Reviewed, UniProtKB/Swiss-Prot Q9NQC7 (CYLD_HUMAN)

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, KIAA0849
ORF Names:	HSPC057

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	956 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. Ref.6 Ref.7 Ref.8 Ref.9
Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
Subunit structure	Interacts with NEMO, TRAF2 and TRIP. Ref.6 Ref.7 Ref.8 Ref.9
Subcellular location	Cytoplasm › perinuclear region Ref.9.
Tissue specificity	Detected in fetal brain, testis, and skeletal muscle, and at a lower level in adult brain, leukocytes, liver, heart, kidney, spleen, ovary and lung. Isoform 2 is found in all tissues except kidney. Ref.1
Involvement in disease	Defects in CYLD are the cause of familial cylindromatosis [MIM:132700]; also known as Ancell-Spiegler cylindromas or turban tumor syndrome or dermal eccrine cylindromatosis. CYLD is an autosomal dominant and highly tumor type-specific disorder. The tumors (known as cylindromas because of their characteristic microscopic architecture) are believed to arise from or recapitulate the appearance of the eccrine or apocrine cells of the skin that secrete sweat and scent respectively. Cylindromas arise predominantly in hairy parts of the body with approximately 90% on the head and neck. The development of a confluent mass which may ulcerate or become infected has led to the designation 'turban tumor syndrome'. The skin tumors show differentiation in the direction of hair structures, hence the synonym trichoepithelioma. Defects in CYLD are the cause of multiple familial trichoepithelioma type 1 (MFT1) [MIM:601606]; also known as epithelioma adenoides cysticum of Brooke (EAC) or hereditary multiple benign cystic epithelioma or Brooke-Fordyce trichoepitheliomas. MFT1 is an autosomal dominant dermatosis characterized by the presence of many skin tumors predominantly on the face. Since histologic examination shows dermal aggregates of basaloid cells with connection to or differentiation toward hair follicles, this disorder has been thought to represent a benign hamartoma of the pilosebaceous apparatus. Trichoepitheliomas can degenerate into basal cell carcinoma. Ref.14 Ref.15 Ref.17 Defects in CYLD are the cause of Brooke-Spiegler syndrome (BRSS) [MIM:605041]. BRSS is an autosomal dominant disorder characterized by the appearance of multiple skin appendage tumors such as cylindroma, trichoepithelioma, and spiradenoma. These tumors are typically located in the head and neck region, appear in early adulthood, and gradually increase in size and number throughout life. Ref.14 Ref.12 Ref.13 Ref.16
Sequence similarities	Belongs to the peptidase C67 family. Contains 2 CAP-Gly domains.
Sequence caution	The sequence AAF29029.1 differs from that shown. Reason: Frameshift at positions 776, 808 and 932.

Ontologies

Keywords
Biological process	Cell cycle Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Tumor suppressor
Domain	Repeat
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW translation Inferred from electronic annotation. Source: InterPro ubiquitin-dependent protein catabolic process Non-traceable author statement. Source: UniProtKB
Cellular component	cytoskeleton Ref.1 Non-traceable author statement. Source: UniProtKB 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 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9NQC7-1)

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: Q9NQC7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     305-307: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 956

956

Probable ubiquitin carboxyl-terminal hydrolase CYLD

PRO_0000080698

Regions

Domain

153 – 198

46

CAP-Gly 1

Domain

492 – 535

44

CAP-Gly 2

Region

106 – 593

488

Interaction with TRIP

Region

394 – 469

76

Interaction with TRAF2

Region

470 – 684

215

Interaction with NEMO

Sites

Active site

601

1

By similarity

Active site

871

1

By similarity

Amino acid modifications

Modified residue

399

1

Phosphoserine Ref.10

Modified residue

418

1

Phosphoserine By similarity

Natural variations

Alternative sequence

305 – 307

3

Missing in isoform 2.

VSP_011277

Natural variant

747

1

E → G in MFT1 and BRSS. Ref.14

VAR_045967

Experimental info

Mutagenesis

457

1

S → A: Abolishes binding to TRAF2. Ref.8

Mutagenesis

601

1

C → S: Loss of deubiquitinating activity. Ref.6 Ref.7

Mutagenesis

871

1

H → N: Loss of deubiquitinating activity. Ref.8

Secondary structure

1

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956

Helix Strand Turn

Details...

Beta strand

130 – 134

5

Beta strand

136 – 139

4

Beta strand

141 – 149

9

Beta strand

154 – 157

4

Beta strand

163 – 167

5

Beta strand

169 – 171

3

Turn

191 – 193

3

Beta strand

194 – 197

4

Helix

199 – 201

3

Beta strand

202 – 204

3

Beta strand

235 – 240

6

Beta strand

243 – 253

11

Turn

259 – 261

3

Beta strand

264 – 272

9

Beta strand

278 – 280

3

Beta strand

283 – 285

3

Beta strand

293 – 298

6

Helix

299 – 301

3

Turn

463 – 465

3

Beta strand

466 – 468

3

Beta strand

474 – 478

5

Beta strand

480 – 482

3

Beta strand

486 – 492

7

Beta strand

495 – 497

3

Beta strand

501 – 508

8

Beta strand

514 – 518

5

Beta strand

531 – 535

5

Helix

536 – 538

3

Beta strand

539 – 541

3

Helix

584 – 586

3

Beta strand

588 – 591

4

Helix

601 – 611

11

Beta strand

612 – 614

3

Helix

615 – 617

3

Helix

618 – 622

5

Helix

633 – 642

10

Helix

645 – 650

6

Beta strand

652 – 654

3

Helix

656 – 669

14

Helix

682 – 690

9

Turn

691 – 694

4

Beta strand

699 – 704

6

Beta strand

710 – 713

4

Helix

730 – 741

12

Beta strand

743 – 747

5

Beta strand

750 – 755

6

Beta strand

760 – 764

5

Beta strand

773 – 775

3

Helix

778 – 780

3

Beta strand

781 – 784

4

Turn

789 – 791

3

Helix

800 – 802

3

Turn

806 – 811

6

Helix

818 – 824

7

Helix

828 – 830

3

Beta strand

859 – 868

10

Beta strand

871 – 877

7

Beta strand

879 – 881

3

Beta strand

885 – 889

5

Beta strand

905 – 908

4

Helix

911 – 914

4

Helix

920 – 925

6

Helix

928 – 930

3

Helix

935 – 940

6

Beta strand

944 – 948

5

Helix

950 – 952

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 01831F9A83424631	FASTA	956	107,316
	10 20 30 40 50 60 MSSGLWSQEK VTSPYWEERI FYLLLQECSV TDKQTQKLLK VPKGSIGQYI QDRSVGHSRI 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 ALESDYAGPG DTMQVELPPL EINSRVSLKV 250 260 270 280 290 300 GETIESGTVI FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAC VESTILLHIN 310 320 330 340 350 360 DIIPALSESV TQERRPPKLA FMSRGVGDKG SSSHNKPKAT GSTSDPGNRN RSELFYTLNG 370 380 390 400 410 420 SSVDSQPQSK SKNTWYIDEV AEDPAKSLTE ISTDFDRSSP PLQPPPVNSL TTENRFHSLP 430 440 450 460 470 480 FSLTKMPNTN GSIGHSPLSL SAQSVMEELN TAPVQESPPL AMPPGNSHGL EVGSLAEVKE 490 500 510 520 530 540 NPPFYGVIRW IGQPPGLNEV LAGLELEDEC AGCTDGTFRG TRYFTCALKK ALFVKLKSCR 550 560 570 580 590 600 PDSRFASLQP VSNQIERCNS LAFGGYLSEV VEENTPPKME KEGLEIMIGK KKGIQGHYNS 610 620 630 640 650 660 CYLDSTLFCL FAFSSVLDTV LLRPKEKNDV EYYSETQELL RTEIVNPLRI YGYVCATKIM 670 680 690 700 710 720 KLRKILEKVE AASGFTSEEK DPEEFLNILF HHILRVEPLL KIRSAGQKVQ DCYFYQIFME 730 740 750 760 770 780 KNEKVGVPTI QQLLEWSFIN SNLKFAEAPS CLIIQMPRFG KDFKLFKKIF PSLELNITDL 790 800 810 820 830 840 LEDTPRQCRI CGGLAMYECR ECYDDPDISA GKIKQFCKTC NTQVHLHPKR LNHKYNPVSL 850 860 870 880 890 900 PKDLPDWDWR HGCIPCQNME LFAVLCIETS HYVAFVKYGK DDSAWLFFDS MADRDGGQNG 910 920 930 940 950 FNIPQVTPCP EVGEYLKMSL EDLHSLDSRR IQGCARRLLC DAYMCMYQSP TMSLYK
	Isoform 2. Checksum: 0CCB3D21E2FF8851	FASTA	953	107,044
	10 20 30 40 50 60 MSSGLWSQEK VTSPYWEERI FYLLLQECSV TDKQTQKLLK VPKGSIGQYI QDRSVGHSRI 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 ALESDYAGPG DTMQVELPPL EINSRVSLKV 250 260 270 280 290 300 GETIESGTVI FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAC VESTILLHIN 310 320 330 340 350 360 DIIPESVTQE RRPPKLAFMS RGVGDKGSSS HNKPKATGST SDPGNRNRSE LFYTLNGSSV 370 380 390 400 410 420 DSQPQSKSKN TWYIDEVAED PAKSLTEIST DFDRSSPPLQ PPPVNSLTTE NRFHSLPFSL 430 440 450 460 470 480 TKMPNTNGSI GHSPLSLSAQ SVMEELNTAP VQESPPLAMP PGNSHGLEVG SLAEVKENPP 490 500 510 520 530 540 FYGVIRWIGQ PPGLNEVLAG LELEDECAGC TDGTFRGTRY FTCALKKALF VKLKSCRPDS 550 560 570 580 590 600 RFASLQPVSN QIERCNSLAF GGYLSEVVEE NTPPKMEKEG LEIMIGKKKG 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 LEWSFINSNL KFAEAPSCLI IQMPRFGKDF KLFKKIFPSL ELNITDLLED 790 800 810 820 830 840 TPRQCRICGG LAMYECRECY DDPDISAGKI KQFCKTCNTQ VHLHPKRLNH KYNPVSLPKD 850 860 870 880 890 900 LPDWDWRHGC IPCQNMELFA VLCIETSHYV AFVKYGKDDS AWLFFDSMAD RDGGQNGFNI 910 920 930 940 950 PQVTPCPEVG EYLKMSLEDL HSLDSRRIQG CARRLLCDAY MCMYQSPTMS LYK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of the familial cylindromatosis tumor suppressor gene." Bignell G.R., Brown C., Biggs P.J., Lakhani S.R., Jones C., Hansen J., Blair E., Hofmann B., Siebert R., Turner G., Evans D.G., Schrander-Stumpel C., Beemer F.A., Van Den Ouweland A., Halley D., Delpech B., Cleveland M.G., Leigh I. , Leisti J., Rasmussen S., Wallace M.R., Fenske C., Banerjee P., Oiso N., Chaggar R., Merrett S., Leonard N., Huber M., Hohl D., Chapman P., Burn J., Swift S., Smith A., Ashworth A., Stratton M.R. Nat. Genet. 25:160-165(2000) [PubMed: 10835629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INVOLVEMENT IN FAMILIAL CYLINDROMATOSIS.
[2]	"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:355-364(1998) [PubMed: 10048485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[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] (ISOFORM 2). Tissue: Uterus.
[5]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 397-956. Tissue: Umbilical cord blood.
[6]	"CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members." Trompouki E., Hatzivassiliou E., Tsichritzis T., Farmer H., Ashworth A., Mosialos G. Nature 424:793-796(2003) [PubMed: 12917689] [Abstract] Cited for: FUNCTION, INTERACTION WITH NEMO, MUTAGENESIS OF CYS-601.
[7]	"Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB." Brummelkamp T.R., Nijman S.M.B., Dirac A.M.G., Bernards R. Nature 424:797-801(2003) [PubMed: 12917690] [Abstract] Cited for: FUNCTION, INTERACTION WITH NEMO, MUTAGENESIS OF CYS-601.
[8]	"The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination." Kovalenko A., Chable-Bessia C., Cantarella G., Israeel A., Wallach D., Courtois G. Nature 424:801-805(2003) [PubMed: 12917691] [Abstract] Cited for: FUNCTION, INTERACTION WITH NEMO AND TRAF2, MUTAGENESIS OF SER-457 AND HIS-871.
[9]	"The tumor suppressor CYLD interacts with TRIP and regulates negatively nuclear factor kappaB activation by tumor necrosis factor." Regamey A., Hohl D., Liu J.W., Roger T., Kogerman P., Toftgaard R., Huber M. J. Exp. Med. 198:1959-1964(2003) [PubMed: 14676304] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TRIP.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"Solution structure of the 1st and 2nd CAP-GLY domains in human cylindromatosis tumor suppressor CYLD." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 125-304.
[12]	"Phenotype diversity in familial cylindromatosis: a frameshift mutation in the tumor suppressor gene CYLD underlies different tumors of skin appendages." Poblete Gutierrez P., Eggermann T., Hoeller D., Jugert F.K., Beermann T., Grussendorf-Conen E.-I., Zerres K., Merk H.F., Frank J. J. Invest. Dermatol. 119:527-531(2002) [PubMed: 12190880] [Abstract] Cited for: INVOLVEMENT IN FAMILIAL CYLINDROMATAOSIS, INVOLVEMENT IN BRSS.
[13]	"Identification of a recurrent mutation in the CYLD gene in Brooke-Spiegler syndrome." Scheinfeld N., Hu G., Gill M., Austin C., Celebi J.T. Clin. Exp. Dermatol. 28:539-541(2003) [PubMed: 12950348] [Abstract] Cited for: INVOLVEMENT IN BRSS.
[14]	"A novel missense mutation in CYLD in a family with Brooke-Spiegler syndrome." Hu G., Oender M., Gill M., Aksakal B., Oeztas M., Guerer M.A., Celebi J.T. J. Invest. Dermatol. 121:732-734(2003) [PubMed: 14632188] [Abstract] Cited for: VARIANT MFT1 GLY-747, VARIANT BRSS GLY-747.
[15]	"Two novel CYLD gene mutations in Chinese families with trichoepithelioma and a literature review of 16 families with trichoepithelioma reported in China." Liang Y.H., Gao M., Sun L.D., Liu L.J., Cui Y., Yang S., Fan X., Wang J., Xiao F.L., Zhang X.J. Br. J. Dermatol. 153:1213-1215(2005) [PubMed: 16307661] [Abstract] Cited for: INVOLVEMENT IN MFT1.
[16]	"Mutations in the CYLD gene in Brooke-Spiegler syndrome, familial cylindromatosis, and multiple familial trichoepithelioma: lack of genotype-phenotype correlation." Bowen S., Gill M., Lee D.A., Fisher G., Geronemus R.G., Vazquez M.E., Celebi J.T. J. Invest. Dermatol. 124:919-920(2005) [PubMed: 15854031] [Abstract] Cited for: INVOLVEMENT IN BRSS.
[17]	"CYLD mutations underlie Brooke-Spiegler, familial cylindromatosis, and multiple familial trichoepithelioma syndromes." Young A.L., Kellermayer R., Szigeti R., Teszas A., Azmi S., Celebi J.T. Clin. Genet. 70:246-249(2006) [PubMed: 16922728] [Abstract] Cited for: INVOLVEMENT IN FAMILIAL CYLINDROMATAOSIS, INVOLVEMENT IN MFT1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ250014 mRNA. Translation: CAB93533.1.
AB020656 mRNA. Translation: BAA74872.2. Different initiation.
BC012342 mRNA. Translation: AAH12342.1.
AF161542 mRNA. Translation: AAF29029.1. Frameshift.

IPI

IPI00106663.
IPI00456609.

RefSeq

NP_001035814.1.
NP_001035877.1.
NP_056062.1.

UniGene

Hs.578973

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IXD	NMR	-	A	460-550	[»]
1WHL	NMR	-	A	125-206	[»]
1WHM	NMR	-	A	228-304	[»]
2VHF	X-ray	2.80	A/B	583-956	[»]

SMR

Q9NQC7. Positions 420-540.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9NQC7.

Protein family/group databases

MEROPS

C67.001.

PTM databases

PhosphoSite

Q9NQC7.

Proteomic databases

PRIDE

Q9NQC7.

Genome annotation databases

Ensembl

ENST00000311559; ENSP00000308928; ENSG00000083799; Homo sapiens. [Genome view]

GeneID

1540.

KEGG

hsa:1540.

UCSC

uc002egp.1. human.
uc002egq.1. human.

Organism-specific databases

CTD

1540.

GeneCards

GC16P049333.

HGNC

HGNC:2584. CYLD.

HPA

CAB011713.

MIM

132700. phenotype.
601606. phenotype.
605018. gene.
605041. phenotype.

Orphanet

79493. Brooke-Spiegler syndrome.
211. Cylindromatosis, familial.
867. Trichoepithelioma multiple, familial.

PharmGKB

PA27084.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06812.

HOGENOM

HBG357068.

HOVERGEN

Q9NQC7.

InParanoid

Q9NQC7.

OMA

GVQLCSF.

OrthoDB

EOG9MSGJC.

Enzyme and pathway databases

BRENDA

3.1.2.15. 247.

Pathway_Interaction_DB

nfkappabcanonicalpathway. Canonical NF-kappaB pathway.
tnfpathway. TNF receptor signaling pathway.

Gene expression databases

ArrayExpress

Q9NQC7.

Bgee

Q9NQC7.

CleanEx

HS_CYLD.

Genevestigator

Q9NQC7.

GermOnline

ENSG00000083799. Homo sapiens.

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...

Other Resources

NextBio

6377.

SOURCE

Search...

Entry information

Entry name

CYLD_HUMAN

Accession

Primary (citable) accession number: Q9NQC7
Secondary accession number(s): O94934 , Q7L3N6, Q96EH0, Q9NZX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	October 1, 2000
Last modified:	January 19, 2010
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.