine Ref.15 Ref.16 Ref.19 Ref.21
Modified residue4791Phosphothreonine Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.21
Modified residue4831Phosphoserine Ref.15 Ref.16

Natural variations

Alternative sequence1 – 1111MPLPVQVFNLQ → MRDSSAPSSASSSVTDLYCT PHSSRSDLVLPGTAGDFSLS ASLSACTLLYE in isoform 2.
VSP_036240
Alternative sequence12 – 10998GAVEP…SLREL → PASSVSGSGGAESQDRMRDS SAPSSASSSVTDLYCTPHSS RSDLVLPGMAGDFSLSASLS ACTLLYEGAVEPMQIDVDPQ EDP in isoform 3.
VSP_036241
Alternative sequence103 – 1064Missing in isoform 2 and isoform 4.
VSP_036242
Alternative sequence471 – 49121REGSQ…MSTNM → TSTDLGPPGGSVLPAAQLRG LATGCHPACVPSLGLRRQAA ASCGPSWKERPAGLDPVGFC PQGADCAAPRPSGTISQTPP VPASVRCRQVGGVH in isoform 3.
VSP_011882

Experimental info

Sequence conflict2591A → T in BAC04120. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 10, 2009. Version 4.
Checksum: BF925164ED985638

FASTA49155,537
        10         20         30         40         50         60 
MPLPVQVFNL QGAVEPMQID VDPQEDPQNA PDVNYVVENP SLDLEQYAAS YSGLMRIERL 

        70         80         90        100        110        120 
QFIADHCPTL RVEALKMALS FVQRTFNVDM YEEIHRKLSE ATRSSLRELQ NAPDAIPESG 

       130        140        150        160        170        180 
VEPPALDTAW VEATRKKALL KLEKLDTDLK NYKGNSIKES IRRGHDDLGD HYLDCGDLSN 

       190        200        210        220        230        240 
ALKCYSRARD YCTSAKHVIN MCLNVIKVSV YLQNWSHVLS YVSKAESTPE IAEQRGERDS 

       250        260        270        280        290        300 
QTQAILTKLK CAAGLAELAA RKYKQAAKCL LLASFDHCDF PELLSPSNVA IYGGLCALAT 

       310        320        330        340        350        360 
FDRQELQRNV ISSSSFKLFL ELEPQVRDII FKFYESKYAS CLKMLDEMKD NLLLDMYLAP 

       370        380        390        400        410        420 
HVRTLYTQIR NRALIQYFSP YVSADMHRMA AAFNTTVAAL EDELTQLILE GLISARVDSH 

       430        440        450        460        470        480 
SKILYARDVD QRSTTFEKSL LMGKEFQRRA KAMMLRAAVL RNQIHVKSPP REGSQGELTP 

       490 
ANSQSRMSTN M 

« Hide

Isoform 4 [UniParc].

Checksum: 8E706F5C8E4763A5
Show »

FASTA48755,093
Isoform 3 [UniParc].

Checksum: B0C46F7860CB480E
Show »

FASTA54959,818
Isoform 2 [UniParc].

Checksum: 6081BEBD48CAF32C
Show »

FASTA52759,050

References

« Hide 'large scale' references
[1]"Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11), suppress G-protein- and mitogen-activated protein kinase-mediated signal transduction in yeast and mammalian cells."
Spain B.H., Bowdish K.S., Pacal A., Flueckiger Staub S., Koo D., Chang K.-Y.R., Xie W., Colicelli J.
Mol. Cell. Biol. 16:6698-6706(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY.
[2]"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. expand/collapse author list , 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] (ISOFORM 3).
Tissue: Testis.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
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: Placenta and Prostate.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-491 (ISOFORM 1).
[6]"A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits."
Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R., Schade R., Gordon C., Naumann M., Dubiel W.
FASEB J. 12:469-478(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
[7]"COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system."
Bech-Otschir D., Kraft R., Huang X., Henklein P., Kapelari B., Pollmann C., Dubiel W.
EMBO J. 20:1630-1639(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The subunit 1 of the COP9 signalosome suppresses gene expression through its N-terminal domain and incorporates into the complex through the PCI domain."
Tsuge T., Matsui M., Wei N.
J. Mol. Biol. 305:1-9(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, INTERACTION WITH COPS2; COPS3 AND COPS4.
[9]"Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome."
Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C., Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.
Science 292:1382-1385(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPOSITION OF THE CSN COMPLEX.
[10]"Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1."
Sun Y., Wilson M.P., Majerus P.W.
J. Biol. Chem. 277:45759-45764(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITPK1.
[11]"The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage."
Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.
Cell 113:357-367(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome."
Uhle S., Medalia O., Waldron R., Dumdey R., Henklein P., Bech-Otschir D., Huang X., Berse M., Sperling J., Schade R., Dubiel W.
EMBO J. 22:1302-1312(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[15]"Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry."
Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.
J. Proteome Res. 7:4914-4925(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT SER-468; SER-474; THR-479 AND SER-483.
[16]"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-474; THR-479 AND SER-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"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-474 AND THR-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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].
[21]"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-468; SER-474 AND THR-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U20285 mRNA. Translation: AAC50906.2. Different initiation.
AK093283 mRNA. Translation: BAC04120.1.
AC135056 Genomic DNA. No translation available.
BC000155 mRNA. Translation: AAH00155.3.
BC064503 mRNA. Translation: AAH64503.1.
BT009834 mRNA. Translation: AAP88836.1.
CCDSCCDS11800.1. [Q13098-7]
CCDS32774.1. [Q13098-4]
PIRG01646.
RefSeqNP_004118.3. NM_004127.4. [Q13098-4]
NP_997657.1. NM_212492.1. [Q13098-7]
XP_005256420.1. XM_005256363.1. [Q13098-5]
UniGeneHs.268530.

3D structure databases

ProteinModelPortalQ13098.
SMRQ13098. Positions 42-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109131. 48 interactions.
DIPDIP-42077N.
IntActQ13098. 12 interactions.
MINTMINT-1203964.
STRING9606.ENSP00000347251.

PTM databases

PhosphoSiteQ13098.

Polymorphism databases

DMDM223590263.

Proteomic databases

MaxQBQ13098.
PaxDbQ13098.
PRIDEQ13098.

Protocols and materials databases

DNASU2873.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306823; ENSP00000302873; ENSG00000169727. [Q13098-4]
ENST00000355130; ENSP00000347251; ENSG00000169727. [Q13098-7]
ENST00000392358; ENSP00000376167; ENSG00000169727. [Q13098-7]
ENST00000578552; ENSP00000462265; ENSG00000169727. [Q13098-5]
GeneID2873.
KEGGhsa:2873.
UCSCuc002kdk.1. human. [Q13098-7]
uc002kdl.1. human. [Q13098-4]
uc002kdn.1. human. [Q13098-5]

Organism-specific databases

CTD2873.
GeneCardsGC17P080009.
HGNCHGNC:4549. GPS1.
HPAHPA052848.
MIM601934. gene.
neXtProtNX_Q13098.
PharmGKBPA28944.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5187.
HOGENOMHOG000091977.
HOVERGENHBG030722.
KOK12175.
OMAIADHCPP.
PhylomeDBQ13098.
TreeFamTF101167.

Gene expression databases

ArrayExpressQ13098.
BgeeQ13098.
CleanExHS_GPS1.
GenevestigatorQ13098.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.25.40.10. 2 hits.
InterProIPR019585. 26S_proteasome_reg_su-Rpn7.
IPR000717. PCI_dom.
IPR011990. TPR-like_helical.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF01399. PCI. 1 hit.
PF10602. RPN7. 1 hit.
[Graphical view]
SMARTSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGPS1. human.
GeneWikiGPS1.
GenomeRNAi2873.
NextBio11339.
PROQ13098.
SOURCESearch...

Entry information

Entry nameCSN1_HUMAN
AccessionPrimary (citable) accession number: Q13098
Secondary accession number(s): Q8NA10, Q9BWL1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM