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Q13098

- CSN1_HUMAN

UniProt

Q13098 - CSN1_HUMAN

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Protein
COP9 signalosome complex subunit 1
Gene
GPS1, COPS1, CSN1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

  1. GTPase inhibitor activity Source: ProtInc
  2. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. JNK cascade Source: ProtInc
  2. cell cycle Source: ProtInc
  3. cullin deneddylation Source: UniProtKB
  4. inactivation of MAPK activity Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GPS1
Synonyms:COPS1, CSN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:4549. GPS1.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. COP9 signalosome Source: UniProtKB
  2. cytoplasm Source: HPA
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Signalosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28944.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 491490COP9 signalosome complex subunit 1
PRO_0000120959Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei468 – 4681Phosphoserine2 Publications
Modified residuei474 – 4741Phosphoserine4 Publications
Modified residuei479 – 4791Phosphothreonine7 Publications
Modified residuei483 – 4831Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13098.
PaxDbiQ13098.
PRIDEiQ13098.

PTM databases

PhosphoSiteiQ13098.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

ArrayExpressiQ13098.
BgeeiQ13098.
CleanExiHS_GPS1.
GenevestigatoriQ13098.

Organism-specific databases

HPAiHPA052848.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COPS5Q929053EBI-725197,EBI-594661

Protein-protein interaction databases

BioGridi109131. 48 interactions.
DIPiDIP-42077N.
IntActiQ13098. 12 interactions.
MINTiMINT-1203964.
STRINGi9606.ENSP00000347251.

Structurei

3D structure databases

ProteinModelPortaliQ13098.
SMRiQ13098. Positions 42-436.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini324 – 428105PCI
Add
BLAST

Domaini

The PCI domain is necessary and sufficient for the interactions with other CSN subunits of the complex. Mediates the interaction with CAPN8 By similarity.1 Publication
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.1 Publication

Sequence similaritiesi

Belongs to the CSN1 family.
Contains 1 PCI domain.

Phylogenomic databases

eggNOGiCOG5187.
HOGENOMiHOG000091977.
HOVERGENiHBG030722.
KOiK12175.
OMAiIADHCPP.
PhylomeDBiQ13098.
TreeFamiTF101167.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 2 hits.
InterProiIPR019585. 26S_proteasome_reg_su-Rpn7.
IPR000717. PCI_dom.
IPR011990. TPR-like_helical.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
PF10602. RPN7. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13098-4) [UniParc]FASTAAdd to Basket

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.

« Hide

MPLPVQVFNL QGAVEPMQID VDPQEDPQNA PDVNYVVENP SLDLEQYAAS    50
YSGLMRIERL QFIADHCPTL RVEALKMALS FVQRTFNVDM YEEIHRKLSE 100
ATRSSLRELQ NAPDAIPESG VEPPALDTAW VEATRKKALL KLEKLDTDLK 150
NYKGNSIKES IRRGHDDLGD HYLDCGDLSN ALKCYSRARD YCTSAKHVIN 200
MCLNVIKVSV YLQNWSHVLS YVSKAESTPE IAEQRGERDS QTQAILTKLK 250
CAAGLAELAA RKYKQAAKCL LLASFDHCDF PELLSPSNVA IYGGLCALAT 300
FDRQELQRNV ISSSSFKLFL ELEPQVRDII FKFYESKYAS CLKMLDEMKD 350
NLLLDMYLAP HVRTLYTQIR NRALIQYFSP YVSADMHRMA AAFNTTVAAL 400
EDELTQLILE GLISARVDSH SKILYARDVD QRSTTFEKSL LMGKEFQRRA 450
KAMMLRAAVL RNQIHVKSPP REGSQGELTP ANSQSRMSTN M 491
Length:491
Mass (Da):55,537
Last modified:February 10, 2009 - v4
Checksum:iBF925164ED985638
GO
Isoform 4 (identifier: Q13098-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     103-106: Missing.

Show »
Length:487
Mass (Da):55,093
Checksum:i8E706F5C8E4763A5
GO
Isoform 3 (identifier: Q13098-6) [UniParc]FASTAAdd to Basket

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.

Show »
Length:549
Mass (Da):59,818
Checksum:iB0C46F7860CB480E
GO
Isoform 2 (identifier: Q13098-7) [UniParc]FASTAAdd to Basket

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

Show »
Length:527
Mass (Da):59,050
Checksum:i6081BEBD48CAF32C
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1111MPLPVQVFNLQ → MRDSSAPSSASSSVTDLYCT PHSSRSDLVLPGTAGDFSLS ASLSACTLLYE in isoform 2.
VSP_036240Add
BLAST
Alternative sequencei12 – 10998GAVEP…SLREL → PASSVSGSGGAESQDRMRDS SAPSSASSSVTDLYCTPHSS RSDLVLPGMAGDFSLSASLS ACTLLYEGAVEPMQIDVDPQ EDP in isoform 3.
VSP_036241Add
BLAST
Alternative sequencei103 – 1064Missing in isoform 2 and isoform 4.
VSP_036242
Alternative sequencei471 – 49121REGSQ…MSTNM → TSTDLGPPGGSVLPAAQLRG LATGCHPACVPSLGLRRQAA ASCGPSWKERPAGLDPVGFC PQGADCAAPRPSGTISQTPP VPASVRCRQVGGVH in isoform 3.
VSP_011882Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2591A → T in BAC04120. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11800.1. [Q13098-7]
CCDS32774.1. [Q13098-4]
PIRiG01646.
RefSeqiNP_004118.3. NM_004127.4. [Q13098-4]
NP_997657.1. NM_212492.1. [Q13098-7]
XP_005256420.1. XM_005256363.1. [Q13098-5]
UniGeneiHs.268530.

Genome annotation databases

EnsembliENST00000306823; ENSP00000302873; ENSG00000169727. [Q13098-4]
ENST00000355130; ENSP00000347251; ENSG00000169727. [Q13098-7]
ENST00000392358; ENSP00000376167; ENSG00000169727. [Q13098-7]
ENST00000578552; ENSP00000462265; ENSG00000169727. [Q13098-5]
GeneIDi2873.
KEGGihsa:2873.
UCSCiuc002kdk.1. human. [Q13098-7]
uc002kdl.1. human. [Q13098-4]
uc002kdn.1. human. [Q13098-5]

Polymorphism databases

DMDMi223590263.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11800.1. [Q13098-7 ]
CCDS32774.1. [Q13098-4 ]
PIRi G01646.
RefSeqi NP_004118.3. NM_004127.4. [Q13098-4 ]
NP_997657.1. NM_212492.1. [Q13098-7 ]
XP_005256420.1. XM_005256363.1. [Q13098-5 ]
UniGenei Hs.268530.

3D structure databases

ProteinModelPortali Q13098.
SMRi Q13098. Positions 42-436.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109131. 48 interactions.
DIPi DIP-42077N.
IntActi Q13098. 12 interactions.
MINTi MINT-1203964.
STRINGi 9606.ENSP00000347251.

PTM databases

PhosphoSitei Q13098.

Polymorphism databases

DMDMi 223590263.

Proteomic databases

MaxQBi Q13098.
PaxDbi Q13098.
PRIDEi Q13098.

Protocols and materials databases

DNASUi 2873.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000306823 ; ENSP00000302873 ; ENSG00000169727 . [Q13098-4 ]
ENST00000355130 ; ENSP00000347251 ; ENSG00000169727 . [Q13098-7 ]
ENST00000392358 ; ENSP00000376167 ; ENSG00000169727 . [Q13098-7 ]
ENST00000578552 ; ENSP00000462265 ; ENSG00000169727 . [Q13098-5 ]
GeneIDi 2873.
KEGGi hsa:2873.
UCSCi uc002kdk.1. human. [Q13098-7 ]
uc002kdl.1. human. [Q13098-4 ]
uc002kdn.1. human. [Q13098-5 ]

Organism-specific databases

CTDi 2873.
GeneCardsi GC17P080009.
HGNCi HGNC:4549. GPS1.
HPAi HPA052848.
MIMi 601934. gene.
neXtProti NX_Q13098.
PharmGKBi PA28944.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5187.
HOGENOMi HOG000091977.
HOVERGENi HBG030722.
KOi K12175.
OMAi IADHCPP.
PhylomeDBi Q13098.
TreeFami TF101167.

Miscellaneous databases

ChiTaRSi GPS1. human.
GeneWikii GPS1.
GenomeRNAii 2873.
NextBioi 11339.
PROi Q13098.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13098.
Bgeei Q13098.
CleanExi HS_GPS1.
Genevestigatori Q13098.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
1.25.40.10. 2 hits.
InterProi IPR019585. 26S_proteasome_reg_su-Rpn7.
IPR000717. PCI_dom.
IPR011990. TPR-like_helical.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF01399. PCI. 1 hit.
PF10602. RPN7. 1 hit.
[Graphical view ]
SMARTi SM00088. PINT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. 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].

Entry informationi

Entry nameiCSN1_HUMAN
AccessioniPrimary (citable) accession number: Q13098
Secondary accession number(s): Q8NA10, Q9BWL1
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi