Q13098 (CSN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	GPS1
Synonyms:	COPS1, CSN1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	491 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 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
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
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20
Sequence similarities	Belongs to the CSN1 family. Contains 1 PCI domain.
Sequence caution	The sequence AAC50906.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Signalosome
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	JNK cascade Traceable author statement. Source: ProtInc cell cycle Traceable author statement. Source: ProtInc cullin deneddylation Inferred from direct assay. Source: UniProtKB inactivation of MAPK activity Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell signalosome Inferred from direct assay Ref.17. Source: UniProtKB
Molecular function	GTPase inhibitor activity Traceable author statement. Source: ProtInc binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.17
	Chain	2 – 491	490	COP9 signalosome complex subunit 1		PRO_0000120959
Regions
	Domain	324 – 428	105	PCI
Amino acid modifications
	Modified residue	377	1	Phosphotyrosine Ref.13
	Modified residue	467	1	N6-acetyllysine Ref.21
	Modified residue	468	1	Phosphoserine Ref.15 Ref.17
	Modified residue	474	1	Phosphoserine Ref.16 Ref.17 Ref.18 Ref.19 Ref.20
	Modified residue	479	1	Phosphothreonine Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20
	Modified residue	483	1	Phosphoserine Ref.16 Ref.17 Ref.18
	Modified residue	488	1	Phosphoserine Ref.15
Natural variations
	Alternative sequence	1 – 11	11	MPLPVQVFNLQ → MRDSSAPSSASSSVTDLYCT PHSSRSDLVLPGTAGDFSLS ASLSACTLLYE in isoform 2.		VSP_036240
	Alternative sequence	12 – 109	98	GAVEP…SLREL → PASSVSGSGGAESQDRMRDS SAPSSASSSVTDLYCTPHSS RSDLVLPGMAGDFSLSASLS ACTLLYEGAVEPMQIDVDPQ EDP in isoform 3.		VSP_036241
	Alternative sequence	103 – 106	4	Missing in isoform 2 and isoform 4.		VSP_036242
	Alternative sequence	471 – 491	21	REGSQ…MSTNM → TSTDLGPPGGSVLPAAQLRG LATGCHPACVPSLGLRRQAA ASCGPSWKERPAGLDPVGFC PQGADCAAPRPSGTISQTPP VPASVRCRQVGGVH in isoform 3.		VSP_011882
Experimental info
	Sequence conflict	259	1	A → T in BAC04120. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 10, 2009. Version 4. Checksum: BF925164ED985638	FASTA	491	55,537
	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
	Isoform 4 [UniParc]. Checksum: 8E706F5C8E4763A5	FASTA	487	55,093
	10 20 30 40 50 60 MPLPVQVFNL QGAVEPMQID VDPQEDPQNA PDVNYVVENP SLDLEQYAAS YSGLMRIERL 70 80 90 100 110 120 QFIADHCPTL RVEALKMALS FVQRTFNVDM YEEIHRKLSE ATRELQNAPD AIPESGVEPP 130 140 150 160 170 180 ALDTAWVEAT RKKALLKLEK LDTDLKNYKG NSIKESIRRG HDDLGDHYLD CGDLSNALKC 190 200 210 220 230 240 YSRARDYCTS AKHVINMCLN VIKVSVYLQN WSHVLSYVSK AESTPEIAEQ RGERDSQTQA 250 260 270 280 290 300 ILTKLKCAAG LAELAARKYK QAAKCLLLAS FDHCDFPELL SPSNVAIYGG LCALATFDRQ 310 320 330 340 350 360 ELQRNVISSS SFKLFLELEP QVRDIIFKFY ESKYASCLKM LDEMKDNLLL DMYLAPHVRT 370 380 390 400 410 420 LYTQIRNRAL IQYFSPYVSA DMHRMAAAFN TTVAALEDEL TQLILEGLIS ARVDSHSKIL 430 440 450 460 470 480 YARDVDQRST TFEKSLLMGK EFQRRAKAMM LRAAVLRNQI HVKSPPREGS QGELTPANSQ SRMSTNM
	Isoform 3 [UniParc]. Checksum: B0C46F7860CB480E	FASTA	549	59,818
	10 20 30 40 50 60 MPLPVQVFNL QPASSVSGSG GAESQDRMRD SSAPSSASSS VTDLYCTPHS SRSDLVLPGM 70 80 90 100 110 120 AGDFSLSASL SACTLLYEGA VEPMQIDVDP QEDPQNAPDA IPESGVEPPA LDTAWVEATR 130 140 150 160 170 180 KKALLKLEKL DTDLKNYKGN SIKESIRRGH DDLGDHYLDC GDLSNALKCY SRARDYCTSA 190 200 210 220 230 240 KHVINMCLNV IKVSVYLQNW SHVLSYVSKA ESTPEIAEQR GERDSQTQAI LTKLKCAAGL 250 260 270 280 290 300 AELAARKYKQ AAKCLLLASF DHCDFPELLS PSNVAIYGGL CALATFDRQE LQRNVISSSS 310 320 330 340 350 360 FKLFLELEPQ VRDIIFKFYE SKYASCLKML DEMKDNLLLD MYLAPHVRTL YTQIRNRALI 370 380 390 400 410 420 QYFSPYVSAD MHRMAAAFNT TVAALEDELT QLILEGLISA RVDSHSKILY ARDVDQRSTT 430 440 450 460 470 480 FEKSLLMGKE FQRRAKAMML RAAVLRNQIH VKSPPTSTDL GPPGGSVLPA AQLRGLATGC 490 500 510 520 530 540 HPACVPSLGL RRQAAASCGP SWKERPAGLD PVGFCPQGAD CAAPRPSGTI SQTPPVPASV RCRQVGGVH
	Isoform 2 [UniParc]. Checksum: 6081BEBD48CAF32C	FASTA	527	59,050
	10 20 30 40 50 60 MRDSSAPSSA SSSVTDLYCT PHSSRSDLVL PGTAGDFSLS ASLSACTLLY EGAVEPMQID 70 80 90 100 110 120 VDPQEDPQNA PDVNYVVENP SLDLEQYAAS YSGLMRIERL QFIADHCPTL RVEALKMALS 130 140 150 160 170 180 FVQRTFNVDM YEEIHRKLSE ATRELQNAPD AIPESGVEPP ALDTAWVEAT RKKALLKLEK 190 200 210 220 230 240 LDTDLKNYKG NSIKESIRRG HDDLGDHYLD CGDLSNALKC YSRARDYCTS AKHVINMCLN 250 260 270 280 290 300 VIKVSVYLQN WSHVLSYVSK AESTPEIAEQ RGERDSQTQA ILTKLKCAAG LAELAARKYK 310 320 330 340 350 360 QAAKCLLLAS FDHCDFPELL SPSNVAIYGG LCALATFDRQ ELQRNVISSS SFKLFLELEP 370 380 390 400 410 420 QVRDIIFKFY ESKYASCLKM LDEMKDNLLL DMYLAPHVRT LYTQIRNRAL IQYFSPYVSA 430 440 450 460 470 480 DMHRMAAAFN TTVAALEDEL TQLILEGLIS ARVDSHSKIL YARDVDQRST TFEKSLLMGK 490 500 510 520 EFQRRAKAMM LRAAVLRNQI HVKSPPREGS QGELTPANSQ SRMSTNM

References

	« Hide 'large scale' referencesShow '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: 8943324] [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: 14702039] [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: 16625196] [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: 15489334] [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: 9535219] [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: 11285227] [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: 11114242] [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: 11337588] [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: 12324474] [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: 12732143] [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: 12628923] [Abstract] Cited for: FUNCTION.
[13]	"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling." Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z. EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-377, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND SER-488, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; THR-479 AND SER-483, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"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: 18850735] [Abstract] Cited for: IDENTIFICATION IN THE CSN COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT SER-468; SER-474; THR-479 AND SER-483.
[18]	"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-474; THR-479 AND SER-483, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474 AND THR-479, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"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-474 AND THR-479, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-467, MASS SPECTROMETRY.
[22]	"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: 21269460] [Abstract] Cited for: 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.
IPI	IPI00156282. IPI00300386. IPI00414289. IPI00921488.
PIR	G01646.
RefSeq	NP_004118.3. NM_004127.4. NP_997657.1. NM_212492.1.
UniGene	Hs.268530.
3D structure databases
ProteinModelPortal	Q13098.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42077N.
IntAct	Q13098. 6 interactions.
MINT	MINT-1203964.
STRING	Q13098.
PTM databases
PhosphoSite	Q13098.
Polymorphism databases
DMDM	223590263.
Proteomic databases
PRIDE	Q13098.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000306823; ENSP00000302873; ENSG00000169727.
GeneID	2873.
KEGG	hsa:2873.
UCSC	uc002kdk.1. human. uc002kdl.1. human.
Organism-specific databases
CTD	2873.
GeneCards	GC17P080009.
HGNC	HGNC:4549. GPS1.
MIM	601934. gene.
neXtProt	NX_Q13098.
PharmGKB	PA28944.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10929.
GeneTree	ENSGT00510000046608.
HOVERGEN	HBG030722.
OMA	YKSNSIK.
PhylomeDB	Q13098.
Gene expression databases
ArrayExpress	Q13098.
Bgee	Q13098.
CleanEx	HS_GPS1.
Genevestigator	Q13098.
GermOnline	ENSG00000169727. Homo sapiens.
Family and domain databases
InterPro	IPR019585. 26S_proteasome_reg_su-Rpn7. IPR000717. PCI_dom. IPR011990. TPR-like_helical. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K12175.
Pfam	PF01399. PCI. 1 hit. PF10602. RPN7. 1 hit. [Graphical view]
SMART	SM00088. PINT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	11339.
SOURCE	Search...

Entry information

Entry name

CSN1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 113 of the entry and version 4 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.