Reviewed, UniProtKB/Swiss-Prot P19474 (RO52_HUMAN)

Names and origin

Protein names

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

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.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Ribonucleoprotein particle composed of a single polypeptide and one of four small RNA molecules. It is present in all mammalian cells studied but has no known function. 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.
Subcellular location	Cytoplasm. Nucleus.
Involvement in disease	Sera from patients with systemic lupus erythematosus (SLE) or primary Sjoegren syndrome often contain antibodies that react with normal cellular RO protein as if this antigen was foreign.
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
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Disease	Systemic lupus erythematosus
Domain	Coiled coil Zinc-finger
Ligand	DNA-binding Metal-binding RNA-binding Zinc
Molecular function	Ribonucleoprotein
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein trimerization Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA ribonucleoprotein complex Traceable author statement. Source: ProtInc
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. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 475

475

52 kDa Ro protein

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.7

Natural variations

Natural variant

52

1

P → A: dbSNP rs1042302. Ref.2

VAR_013749

Natural variant

96

1

G → R: dbSNP rs2975162. Ref.5

VAR_013750

Natural variant

231

1

E → K: dbSNP rs2554934.

VAR_013751

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)
	P19474-1 [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

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]. 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], 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].
[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].
[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]	"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]. Tissue: Pancreas.
[7]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
BC010861 mRNA. Translation: AAH10861.1.

IPI

IPI00018971.

PIR

A37241. A55642.

RefSeq

NP_003132.2.

UniGene

Hs.532357

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P19474. 5 interactions.

PTM databases

PhosphoSite

P19474.

Proteomic databases

PRIDE

P19474.

Genome annotation databases

Ensembl

ENSG00000132109. Homo sapiens. [Contig view]

GeneID

6737.

KEGG

hsa:6737.

Organism-specific databases

GeneCards

GC11M004363.

H-InvDB

HIX0009382.

HGNC

HGNC:11312. TRIM21.

HPA

CAB004566.
HPA005673.

MIM

109092. gene.

PharmGKB

PA36136.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P19474.

HOVERGEN

P19474.

Gene expression databases

ArrayExpress

P19474.

Bgee

P19474.

CleanEx

HS_TRIM21.

GermOnline

ENSG00000132109. Homo sapiens.

Family and domain databases

InterPro

IPR001870. B302.
IPR003879. Butyrophylin.
IPR006574. PRY.
IPR018355. SPla/RYanodine_receptor_sg.
IPR003877. SPRY_rcpt.
IPR000315. Znf_B-box.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

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

PRINTS

PR01407. BUTYPHLNCDUF.

SMART

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

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 Resources

NextBio

26280.

SOURCE

Search...

Entry information

Entry name

RO52_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)