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Protein

SUMO-activating enzyme subunit 2

Gene

UBA2

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

Functioni

The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.6 Publications

Pathwayi: protein sumoylation

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei48ATP1 Publication1
Binding sitei72ATP1 Publication1
Metal bindingi158Zinc1
Metal bindingi161Zinc1
Active sitei173Glycyl thioester intermediatePROSITE-ProRule annotation2 Publications1
Metal bindingi441Zinc1
Metal bindingi444Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi24 – 29ATP1 Publication6
Nucleotide bindingi56 – 59ATP1 Publication4
Nucleotide bindingi95 – 96ATP1 Publication2
Nucleotide bindingi117 – 122ATP1 Publication6

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme activator activity Source: ProtInc
  • metal ion binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: UniProtKB
  • SUMO activating enzyme activity Source: UniProtKB

GO - Biological processi

  • protein sumoylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-HSA-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
SUMO-activating enzyme subunit 2 (EC:6.3.2.-)
Alternative name(s):
Anthracycline-associated resistance ARX
Ubiquitin-like 1-activating enzyme E1B
Ubiquitin-like modifier-activating enzyme 2
Gene namesi
Name:UBA2
Synonyms:SAE2, UBLE1B
ORF Names:HRIHFB2115
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:30661. UBA2.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Shuttles between the cytoplasm and the nucleus, sumoylation is required either for nuclear translocation or nuclear retention.

GO - Cellular componenti

  • cytosol Source: GO_Central
  • nucleoplasm Source: HPA
  • SUMO activating enzyme complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi56N → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication1
Mutagenesisi57L → A: Strongly reduces ATP-dependent activation of SUMO proteins. 1 Publication1
Mutagenesisi59R → A: Strongly reduces ATP-dependent activation of SUMO proteins. 1 Publication1
Mutagenesisi72K → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication1
Mutagenesisi117D → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication1
Mutagenesisi173C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi174T → A: Slightly reduced enzyme activity. 1 Publication1
Mutagenesisi184H → Q: No effect on enzyme activity. 1 Publication1
Mutagenesisi235I → A: Strongly reduced interaction with UBE2I; when associated with A-238. 1 Publication1
Mutagenesisi238I → A: Strongly reduced interaction with UBE2I; when associated with A-235. 1 Publication1
Mutagenesisi484Missing : Strongly reduced interaction with UBE2I. 1 Publication1
Mutagenesisi485G → GGGG: Strongly reduced interaction with UBE2I. 1 Publication1

Organism-specific databases

DisGeNETi10054.
OpenTargetsiENSG00000126261.
PharmGKBiPA162407583.

Chemistry databases

ChEMBLiCHEMBL2095174.

Polymorphism and mutation databases

BioMutaiUBA2.
DMDMi42559898.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001949681 – 640SUMO-activating enzyme subunit 2Add BLAST640

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki190Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei207PhosphoserineCombined sources1
Cross-linki236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Cross-linki236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei271N6-acetyllysine; alternateCombined sources1
Cross-linki271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei507PhosphoserineCombined sources1
Modified residuei592PhosphoserineCombined sources1
Cross-linki611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei613N6-acetyllysine; alternateBy similarity1
Cross-linki613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki617Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Sumoylated with SUMO1 and SUMO2/3 and by UBC9. Sumoylation at Lys-236 inhibits enzymatic activity. Sumoylation at the C-terminal lysine cluster plays an essential role in nuclear trafficking.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UBT2.
PaxDbiQ9UBT2.
PeptideAtlasiQ9UBT2.
PRIDEiQ9UBT2.

PTM databases

iPTMnetiQ9UBT2.
PhosphoSitePlusiQ9UBT2.
SwissPalmiQ9UBT2.

Expressioni

Gene expression databases

BgeeiENSG00000126261.
CleanExiHS_UBA2.
ExpressionAtlasiQ9UBT2. baseline and differential.
GenevisibleiQ9UBT2. HS.

Organism-specific databases

HPAiHPA041436.

Interactioni

Subunit structurei

Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds to the two domains that are encoded on a single polypeptide chain in ubiquitin-activating enzyme E1. Interacts with UBE2I.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
G2XKQ05EBI-718569,EBI-10175576
SAE1Q9UBE08EBI-718569,EBI-743154
SUMO1P631655EBI-718569,EBI-80140

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115365. 80 interactors.
DIPiDIP-35136N.
IntActiQ9UBT2. 15 interactors.
MINTiMINT-1405216.
STRINGi9606.ENSP00000246548.

Chemistry databases

BindingDBiQ9UBT2.

Structurei

Secondary structure

1640
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 17Combined sources9
Beta strandi19 – 23Combined sources5
Helixi27 – 39Combined sources13
Beta strandi43 – 48Combined sources6
Helixi54 – 58Combined sources5
Helixi65 – 67Combined sources3
Helixi72 – 81Combined sources10
Beta strandi88 – 94Combined sources7
Helixi103 – 106Combined sources4
Beta strandi110 – 114Combined sources5
Helixi119 – 132Combined sources14
Beta strandi136 – 142Combined sources7
Beta strandi145 – 151Combined sources7
Turni153 – 155Combined sources3
Beta strandi168 – 171Combined sources4
Turni172 – 176Combined sources5
Helixi182 – 197Combined sources16
Helixi202 – 204Combined sources3
Helixi213 – 215Combined sources3
Beta strandi225 – 227Combined sources3
Beta strandi234 – 236Combined sources3
Helixi241 – 246Combined sources6
Helixi251 – 259Combined sources9
Helixi261 – 266Combined sources6
Helixi270 – 272Combined sources3
Beta strandi274 – 276Combined sources3
Helixi284 – 289Combined sources6
Helixi308 – 310Combined sources3
Helixi315 – 335Combined sources21
Turni337 – 339Combined sources3
Helixi349 – 365Combined sources17
Helixi373 – 381Combined sources9
Helixi388 – 406Combined sources19
Helixi410 – 412Combined sources3
Beta strandi414 – 418Combined sources5
Beta strandi426 – 433Combined sources8
Turni442 – 444Combined sources3
Beta strandi445 – 447Combined sources3
Beta strandi449 – 454Combined sources6
Turni456 – 458Combined sources3
Helixi461 – 466Combined sources6
Helixi467 – 472Combined sources6
Beta strandi479 – 486Combined sources8
Beta strandi489 – 491Combined sources3
Beta strandi493 – 498Combined sources6
Helixi501 – 503Combined sources3
Helixi506 – 509Combined sources4
Beta strandi516 – 521Combined sources6
Turni522 – 525Combined sources4
Beta strandi526 – 534Combined sources9
Beta strandi544 – 546Combined sources3
Turni609 – 611Combined sources3
Turni614 – 619Combined sources6
Helixi620 – 626Combined sources7
Helixi627 – 629Combined sources3
Beta strandi636 – 638Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y8QX-ray2.25B/D1-640[»]
1Y8RX-ray2.75B/E1-640[»]
2PX9NMR-A166-382[»]
3KYCX-ray2.45B1-640[»]
3KYDX-ray2.61B1-549[»]
4W5VX-ray2.50B445-561[»]
DisProtiDP00486.
ProteinModelPortaliQ9UBT2.
SMRiQ9UBT2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBT2.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

eggNOGiKOG2013. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00550000074924.
HOGENOMiHOG000216514.
HOVERGENiHBG060266.
InParanoidiQ9UBT2.
KOiK10685.
OMAiVQWDTLL.
OrthoDBiEOG091G07PV.
PhylomeDBiQ9UBT2.
TreeFamiTF300765.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR016040. NAD(P)-bd_dom.
IPR030661. SAE2/Uba2.
IPR000594. ThiF_NAD_FAD-bd.
IPR028077. UAE_UbL_dom.
IPR032426. UBA2_C.
IPR019572. UBA_E1_Cys.
IPR018074. UBQ-activ_enz_E1_CS.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
PF14732. UAE_UbL. 1 hit.
PF16195. UBA2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF039133. SUMO_E1B. 1 hit.
SUPFAMiSSF69572. SSF69572. 2 hits.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_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: Q9UBT2-1) [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
MALSRGLPRE LAEAVAGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD
60 70 80 90 100
TIDVSNLNRQ FLFQKKHVGR SKAQVAKESV LQFYPKANIV AYHDSIMNPD
110 120 130 140 150
YNVEFFRQFI LVMNALDNRA ARNHVNRMCL AADVPLIESG TAGYLGQVTT
160 170 180 190 200
IKKGVTECYE CHPKPTQRTF PGCTIRNTPS EPIHCIVWAK YLFNQLFGEE
210 220 230 240 250
DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST KEWAKSTGYD
260 270 280 290 300
PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEETNASDQQ
310 320 330 340 350
NEPQLGLKDQ QVLDVKSYAR LFSKSIETLR VHLAEKGDGA ELIWDKDDPS
360 370 380 390 400
AMDFVTSAAN LRMHIFSMNM KSRFDIKSMA GNIIPAIATT NAVIAGLIVL
410 420 430 440 450
EGLKILSGKI DQCRTIFLNK QPNPRKKLLV PCALDPPNPN CYVCASKPEV
460 470 480 490 500
TVRLNVHKVT VLTLQDKIVK EKFAMVAPDV QIEDGKGTIL ISSEEGETEA
510 520 530 540 550
NNHKKLSEFG IRNGSRLQAD DFLQDYTLLI NILHSEDLGK DVEFEVVGDA
560 570 580 590 600
PEKVGPKQAE DAAKSITNGS DDGAQPSTST AQEQDDVLIV DSDEEDSSNN
610 620 630 640
ADVSEEERSR KRKLDEKENL SAKRSRIEQK EELDDVIALD
Length:640
Mass (Da):71,224
Last modified:February 16, 2004 - v2
Checksum:iC12D15293BBF90EB
GO
Isoform 2 (identifier: Q9UBT2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: Missing.

Note: No experimental confirmation available.
Show »
Length:544
Mass (Da):60,839
Checksum:i24F5E43AB6FA2B05
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti229S → C in AAD12784 (PubMed:9920803).Curated1
Sequence conflicti229S → C in AAD23914 (PubMed:10217437).Curated1
Sequence conflicti341E → G in CAB66839 (PubMed:11230166).Curated1
Sequence conflicti456V → L in BAD92109 (Ref. 11) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017689307L → R.2 PublicationsCorresponds to variant rs1043062dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0561641 – 96Missing in isoform 2. 1 PublicationAdd BLAST96

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090384 mRNA. Translation: AAD12784.1.
AF079566 mRNA. Translation: AAD23914.1.
AF110957 mRNA. Translation: AAD24434.1.
U35832 mRNA. Translation: AAC99992.1.
AL136905 mRNA. Translation: CAB66839.1.
AK124730 mRNA. Translation: BAG54081.1.
BT009781 mRNA. Translation: AAP88783.1.
CR456756 mRNA. Translation: CAG33037.1.
AC008747 Genomic DNA. No translation available.
BC003153 mRNA. Translation: AAH03153.1.
AB208872 mRNA. Translation: BAD92109.1.
AB015337 mRNA. Translation: BAA34795.1.
CCDSiCCDS12439.1. [Q9UBT2-1]
PIRiT46936.
RefSeqiNP_005490.1. NM_005499.2. [Q9UBT2-1]
UniGeneiHs.631580.

Genome annotation databases

EnsembliENST00000246548; ENSP00000246548; ENSG00000126261. [Q9UBT2-1]
ENST00000439527; ENSP00000437484; ENSG00000126261. [Q9UBT2-2]
GeneIDi10054.
KEGGihsa:10054.
UCSCiuc002nvk.4. human. [Q9UBT2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090384 mRNA. Translation: AAD12784.1.
AF079566 mRNA. Translation: AAD23914.1.
AF110957 mRNA. Translation: AAD24434.1.
U35832 mRNA. Translation: AAC99992.1.
AL136905 mRNA. Translation: CAB66839.1.
AK124730 mRNA. Translation: BAG54081.1.
BT009781 mRNA. Translation: AAP88783.1.
CR456756 mRNA. Translation: CAG33037.1.
AC008747 Genomic DNA. No translation available.
BC003153 mRNA. Translation: AAH03153.1.
AB208872 mRNA. Translation: BAD92109.1.
AB015337 mRNA. Translation: BAA34795.1.
CCDSiCCDS12439.1. [Q9UBT2-1]
PIRiT46936.
RefSeqiNP_005490.1. NM_005499.2. [Q9UBT2-1]
UniGeneiHs.631580.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y8QX-ray2.25B/D1-640[»]
1Y8RX-ray2.75B/E1-640[»]
2PX9NMR-A166-382[»]
3KYCX-ray2.45B1-640[»]
3KYDX-ray2.61B1-549[»]
4W5VX-ray2.50B445-561[»]
DisProtiDP00486.
ProteinModelPortaliQ9UBT2.
SMRiQ9UBT2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115365. 80 interactors.
DIPiDIP-35136N.
IntActiQ9UBT2. 15 interactors.
MINTiMINT-1405216.
STRINGi9606.ENSP00000246548.

Chemistry databases

BindingDBiQ9UBT2.
ChEMBLiCHEMBL2095174.

PTM databases

iPTMnetiQ9UBT2.
PhosphoSitePlusiQ9UBT2.
SwissPalmiQ9UBT2.

Polymorphism and mutation databases

BioMutaiUBA2.
DMDMi42559898.

Proteomic databases

EPDiQ9UBT2.
PaxDbiQ9UBT2.
PeptideAtlasiQ9UBT2.
PRIDEiQ9UBT2.

Protocols and materials databases

DNASUi10054.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000246548; ENSP00000246548; ENSG00000126261. [Q9UBT2-1]
ENST00000439527; ENSP00000437484; ENSG00000126261. [Q9UBT2-2]
GeneIDi10054.
KEGGihsa:10054.
UCSCiuc002nvk.4. human. [Q9UBT2-1]

Organism-specific databases

CTDi10054.
DisGeNETi10054.
GeneCardsiUBA2.
HGNCiHGNC:30661. UBA2.
HPAiHPA041436.
MIMi613295. gene.
neXtProtiNX_Q9UBT2.
OpenTargetsiENSG00000126261.
PharmGKBiPA162407583.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2013. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00550000074924.
HOGENOMiHOG000216514.
HOVERGENiHBG060266.
InParanoidiQ9UBT2.
KOiK10685.
OMAiVQWDTLL.
OrthoDBiEOG091G07PV.
PhylomeDBiQ9UBT2.
TreeFamiTF300765.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-HSA-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-HSA-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

Miscellaneous databases

ChiTaRSiUBA2. human.
EvolutionaryTraceiQ9UBT2.
GeneWikiiUBA2.
GenomeRNAii10054.
PROiQ9UBT2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000126261.
CleanExiHS_UBA2.
ExpressionAtlasiQ9UBT2. baseline and differential.
GenevisibleiQ9UBT2. HS.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR016040. NAD(P)-bd_dom.
IPR030661. SAE2/Uba2.
IPR000594. ThiF_NAD_FAD-bd.
IPR028077. UAE_UbL_dom.
IPR032426. UBA2_C.
IPR019572. UBA_E1_Cys.
IPR018074. UBQ-activ_enz_E1_CS.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
PF14732. UAE_UbL. 1 hit.
PF16195. UBA2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF039133. SUMO_E1B. 1 hit.
SUPFAMiSSF69572. SSF69572. 2 hits.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSAE2_HUMAN
AccessioniPrimary (citable) accession number: Q9UBT2
Secondary accession number(s): B3KWB9
, O95605, Q59H87, Q6IBP6, Q9NTJ1, Q9UED2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: February 16, 2004
Last modified: November 30, 2016
This is version 155 of the entry and version 2 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 19
    Human chromosome 19: 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.