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Protein

Ubiquitin-conjugating enzyme E2 D3

Gene

UBE2D3

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

Functioni

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction.14 Publications

Catalytic activityi

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.PROSITE-ProRule annotation1 Publication
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.1 Publication

Pathwayi: protein ubiquitination

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei85 – 851Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ubiquitin conjugating enzyme activity Source: ParkinsonsUK-UCL
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • BMP signaling pathway Source: Reactome
  • cellular protein modification process Source: ProtInc
  • DNA repair Source: UniProtKB-KW
  • negative regulation of transcription from RNA polymerase II promoter Source: Reactome
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein autoubiquitination Source: ParkinsonsUK-UCL
  • protein K11-linked ubiquitination Source: UniProtKB
  • protein K48-linked ubiquitination Source: UniProtKB
  • protein monoubiquitination Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  • TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  • ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Apoptosis, DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.3.2.B6. 2681.
ReactomeiR-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-201451. Signaling by BMP.
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
R-HSA-937041. IKK complex recruitment mediated by RIP1.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP61077.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 D3 (EC:2.3.2.231 Publication)
Alternative name(s):
(E3-independent) E2 ubiquitin-conjugating enzyme D3 (EC:2.3.2.241 Publication)
E2 ubiquitin-conjugating enzyme D3
Ubiquitin carrier protein D3
Ubiquitin-conjugating enzyme E2(17)KB 3
Ubiquitin-conjugating enzyme E2-17 kDa 3
Ubiquitin-protein ligase D3
Gene namesi
Name:UBE2D3
Synonyms:UBC5C, UBCH5C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:12476. UBE2D3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • endosome membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi77 – 771N → S: Activity is restricted HECT-type and not RING-containing E3 ubiquitin-protein ligases. Exhibits ubiquitin transfer with ARIH1 and PARK2. 1 Publication
Mutagenesisi85 – 851C → A: Loss of function. 1 Publication
Mutagenesisi87 – 871D → E or P: Has intermediate lysine reactivity. 1 Publication
Mutagenesisi87 – 871D → K: Abolishes affect lysine reactivity. 1 Publication
Mutagenesisi87 – 871D → N: Does not affect lysine reactivity. 1 Publication
Mutagenesisi117 – 1171D → H: Strongly impairs lysine reactivity but retains some ability to transfer ubiquitin to BRCA1. 1 Publication

Organism-specific databases

PharmGKBiPA37126.

Polymorphism and mutation databases

DMDMi46577654.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 147147Ubiquitin-conjugating enzyme E2 D3PRO_0000082466Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 1071 Publication

Post-translational modificationi

Phosphorylated by AURKB.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP61077.
MaxQBiP61077.
PaxDbiP61077.
PeptideAtlasiP61077.
PRIDEiP61077.
TopDownProteomicsiP61077-1. [P61077-1]
P61077-2. [P61077-2]

PTM databases

iPTMnetiP61077.
PhosphoSiteiP61077.

Expressioni

Gene expression databases

BgeeiENSG00000109332.
CleanExiHS_UBE2D3.
ExpressionAtlasiP61077. baseline and differential.
GenevisibleiP61077. HS.

Organism-specific databases

HPAiHPA003920.

Interactioni

Subunit structurei

Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex; when Cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened. Interacts with DAPK3. Interacts with BRCA1; the DNA damage checkpoint promotes the association with BRCA1 after ionizing radiation. Interacts non-covalently with ubiquitin. Interacts with E3 ubiquitin-protein ligase CBLC.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dapk3O547842EBI-348268,EBI-77359From a different organism.
DTX2Q4ZH493EBI-348268,EBI-10192429
DTX2Q86UW93EBI-348268,EBI-740376
MID1O153444EBI-348268,EBI-2340316
ospGQ99PZ66EBI-348268,EBI-9316527From a different organism.
OTUB1Q96FW19EBI-348268,EBI-1058491
RNF11Q9Y3C53EBI-348268,EBI-396669
RNF111Q6ZNA45EBI-348268,EBI-2129175
RNF115Q9Y4L54EBI-348268,EBI-2129242
RNF126Q9BV683EBI-348268,EBI-357322
RNF43Q68DV72EBI-348268,EBI-1647060
RNF5Q999426EBI-348268,EBI-348482
sspH2P0CE127EBI-348268,EBI-10761075From a different organism.
TRAF6Q9Y4K32EBI-348268,EBI-359276
TRIM39Q9HCM95EBI-348268,EBI-739510
XIAPP981702EBI-348268,EBI-517127
ZNRF1Q8ND253EBI-348268,EBI-2129250

Protein-protein interaction databases

BioGridi113171. 215 interactions.
DIPiDIP-29062N.
IntActiP61077. 104 interactions.
MINTiMINT-1032046.
STRINGi9606.ENSP00000381717.

Structurei

Secondary structure

147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1515Combined sources
Beta strandi21 – 266Combined sources
Beta strandi32 – 387Combined sources
Beta strandi41 – 433Combined sources
Turni44 – 474Combined sources
Beta strandi49 – 557Combined sources
Turni58 – 614Combined sources
Beta strandi66 – 694Combined sources
Beta strandi76 – 783Combined sources
Beta strandi80 – 845Combined sources
Helixi87 – 893Combined sources
Turni90 – 923Combined sources
Helixi99 – 11113Combined sources
Helixi121 – 1299Combined sources
Helixi131 – 14515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X23X-ray1.85A/B/C/D1-147[»]
2FUHNMR-A2-147[»]
3L1ZX-ray3.17A1-147[»]
3RPGX-ray2.65A2-147[»]
3UGBX-ray2.35A1-147[»]
4BVUX-ray2.70B1-147[»]
4R8PX-ray3.28L/N2-147[»]
4S3OX-ray2.00A/D2-147[»]
5IFRX-ray2.20A2-147[»]
ProteinModelPortaliP61077.
SMRiP61077. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61077.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0417. Eukaryota.
COG5078. LUCA.
GeneTreeiENSGT00760000119012.
HOVERGENiHBG063308.
InParanoidiP61077.
KOiK06689.
OMAiLYKTDRT.
OrthoDBiEOG091G0GF8.
PhylomeDBiP61077.
TreeFamiTF101108.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P61077-1) [UniParc]FASTAAdd to basket

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
MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF
60 70 80 90 100
FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS
110 120 130 140
KVLLSICSLL CDPNPDDPLV PEIARIYKTD RDKYNRISRE WTQKYAM
Length:147
Mass (Da):16,687
Last modified:April 26, 2004 - v1
Checksum:iADD74A8A708EFEE3
GO
Isoform 2 (identifier: P61077-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-147: YNRISREWTQKYAM → YNRLAREWTEKYAML

Show »
Length:148
Mass (Da):16,785
Checksum:iE73DC194DB6D4EFE
GO
Isoform 3 (identifier: P61077-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MALKRINK → MLSNRKCLSK

Show »
Length:149
Mass (Da):16,893
Checksum:iF20F36FCD312444A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501Missing in DB045280 (PubMed:14702039).Curated
Sequence conflicti123 – 1231I → L in AAH66917 (PubMed:15489334).Curated
Sequence conflicti137 – 1371I → V in CAG33197 (PubMed:14702039).Curated
Sequence conflicti147 – 1471M → I in CAG33197 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 88MALKRINK → MLSNRKCLSK in isoform 3. 1 PublicationVSP_038096
Alternative sequencei134 – 14714YNRIS…QKYAM → YNRLAREWTEKYAML in isoform 2. 1 PublicationVSP_038097Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39318 mRNA. Translation: AAA91461.1.
AF213884 Genomic DNA. Translation: AAF35234.1.
AK095822 mRNA. Translation: BAC04632.1.
DB045280 mRNA. No translation available.
CR456916 mRNA. Translation: CAG33197.1.
AC018797 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06138.1.
CH471057 Genomic DNA. Translation: EAX06143.1.
BC003395 mRNA. Translation: AAH03395.1.
BC037894 mRNA. Translation: AAH37894.1.
BC066917 mRNA. Translation: AAH66917.1.
CCDSiCCDS3659.1. [P61077-3]
CCDS3660.1. [P61077-1]
CCDS3661.1. [P61077-2]
RefSeqiNP_003331.1. NM_003340.6. [P61077-1]
NP_871615.1. NM_181886.3. [P61077-1]
NP_871616.1. NM_181887.2. [P61077-1]
NP_871617.1. NM_181888.3. [P61077-1]
NP_871618.1. NM_181889.2. [P61077-1]
NP_871619.1. NM_181890.2. [P61077-1]
NP_871620.1. NM_181891.2. [P61077-1]
NP_871621.1. NM_181892.3. [P61077-2]
NP_871622.1. NM_181893.2. [P61077-3]
UniGeneiHs.518773.
Hs.595430.
Hs.621366.

Genome annotation databases

EnsembliENST00000321805; ENSP00000318494; ENSG00000109332. [P61077-1]
ENST00000338145; ENSP00000337208; ENSG00000109332. [P61077-1]
ENST00000343106; ENSP00000345285; ENSG00000109332. [P61077-2]
ENST00000349311; ENSP00000344069; ENSG00000109332. [P61077-1]
ENST00000357194; ENSP00000349722; ENSG00000109332. [P61077-3]
ENST00000394801; ENSP00000378280; ENSG00000109332. [P61077-1]
ENST00000394803; ENSP00000378282; ENSG00000109332. [P61077-1]
ENST00000394804; ENSP00000378283; ENSG00000109332. [P61077-1]
ENST00000453744; ENSP00000396901; ENSG00000109332. [P61077-1]
GeneIDi7323.
KEGGihsa:7323.
UCSCiuc003hwi.5. human. [P61077-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39318 mRNA. Translation: AAA91461.1.
AF213884 Genomic DNA. Translation: AAF35234.1.
AK095822 mRNA. Translation: BAC04632.1.
DB045280 mRNA. No translation available.
CR456916 mRNA. Translation: CAG33197.1.
AC018797 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06138.1.
CH471057 Genomic DNA. Translation: EAX06143.1.
BC003395 mRNA. Translation: AAH03395.1.
BC037894 mRNA. Translation: AAH37894.1.
BC066917 mRNA. Translation: AAH66917.1.
CCDSiCCDS3659.1. [P61077-3]
CCDS3660.1. [P61077-1]
CCDS3661.1. [P61077-2]
RefSeqiNP_003331.1. NM_003340.6. [P61077-1]
NP_871615.1. NM_181886.3. [P61077-1]
NP_871616.1. NM_181887.2. [P61077-1]
NP_871617.1. NM_181888.3. [P61077-1]
NP_871618.1. NM_181889.2. [P61077-1]
NP_871619.1. NM_181890.2. [P61077-1]
NP_871620.1. NM_181891.2. [P61077-1]
NP_871621.1. NM_181892.3. [P61077-2]
NP_871622.1. NM_181893.2. [P61077-3]
UniGeneiHs.518773.
Hs.595430.
Hs.621366.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X23X-ray1.85A/B/C/D1-147[»]
2FUHNMR-A2-147[»]
3L1ZX-ray3.17A1-147[»]
3RPGX-ray2.65A2-147[»]
3UGBX-ray2.35A1-147[»]
4BVUX-ray2.70B1-147[»]
4R8PX-ray3.28L/N2-147[»]
4S3OX-ray2.00A/D2-147[»]
5IFRX-ray2.20A2-147[»]
ProteinModelPortaliP61077.
SMRiP61077. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113171. 215 interactions.
DIPiDIP-29062N.
IntActiP61077. 104 interactions.
MINTiMINT-1032046.
STRINGi9606.ENSP00000381717.

PTM databases

iPTMnetiP61077.
PhosphoSiteiP61077.

Polymorphism and mutation databases

DMDMi46577654.

Proteomic databases

EPDiP61077.
MaxQBiP61077.
PaxDbiP61077.
PeptideAtlasiP61077.
PRIDEiP61077.
TopDownProteomicsiP61077-1. [P61077-1]
P61077-2. [P61077-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321805; ENSP00000318494; ENSG00000109332. [P61077-1]
ENST00000338145; ENSP00000337208; ENSG00000109332. [P61077-1]
ENST00000343106; ENSP00000345285; ENSG00000109332. [P61077-2]
ENST00000349311; ENSP00000344069; ENSG00000109332. [P61077-1]
ENST00000357194; ENSP00000349722; ENSG00000109332. [P61077-3]
ENST00000394801; ENSP00000378280; ENSG00000109332. [P61077-1]
ENST00000394803; ENSP00000378282; ENSG00000109332. [P61077-1]
ENST00000394804; ENSP00000378283; ENSG00000109332. [P61077-1]
ENST00000453744; ENSP00000396901; ENSG00000109332. [P61077-1]
GeneIDi7323.
KEGGihsa:7323.
UCSCiuc003hwi.5. human. [P61077-1]

Organism-specific databases

CTDi7323.
GeneCardsiUBE2D3.
HGNCiHGNC:12476. UBE2D3.
HPAiHPA003920.
MIMi602963. gene.
neXtProtiNX_P61077.
PharmGKBiPA37126.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0417. Eukaryota.
COG5078. LUCA.
GeneTreeiENSGT00760000119012.
HOVERGENiHBG063308.
InParanoidiP61077.
KOiK06689.
OMAiLYKTDRT.
OrthoDBiEOG091G0GF8.
PhylomeDBiP61077.
TreeFamiTF101108.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B6. 2681.
ReactomeiR-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-201451. Signaling by BMP.
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
R-HSA-937041. IKK complex recruitment mediated by RIP1.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP61077.

Miscellaneous databases

ChiTaRSiUBE2D3. human.
EvolutionaryTraceiP61077.
GeneWikiiUBE2D3.
GenomeRNAii7323.
PROiP61077.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000109332.
CleanExiHS_UBE2D3.
ExpressionAtlasiP61077. baseline and differential.
GenevisibleiP61077. HS.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUB2D3_HUMAN
AccessioniPrimary (citable) accession number: P61077
Secondary accession number(s): A6NJ93
, A6NJB1, A6NM99, P47986, Q6IB88, Q6NXS4, Q8N924
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: September 7, 2016
This is version 139 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.