P19474 (RO52_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase TRIM21
EC=6.3.2.-

Alternative name(s):
52 kDa Ro protein
52 kDa ribonucleoprotein autoantigen Ro/SS-A
RING finger protein 81
Ro(SS-A)
Sjoegren syndrome type A antigen
Short name=SS-A
Tripartite motif-containing protein 21

Gene names

Name:	TRIM21
Synonyms:	RNF81, RO52, SSA1

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	475 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts (via C-terminus) with IRF8 (via C-terminus) By similarity. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Interacts with CALR, CUL1, FBXW11, HSPA5, IKBKB, IRF3, SKP1 and VCP. Interacts with SKP2; the interaction with SKP2 does not depend on an intact F-box domain. Interacts (via N-terminus and C-terminus) with DCP2 (via N-terminus and C-terminus). Ref.10 Ref.11 Ref.15 Ref.16 Ref.18 Ref.19 Ref.21
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › P-body. Note: Enters the nucleus upon exposure to nitric oxide. Localizes to small dot- or rod-like structures in the cytoplasm, called cytoplasmic bodies (P-body) that are located underneath the plasma membrane and also diffusely in the cytoplasm and are highly motil in cells. Cytoplasmic bodies are located along the microtubules and do not share the same cytoplasmic bodies with TRIM5. Colocalizes with DCP2 in P-body. Ref.16 Ref.17 Ref.19 Ref.23
Tissue specificity	Isoforms 1 and 2 are expressed in fetal and adult heart and fetal lung.
Induction	Up-regulated by isoform 2 of XBP1.
Domain	The coiled-coil is necessary for the cytoplasmic localization. The B30.2/SPRY domain is necessary for the cytoplasmic localization, the interaction with IRF3 and for the IRF3-driven interferon beta promoter activity. The RING-type zinc finger is necessary for ubiquitination and for the IRF3-driven interferon beta promoter activity. Interacts with SKP2 and CUL1 in a RING finger-independent manner. Ref.17
Post-translational modification	Autoubiquitinated; does not lead to its proteasomal degradation. Deubiquitinated by USP4; leading to its stabilization.
Sequence similarities	Belongs to the TRIM/RBCC family. Contains 1 B box-type zinc finger. Contains 1 B30.2/SPRY domain. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Cell cycle Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	DNA-binding Metal-binding RNA-binding Zinc
Molecular function	Ligase Ribonucleoprotein
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of NF-kappaB transcription factor activity Inferred from direct assay Ref.21. Source: UniProtKB negative regulation of protein deubiquitination Inferred from mutant phenotype Ref.14. Source: UniProtKB positive regulation of cell cycle Inferred from mutant phenotype Ref.15. Source: UniProtKB protein autoubiquitination Inferred from direct assay Ref.15. Source: UniProtKB protein destabilization Inferred from mutant phenotype Ref.15. Source: UniProtKB protein monoubiquitination Inferred from direct assay Ref.12Ref.21. Source: UniProtKB protein polyubiquitination Inferred from direct assay Ref.12. Source: UniProtKB protein trimerization Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasmic mRNA processing body Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.17. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.15Ref.21Ref.10. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay Ref.12Ref.14Ref.15Ref.17Ref.21. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
USP4	Q13107-1	3	EBI-81290,EBI-723305

Alternative products

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

Isoform 1 (identifier: P19474-1)

Also known as: Ro52alpha; 52alpha;

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: P19474-2)

Also known as: Ro52beta; 52beta;

The sequence of this isoform differs from the canonical sequence as follows:
     169-245: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 475

475

E3 ubiquitin-protein ligase TRIM21

PRO_0000056115

Regions

Domain

268 – 465

198

B30.2/SPRY

Zinc finger

16 – 55

40

RING-type

Zinc finger

92 – 123

32

B box-type

Coiled coil

128 – 238

111

Potential

Amino acid modifications

Modified residue

266

1

Phosphoserine Ref.20

Natural variations

Alternative sequence

169 – 245

77

Missing in isoform 2.

VSP_039627

Natural variant

52

1

P → A. Ref.2
Corresponds to variant rs1042302 [ dbSNP | Ensembl ].

VAR_013749

Natural variant

88

1

Q → K.
Corresponds to variant rs58403334 [ dbSNP | Ensembl ].

VAR_061821

Natural variant

96

1

G → R. Ref.5
Corresponds to variant rs2975162 [ dbSNP | Ensembl ].

VAR_013750

Natural variant

231

1

E → K.
Corresponds to variant rs2554934 [ dbSNP | Ensembl ].

VAR_013751

Experimental info

Mutagenesis

16

1

C → A: Loss of E3 ubiquitin-protein ligase activity. Does not inhibit NF-kappa-B-induced gene expression. Ref.12 Ref.14 Ref.21

Sequence conflict

10

1

M → T in AAU89982. Ref.6

Sequence conflict

189

1

L → P in AAU89982. Ref.6

Sequence conflict

216

1

A → T in AAU89982. Ref.6

Sequence conflict

262

1

L → V in AAU89982. Ref.6

Sequence conflict

313

1

D → V in AAU89982. Ref.6

Secondary structure

1

.

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475

Helix Strand Turn

Details...

Turn

293 – 295

3

Beta strand

300 – 302

3

Beta strand

308 – 311

4

Beta strand

327 – 329

3

Beta strand

331 – 334

4

Beta strand

337 – 347

11

Beta strand

354 – 360

7

Turn

373 – 376

4

Beta strand

377 – 383

7

Turn

384 – 386

3

Beta strand

387 – 390

4

Beta strand

396 – 398

3

Beta strand

405 – 412

8

Turn

413 – 416

4

Beta strand

417 – 422

6

Turn

423 – 427

5

Beta strand

429 – 433

5

Beta strand

442 – 447

6

Beta strand

460 – 462

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Ro52alpha) (52alpha) [UniParc]. Last modified February 1, 1991. Version 1. Checksum: DDFF2944AFC629FB	FASTA	475	54,170
	10 20 30 40 50 60 MASAARLTMM WEEVTCPICL DPFVEPVSIE CGHSFCQECI SQVGKGGGSV CPVCRQRFLL 70 80 90 100 110 120 KNLRPNRQLA NMVNNLKEIS QEAREGTQGE RCAVHGERLH LFCEKDGKAL CWVCAQSRKH 130 140 150 160 170 180 RDHAMVPLEE AAQEYQEKLQ VALGELRRKQ ELAEKLEVEI AIKRADWKKT VETQKSRIHA 190 200 210 220 230 240 EFVQQKNFLV EEEQRQLQEL EKDEREQLRI LGEKEAKLAQ QSQALQELIS ELDRRCHSSA 250 260 270 280 290 300 LELLQEVIIV LERSESWNLK DLDITSPELR SVCHVPGLKK MLRTCAVHIT LDPDTANPWL 310 320 330 340 350 360 ILSEDRRQVR LGDTQQSIPG NEERFDSYPM VLGAQHFHSG KHYWEVDVTG KEAWDLGVCR 370 380 390 400 410 420 DSVRRKGHFL LSSKSGFWTI WLWNKQKYEA GTYPQTPLHL QVPPCQVGIF LDYEAGMVSF 430 440 450 460 470 YNITDHGSLI YSFSECAFTG PLRPFFSPGF NDGGKNTAPL TLCPLNIGSQ GSTDY
	Isoform 2 (Ro52beta) (52beta) [UniParc]. Checksum: 552986C67B78356F	FASTA	398	45,057
	10 20 30 40 50 60 MASAARLTMM WEEVTCPICL DPFVEPVSIE CGHSFCQECI SQVGKGGGSV CPVCRQRFLL 70 80 90 100 110 120 KNLRPNRQLA NMVNNLKEIS QEAREGTQGE RCAVHGERLH LFCEKDGKAL CWVCAQSRKH 130 140 150 160 170 180 RDHAMVPLEE AAQEYQEKLQ VALGELRRKQ ELAEKLEVEI AIKRADWKEV IIVLERSESW 190 200 210 220 230 240 NLKDLDITSP ELRSVCHVPG LKKMLRTCAV HITLDPDTAN PWLILSEDRR QVRLGDTQQS 250 260 270 280 290 300 IPGNEERFDS YPMVLGAQHF HSGKHYWEVD VTGKEAWDLG VCRDSVRRKG HFLLSSKSGF 310 320 330 340 350 360 WTIWLWNKQK YEAGTYPQTP LHLQVPPCQV GIFLDYEAGM VSFYNITDHG SLIYSFSECA 370 380 390 FTGPLRPFFS PGFNDGGKNT APLTLCPLNI GSQGSTDY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Protein heterogeneity in the human Ro/SSA ribonucleoproteins. The 52- and 60-kD Ro/SSA autoantigens are encoded by separate genes." Itoh K., Itoh Y., Frank M.B. J. Clin. Invest. 87:177-186(1991) [PubMed: 1985094] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Thymocyte.
[2]	"Molecular definition and sequence motifs of the 52-kD component of human SS-A/Ro autoantigen." Chan E.K., Hamel J.C., Buyon J.P., Tan E.M. J. Clin. Invest. 87:68-76(1991) [PubMed: 1985112] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT ALA-52.
[3]	"The location of a disease-associated polymorphism and genomic structure of the human 52-kDa Ro/SSA locus (SSA1)." Tsugu H., Horowitz R., Gibson N., Frank M.B. Genomics 24:541-548(1994) [PubMed: 7713506] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]	"Structural differences between the human and mouse 52-kD Ro autoantigens associated with poorly conserved autoantibody activity across species." Keech C.L., Gordon T.P., McCluskey J. Clin. Exp. Immunol. 104:255-263(1996) [PubMed: 8625517] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region." Bepler G., O'Briant K.C., Kim Y.-C., Schreiber G., Pitterle D.M. Genomics 55:164-175(1999) [PubMed: 9933563] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-96.
[6]	"Isolation of human Sjogren syndrome type A antigen cDNA clone from HEp-2 cells, isolate 1." Chen Y.-J., Fan Y.-H., Chiou S.-H. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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 1). Tissue: Pancreas.
[9]	"52-kD SS-A/Ro: genomic structure and identification of an alternatively spliced transcript encoding a novel leucine zipper-minus autoantigen expressed in fetal and adult heart." Chan E.K., Di Donato F., Hamel J.C., Tseng C.E., Buyon J.P. J. Exp. Med. 182:983-992(1995) [PubMed: 7561701] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
[10]	"Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen." Cheng S.T., Nguyen T.Q., Yang Y.S., Capra J.D., Sontheimer R.D. J. Immunol. 156:4484-4491(1996) [PubMed: 8666824] [Abstract] Cited for: INTERACTION WITH CALR.
[11]	"Association of stress proteins with autoantigens: a possible mechanism for triggering autoimmunity?" Purcell A.W., Todd A., Kinoshita G., Lynch T.A., Keech C.L., Gething M.J., Gordon T.P. Clin. Exp. Immunol. 132:193-200(2003) [PubMed: 12699405] [Abstract] Cited for: INTERACTION WITH HSPA5.
[12]	"Autoantigen Ro52 is an E3 ubiquitin ligase." Wada K., Kamitani T. Biochem. Biophys. Res. Commun. 339:415-421(2006) [PubMed: 16297862] [Abstract] Cited for: FUNCTION, AUTOUBIQUITINATION, MUTAGENESIS OF CYS-16.
[13]	"Oncogenic protein UnpEL/Usp4 deubiquitinates Ro52 by its isopeptidase activity." Wada K., Tanji K., Kamitani T. Biochem. Biophys. Res. Commun. 339:731-736(2006) [PubMed: 16316627] [Abstract] Cited for: FUNCTION, DEUBIQUITINATION BY USP4.
[14]	"UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself." Wada K., Kamitani T. Biochem. Biophys. Res. Commun. 342:253-258(2006) [PubMed: 16472766] [Abstract] Cited for: FUNCTION, AUTOUBIQUITINATION, DEUBIQUITINATION BY USP4, MUTAGENESIS OF CYS-16.
[15]	"Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein." Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M., Krek W. Mol. Cell. Biol. 26:5994-6004(2006) [PubMed: 16880511] [Abstract] Cited for: FUNCTION, AUTOUBIQUITINATION, INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, INTERACTION WITH SKP2; SKP1; CUL1 AND FBXW11.
[16]	"SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping activity." Yamochi T., Ohnuma K., Hosono O., Tanaka H., Kanai Y., Morimoto C. Biochem. Biophys. Res. Commun. 370:195-199(2008) [PubMed: 18361920] [Abstract] Cited for: FUNCTION, INTERACTION WITH DCP2, SUBCELLULAR LOCATION.
[17]	"The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but enters the nucleus upon cellular exposure to nitric oxide." Espinosa A., Oke V., Elfving A., Nyberg F., Covacu R., Wahren-Herlenius M. Exp. Cell Res. 314:3605-3613(2008) [PubMed: 18845142] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN COILED COIL, DOMAIN B30.2/SPRY.
[18]	"The E3 ubiquitin ligase Ro52 negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3." Higgs R., Ni Gabhann J., Ben Larbi N., Breen E.P., Fitzgerald K.A., Jefferies C.A. J. Immunol. 181:1780-1786(2008) [PubMed: 18641315] [Abstract] Cited for: FUNCTION, INTERACTION WITH IRF3.
[19]	"Ro52 functionally interacts with IgG1 and regulates its quality control via the ERAD system." Takahata M., Bohgaki M., Tsukiyama T., Kondo T., Asaka M., Hatakeyama S. Mol. Immunol. 45:2045-2054(2008) [PubMed: 18022694] [Abstract] Cited for: FUNCTION, INTERACTION WITH VCP, AUTOUBIQUITINATION, SUBCELLULAR LOCATION.
[20]	"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-266, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Ro52-mediated monoubiquitination of IKK{beta} down-regulates NF-{kappa}B signalling." Wada K., Niida M., Tanaka M., Kamitani T. J. Biochem. 146:821-832(2009) [PubMed: 19675099] [Abstract] Cited for: FUNCTION, INTERACTION WITH IKBKB, MUTAGENESIS OF CYS-16.
[22]	"Extraordinary antigenicity of the human Ro52 autoantigen." Burbelo P.D., Ching K.H., Han B.L., Bush E.R., Reeves W.H., Iadarola M.J. Am. J. Transl. Res. 2:145-155(2010) [PubMed: 20407604] [Abstract] Cited for: ANTIGENICITY.
[23]	"Dynamic movements of Ro52 cytoplasmic bodies along microtubules." Tanaka M., Tanji K., Niida M., Kamitani T. Histochem. Cell Biol. 133:273-284(2010) [PubMed: 20013343] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34551 mRNA. Translation: AAA36581.1.
U01882 Genomic DNA. Translation: AAB87094.1.
M62800 mRNA. Translation: AAA36651.1.
U13658, U13657 Genomic DNA. Translation: AAA79867.1.
AF391283 Genomic DNA. Translation: AAK76432.1.
AY742713 mRNA. Translation: AAU89982.1.
AC009758 Genomic DNA. No translation available.
BC010861 mRNA. Translation: AAH10861.1.

IPI

IPI00018971.
IPI00969571.

PIR

A37241. A55642.

RefSeq

NP_003132.2. NM_003141.3.

UniGene

Hs.532357.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IWG	X-ray	2.35	B/E	287-465	[»]

ProteinModelPortal

P19474.

SMR

P19474. Positions 1-74, 84-128, 287-465.

ModBase

Search...

Protein-protein interaction databases

IntAct

P19474. 17 interactions.

MINT

MINT-1462811.

STRING

P19474.

PTM databases

PhosphoSite

P19474.

Polymorphism databases

DMDM

133250.

Proteomic databases

PRIDE

P19474.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000254436; ENSP00000254436; ENSG00000132109.

GeneID

6737.

KEGG

hsa:6737.

UCSC

uc001lyy.1. human.

Organism-specific databases

CTD

6737.

GeneCards

GC11M004363.

H-InvDB

HIX0009382.

HGNC

HGNC:11312. TRIM21.

HPA

CAB004566.
HPA005673.

MIM

109092. gene.

neXtProt

NX_P19474.

PharmGKB

PA36136.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17458.

GeneTree

ENSGT00600000084196.

HOGENOM

HBG755403.

HOVERGEN

HBG001357.

InParanoid

P19474.

OMA

KSGFWTI.

OrthoDB

EOG4KWJSP.

PhylomeDB

P19474.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P19474.

Bgee

P19474.

CleanEx

HS_TRIM21.

Genevestigator

P19474.

GermOnline

ENSG00000132109. Homo sapiens.

Family and domain databases

InterPro

IPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR008985. ConA-like_lec_gl.
IPR006574. PRY.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
IPR000315. Znf_B-box.
IPR020457. Znf_B-box_chordata.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]

Gene3D

G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.

KO

K10651.

Pfam

PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]

PRINTS

PR01406. BBOXZNFINGER.
PR01407. BUTYPHLNCDUF.

SMART

SM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

26280.

SOURCE

Search...

Entry information

Entry name

RO52_HUMAN

Accession

Primary (citable) accession number: P19474
Secondary accession number(s): Q5XPV5, Q96RF8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	January 25, 2012
This is version 133 of the entry and version 1 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.