Reviewed, UniProtKB/Swiss-Prot Q1RMU2 (CYLD_BOVIN)

Names and origin

Protein names

Recommended name:
    Probable ubiquitin carboxyl-terminal hydrolase CYLD
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase CYLD
    Ubiquitin-specific-processing protease CYLD
    Deubiquitinating enzyme CYLD

Gene names

Name:	CYLD
Synonyms:	CYLD1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	953 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Negative regulator of TRAF2 and NF-kappa-B signaling pathway. Has deubiquitinating activity that is directed towards non-'Lys-48'-linked polyubiquitin chains. The inhibition of NF-kappa-B activation is mediated at least in part, by the deubiquitination and inactivation of TRAF2 and, to a lesser extent, TRAF6 By similarity.
Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
Subunit structure	Interacts with NEMO, TRAF2 and TRIP By similarity.
Subcellular location	Cytoplasm › perinuclear region By similarity.
Sequence similarities	Belongs to the peptidase C67 family. Contains 2 CAP-Gly domains.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm
Domain	Repeat
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: InterPro ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell ribosome Inferred from electronic annotation. Source: InterPro
Molecular function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Inferred from electronic annotation. Source: InterPro ubiquitin thiolesterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 953	953	Probable ubiquitin carboxyl-terminal hydrolase CYLD		PRO_0000326147
Regions
	Domain	153 – 198	46	CAP-Gly 1
	Domain	489 – 532	44	CAP-Gly 2
	Region	106 – 590	485	Interaction with TRIP By similarity
	Region	391 – 466	76	Interaction with TRAF2 By similarity
	Region	467 – 681	215	Interaction with NEMO By similarity
Sites
	Active site	598	1	By similarity
	Active site	868	1	By similarity
Amino acid modifications
	Modified residue	396	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1RMU2-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: F478EBCB7D52863E	FASTA	953	106,805
	10 20 30 40 50 60 MSSGLWSQEK VTSPYWEERI FYLLLQECSV TDKQTQKLLK VPKGSIGQNI QDRSVGLSRI 70 80 90 100 110 120 PSAKGKKNQI GLKILEQPHA VLFVDEKDVV EINEKFTELL LAITNCEERF SLFKNRNRLS 130 140 150 160 170 180 KGLQIDVGCP VKVQLRSGEE KFPGVVRFRG PLLAERTVSG IFFGVELLEE GRGQGFTDGV 190 200 210 220 230 240 YQGKQLFQCD EDCGVFVALD KLELIEDDDT GLESDYAGPV DTMQVELPPL EINSRVSLKL 250 260 270 280 290 300 GETIESGTVI FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAS VESTILLHIN 310 320 330 340 350 360 DIIPESVTQE RRPPKLAFMS RGVGDKGSFS HNKPKATGST SDPGTRNRSE LFYTLNGSSV 370 380 390 400 410 420 DSQPQSKSKN SWYIDEVAED PAKSLTEIPP DFGHASPPLQ PPSMNSLSSE NRFHSLPFSL 430 440 450 460 470 480 TKMPNTNGSI SHSPLSLSVQ SVMGELNNAP VQESPPLAVS SGNSHGLEVG SLAEVKENPP 490 500 510 520 530 540 FYGVIRWIGQ PPGLNEVLAG LELEDECAGC TDGTFRGTRY FTCALKKALF VKLKSCRPDS 550 560 570 580 590 600 RFASLQPVSN QIERCNSLAF GGYLSEVVEE NTPPKMEKEG FEIMIGKKKG IQGHYNSCYL 610 620 630 640 650 660 DSTLFCLFAF SSVLDTVLLR PKEKNDVEYY SETQELLRTE IVNPLRIYGY VCATKIMKLR 670 680 690 700 710 720 KILEKVEAAS GFTSEEKDPE EFLNILFHHI LRVEPLLKIR SAGQKVQDCY FYQIFMEKNE 730 740 750 760 770 780 KVGVPTIQQL LECSFINSNL KFAEAPSCLI IQMPRFGKDF KLFKKIFPSL ELNITDLLED 790 800 810 820 830 840 TPRQCRICGG LAMYECRECY DDPDISAGKI KQFCKTCNAQ VHLHPKRLNH KYNPVSLPKD 850 860 870 880 890 900 LPDWDWRHGC IPCQKMELFA VLCIETSHYV AFVKYGKDDS AWLFFDSMAD RDGGQNGFNI 910 920 930 940 950 PQVTPCPEVG EYLKMSLDDL HSLDSRRIQG CARRLLCDAY MCMYQSPTMS LYK

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Uterus.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC114710 mRNA. Translation: AAI14711.1.
IPI	IPI00686064.
RefSeq	NP_001039882.1.
UniGene	Bt.58637
3D structure databases
SMR	Q1RMU2. Positions 125-206, 228-306, 454-547.
ModBase	Search...
Protein family/group databases
MEROPS	C67.001.
Genome annotation databases
Ensembl	ENSBTAG00000006291. Bos taurus. [Contig view]
GeneID	536421.
KEGG	bta:536421.
Phylogenomic databases
HOVERGEN	Q1RMU2.
OMA	Q1RMU2. GVQLCSF.
Enzyme and pathway databases
BRENDA	3.1.2.15. 251.
Family and domain databases
InterPro	IPR000938. Cytoskel-assoc-prot_CAP-Gly. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR001593. Ribosomal_S3Ae. [Graphical view]
PANTHER	PTHR11830. Ribosomal_S3AE. 1 hit.
Pfam	PF01302. CAP_GLY. 3 hits. PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00845. CAP_GLY_1. 1 hit. PS50245. CAP_GLY_2. 2 hits. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. False negative. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYLD_BOVIN

Accession

Primary (citable) accession number: Q1RMU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	May 16, 2006
Last modified:	June 16, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)