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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)DescriptionActionsGraphical viewLength
Zinc fingeri16 – 55RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri92 – 123B box-typePROSITE-ProRule annotationAdd BLAST32

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
  • 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
  • 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

BioCyciZFISH:ENSG00000132109-MONOMER.
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.
SIGNORiP19474.
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)DescriptionActionsGraphical viewLength
Mutagenesisi16C → A: Loss of E3 ubiquitin-protein ligase activity. Does not inhibit NF-kappa-B-induced gene expression. 3 Publications1

Organism-specific databases

DisGeNETi6737.
OpenTargetsiENSG00000132109.
PharmGKBiPA36136.

Polymorphism and mutation databases

BioMutaiTRIM21.
DMDMi133250.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000561151 – 475E3 ubiquitin-protein ligase TRIM21Add BLAST475

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei266PhosphoserineCombined sources1

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.
PeptideAtlasiP19474.
PRIDEiP19474.

PTM databases

iPTMnetiP19474.
PhosphoSitePlusiP19474.

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

BgeeiENSG00000132109.
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
itself5EBI-81290,EBI-81290
GRAPQ135885EBI-81290,EBI-2847510
TRIM3O753824EBI-81290,EBI-2129889
TRIM39Q9HCM94EBI-81290,EBI-739510
TRIM39Q9HCM9-24EBI-81290,EBI-11523450
TXN2Q997575EBI-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. 90 interactors.
IntActiP19474. 51 interactors.
MINTiMINT-1462811.
STRINGi9606.ENSP00000254436.

Structurei

Secondary structure

1475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni293 – 295Combined sources3
Beta strandi300 – 302Combined sources3
Beta strandi308 – 311Combined sources4
Beta strandi327 – 329Combined sources3
Beta strandi331 – 334Combined sources4
Beta strandi337 – 347Combined sources11
Beta strandi354 – 360Combined sources7
Turni373 – 376Combined sources4
Beta strandi377 – 383Combined sources7
Turni384 – 386Combined sources3
Beta strandi387 – 390Combined sources4
Beta strandi396 – 398Combined sources3
Beta strandi405 – 412Combined sources8
Turni413 – 416Combined sources4
Beta strandi417 – 422Combined sources6
Turni423 – 427Combined sources5
Beta strandi429 – 433Combined sources5
Beta strandi442 – 447Combined sources6
Beta strandi460 – 462Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IWGX-ray2.35B/E287-465[»]
ProteinModelPortaliP19474.
SMRiP19474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19474.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini268 – 465B30.2/SPRYPROSITE-ProRule annotationAdd BLAST198

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili128 – 238Sequence analysisAdd BLAST111

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)DescriptionActionsGraphical viewLength
Zinc fingeri16 – 55RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri92 – 123B box-typePROSITE-ProRule annotationAdd BLAST32

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00760000118893.
HOGENOMiHOG000234133.
HOVERGENiHBG001357.
InParanoidiP19474.
KOiK10651.
OMAiVEIAMKR.
OrthoDBiEOG091G05W2.
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)DescriptionActionsGraphical viewLength
Sequence conflicti10M → T in AAU89982 (Ref. 6) Curated1
Sequence conflicti189L → P in AAU89982 (Ref. 6) Curated1
Sequence conflicti216A → T in AAU89982 (Ref. 6) Curated1
Sequence conflicti262L → V in AAU89982 (Ref. 6) Curated1
Sequence conflicti313D → V in AAU89982 (Ref. 6) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01374952P → A.1 PublicationCorresponds to variant rs1042302dbSNPEnsembl.1
Natural variantiVAR_06182188Q → K.Corresponds to variant rs58403334dbSNPEnsembl.1
Natural variantiVAR_01375096G → R.1 PublicationCorresponds to variant rs2975162dbSNPEnsembl.1
Natural variantiVAR_013751231E → K.Corresponds to variant rs2554934dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_039627169 – 245Missing in isoform 2. CuratedAdd BLAST77

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]
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]
UniGeneiHs.532357.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IWGX-ray2.35B/E287-465[»]
ProteinModelPortaliP19474.
SMRiP19474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112615. 90 interactors.
IntActiP19474. 51 interactors.
MINTiMINT-1462811.
STRINGi9606.ENSP00000254436.

PTM databases

iPTMnetiP19474.
PhosphoSitePlusiP19474.

Polymorphism and mutation databases

BioMutaiTRIM21.
DMDMi133250.

Proteomic databases

EPDiP19474.
MaxQBiP19474.
PaxDbiP19474.
PeptideAtlasiP19474.
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.
DisGeNETi6737.
GeneCardsiTRIM21.
HGNCiHGNC:11312. TRIM21.
HPAiCAB004566.
HPA005673.
MIMi109092. gene.
neXtProtiNX_P19474.
OpenTargetsiENSG00000132109.
PharmGKBiPA36136.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00760000118893.
HOGENOMiHOG000234133.
HOVERGENiHBG001357.
InParanoidiP19474.
KOiK10651.
OMAiVEIAMKR.
OrthoDBiEOG091G05W2.
PhylomeDBiP19474.
TreeFamiTF338674.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000132109-MONOMER.
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.
SIGNORiP19474.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000132109.
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...

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: November 30, 2016
This is version 187 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.