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Protein

E3 ubiquitin-protein ligase TRIM21

Gene

TRIM21

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1 and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy. Acts as an autophagy receptor for the degradation of IRF3, hence attenuating type I interferon (IFN)-dependent immune responses (PubMed:26347139).10 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 5540RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri92 – 12332B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • ligase activity Source: UniProtKB-KW
  • RNA binding Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cytokine-mediated signaling pathway Source: Reactome
  • innate immune response Source: UniProtKB
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • negative regulation of protein deubiquitination Source: UniProtKB
  • negative regulation of viral release from host cell Source: UniProtKB
  • negative regulation of viral transcription Source: UniProtKB
  • positive regulation of autophagy Source: UniProtKB
  • positive regulation of cell cycle Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • positive regulation of type I interferon production Source: Reactome
  • positive regulation of viral entry into host cell Source: Ensembl
  • protein autoubiquitination Source: UniProtKB
  • protein destabilization Source: UniProtKB
  • protein monoubiquitination Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
  • protein trimerization Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • regulation of type I interferon production Source: Reactome
  • response to interferon-gamma Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Ribonucleoprotein

Keywords - Biological processi

Cell cycle, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-1834941. STING mediated induction of host immune responses.
R-HSA-3134975. Regulation of innate immune responses to cytosolic DNA.
R-HSA-877300. Interferon gamma signaling.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:TRIM21
Synonyms:RNF81, RO52, SSA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:11312. TRIM21.

Subcellular locationi

GO - Cellular componenti

  • autophagosome Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB-SubCell
  • cytoplasmic vesicle Source: UniProtKB-KW
  • cytosol Source: Reactome
  • intracellular ribonucleoprotein complex Source: ProtInc
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161C → A: Loss of E3 ubiquitin-protein ligase activity. Does not inhibit NF-kappa-B-induced gene expression. 3 Publications

Organism-specific databases

PharmGKBiPA36136.

Polymorphism and mutation databases

BioMutaiTRIM21.
DMDMi133250.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475E3 ubiquitin-protein ligase TRIM21PRO_0000056115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661PhosphoserineCombined sources

Post-translational modificationi

Autoubiquitinated; does not lead to its proteasomal degradation. Deubiquitinated by USP4; leading to its stabilization.5 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP19474.
MaxQBiP19474.
PaxDbiP19474.
PRIDEiP19474.

PTM databases

iPTMnetiP19474.
PhosphoSiteiP19474.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are expressed in fetal and adult heart and fetal lung.

Inductioni

Up-regulated by isoform 2 of XBP1. Up-regulated by IFNG/interferon-gamma, with a peak after 2-4 hours of treatment in monocytes/macrophages.1 Publication

Gene expression databases

BgeeiP19474.
CleanExiHS_TRIM21.
ExpressionAtlasiP19474. baseline and differential.
GenevisibleiP19474. HS.

Organism-specific databases

HPAiCAB004566.
HPA005673.

Interactioni

Subunit structurei

Homotrimer (PubMed:17156811) (PubMed:26347139). 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). Interacts with ULK1, BECN1 and with ATG8 family members, including GABARAP, GABARAPL1, GABARAPL2 and MAP1LC3C/LC3C. Interacts with TRIM21 and SQSTM1/sequestosome 1. Interacts with IRF3 (PubMed:26347139).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-81290,EBI-81290
GRAPQ135883EBI-81290,EBI-2847510
TRIM39Q9HCM94EBI-81290,EBI-739510
TXN2Q997573EBI-81290,EBI-2932492
UBE2IQ7KZS03EBI-81290,EBI-10180829
USP15Q9Y4E83EBI-81290,EBI-1043104
USP4Q13107-13EBI-81290,EBI-723305

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi112615. 79 interactions.
IntActiP19474. 41 interactions.
MINTiMINT-1462811.
STRINGi9606.ENSP00000254436.

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni293 – 2953Combined sources
Beta strandi300 – 3023Combined sources
Beta strandi308 – 3114Combined sources
Beta strandi327 – 3293Combined sources
Beta strandi331 – 3344Combined sources
Beta strandi337 – 34711Combined sources
Beta strandi354 – 3607Combined sources
Turni373 – 3764Combined sources
Beta strandi377 – 3837Combined sources
Turni384 – 3863Combined sources
Beta strandi387 – 3904Combined sources
Beta strandi396 – 3983Combined sources
Beta strandi405 – 4128Combined sources
Turni413 – 4164Combined sources
Beta strandi417 – 4226Combined sources
Turni423 – 4275Combined sources
Beta strandi429 – 4335Combined sources
Beta strandi442 – 4476Combined sources
Beta strandi460 – 4623Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IWGX-ray2.35B/E287-465[»]
ProteinModelPortaliP19474.
SMRiP19474. Positions 10-127, 130-471.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19474.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini268 – 465198B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili128 – 238111Sequence analysisAdd
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 5540RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri92 – 12332B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00760000118893.
HOGENOMiHOG000234133.
HOVERGENiHBG001357.
InParanoidiP19474.
KOiK10651.
OMAiLEVEIAM.
PhylomeDBiP19474.
TreeFamiTF338674.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR003613. Ubox_domain.
IPR000315. Znf_B-box.
IPR020457. Znf_B-box_chordata.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01406. BBOXZNFINGER.
PR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
SM00504. Ubox. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P19474-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASAARLTMM WEEVTCPICL DPFVEPVSIE CGHSFCQECI SQVGKGGGSV
60 70 80 90 100
CPVCRQRFLL KNLRPNRQLA NMVNNLKEIS QEAREGTQGE RCAVHGERLH
110 120 130 140 150
LFCEKDGKAL CWVCAQSRKH RDHAMVPLEE AAQEYQEKLQ VALGELRRKQ
160 170 180 190 200
ELAEKLEVEI AIKRADWKKT VETQKSRIHA EFVQQKNFLV EEEQRQLQEL
210 220 230 240 250
EKDEREQLRI LGEKEAKLAQ QSQALQELIS ELDRRCHSSA LELLQEVIIV
260 270 280 290 300
LERSESWNLK DLDITSPELR SVCHVPGLKK MLRTCAVHIT LDPDTANPWL
310 320 330 340 350
ILSEDRRQVR LGDTQQSIPG NEERFDSYPM VLGAQHFHSG KHYWEVDVTG
360 370 380 390 400
KEAWDLGVCR DSVRRKGHFL LSSKSGFWTI WLWNKQKYEA GTYPQTPLHL
410 420 430 440 450
QVPPCQVGIF LDYEAGMVSF YNITDHGSLI YSFSECAFTG PLRPFFSPGF
460 470
NDGGKNTAPL TLCPLNIGSQ GSTDY
Length:475
Mass (Da):54,170
Last modified:February 1, 1991 - v1
Checksum:iDDFF2944AFC629FB
GO
Isoform 2 (identifier: P19474-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:398
Mass (Da):45,057
Checksum:i552986C67B78356F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101M → T in AAU89982 (Ref. 6) Curated
Sequence conflicti189 – 1891L → P in AAU89982 (Ref. 6) Curated
Sequence conflicti216 – 2161A → T in AAU89982 (Ref. 6) Curated
Sequence conflicti262 – 2621L → V in AAU89982 (Ref. 6) Curated
Sequence conflicti313 – 3131D → V in AAU89982 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521P → A.1 Publication
Corresponds to variant rs1042302 [ dbSNP | Ensembl ].
VAR_013749
Natural varianti88 – 881Q → K.
Corresponds to variant rs58403334 [ dbSNP | Ensembl ].
VAR_061821
Natural varianti96 – 961G → R.1 Publication
Corresponds to variant rs2975162 [ dbSNP | Ensembl ].
VAR_013750
Natural varianti231 – 2311E → K.
Corresponds to variant rs2554934 [ dbSNP | Ensembl ].
VAR_013751

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei169 – 24577Missing in isoform 2. CuratedVSP_039627Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44525.1. [P19474-1]
PIRiA55642. A37241.
RefSeqiNP_003132.2. NM_003141.3. [P19474-1]
XP_006718346.1. XM_006718283.2. [P19474-2]
UniGeneiHs.532357.

Genome annotation databases

EnsembliENST00000254436; ENSP00000254436; ENSG00000132109. [P19474-1]
GeneIDi6737.
KEGGihsa:6737.
UCSCiuc001lyy.2. human. [P19474-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44525.1. [P19474-1]
PIRiA55642. A37241.
RefSeqiNP_003132.2. NM_003141.3. [P19474-1]
XP_006718346.1. XM_006718283.2. [P19474-2]
UniGeneiHs.532357.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IWGX-ray2.35B/E287-465[»]
ProteinModelPortaliP19474.
SMRiP19474. Positions 10-127, 130-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112615. 79 interactions.
IntActiP19474. 41 interactions.
MINTiMINT-1462811.
STRINGi9606.ENSP00000254436.

PTM databases

iPTMnetiP19474.
PhosphoSiteiP19474.

Polymorphism and mutation databases

BioMutaiTRIM21.
DMDMi133250.

Proteomic databases

EPDiP19474.
MaxQBiP19474.
PaxDbiP19474.
PRIDEiP19474.

Protocols and materials databases

DNASUi6737.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254436; ENSP00000254436; ENSG00000132109. [P19474-1]
GeneIDi6737.
KEGGihsa:6737.
UCSCiuc001lyy.2. human. [P19474-1]

Organism-specific databases

CTDi6737.
GeneCardsiTRIM21.
HGNCiHGNC:11312. TRIM21.
HPAiCAB004566.
HPA005673.
MIMi109092. gene.
neXtProtiNX_P19474.
PharmGKBiPA36136.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00760000118893.
HOGENOMiHOG000234133.
HOVERGENiHBG001357.
InParanoidiP19474.
KOiK10651.
OMAiLEVEIAM.
PhylomeDBiP19474.
TreeFamiTF338674.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-1834941. STING mediated induction of host immune responses.
R-HSA-3134975. Regulation of innate immune responses to cytosolic DNA.
R-HSA-877300. Interferon gamma signaling.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiP19474.
GeneWikiiTRIM21.
GenomeRNAii6737.
NextBioi26280.
PROiP19474.
SOURCEiSearch...

Gene expression databases

BgeeiP19474.
CleanExiHS_TRIM21.
ExpressionAtlasiP19474. baseline and differential.
GenevisibleiP19474. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR003613. Ubox_domain.
IPR000315. Znf_B-box.
IPR020457. Znf_B-box_chordata.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01406. BBOXZNFINGER.
PR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
SM00504. Ubox. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPA5.
  12. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOUBIQUITINATION, INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, INTERACTION WITH SKP2; SKP1; CUL1 AND FBXW11.
  16. Cited for: HOMOMERIZATION, SUBCELLULAR LOCATION.
  17. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DCP2, SUBCELLULAR LOCATION.
  18. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, COILED-COIL DOMAIN, DOMAIN B30.2/SPRY.
  19. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IRF3.
  20. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VCP, AUTOUBIQUITINATION, SUBCELLULAR LOCATION.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IKBKB, MUTAGENESIS OF CYS-16.
  23. "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] [Europe PMC] [Abstract]
    Cited for: ANTIGENICITY.
  24. "Dynamic movements of Ro52 cytoplasmic bodies along microtubules."
    Tanaka M., Tanji K., Niida M., Kamitani T.
    Histochem. Cell Biol. 133:273-284(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  25. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity."
    Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T., Deretic V.
    J. Cell Biol. 210:973-989(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY IFNG, INTERACTION WITH MEFV; BECN1; GABARAP; GABARAPL1; GABARAPL2; IRF3; MAP1LC3C; SQSTM1 AND ULK1, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRO52_HUMAN
AccessioniPrimary (citable) accession number: P19474
Secondary accession number(s): Q5XPV5, Q96RF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 11, 2016
This is version 181 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.