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Protein

Ubiquitin-conjugating enzyme E2 W

Gene

UBE2W

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. Catalyzes monoubiquitination. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Transfers ubiquitin in complex with RING/U-box type E3s that do not have active site cysteine residues to form thioester bonds with ubiquitin, and preferentially ubiquitinates the N-terminus of substrates, such as ATXN3, STUB1 and SUMO2.5 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathway:iprotein 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 sitei91 – 911Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: GO_Central
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.3.2.B6. 2681.
2.3.2.B7. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ96B02.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 W (EC:6.3.2.19)
Alternative name(s):
N-terminus-conjugating E2
Ubiquitin carrier protein W
Ubiquitin-conjugating enzyme 16
Short name:
UBC-16
Ubiquitin-protein ligase W
Gene namesi
Name:UBE2W
Synonyms:UBC16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:25616. UBE2W.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: In the nucleus, colocalizes with FANCL.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi83 – 831H → N: Impaired substrate ubiquitination of both Tau and ATXN3. 1 Publication
Mutagenesisi91 – 911C → A: Loss of predominant nuclear localization. 1 Publication

Organism-specific databases

PharmGKBiPA142670657.

Polymorphism and mutation databases

DMDMi74751754.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 151151Ubiquitin-conjugating enzyme E2 WPRO_0000232689Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated in vitro in the presence of FANCL (By similarity). Autoubiquitinated at Met-1.By similarity1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ96B02.
PRIDEiQ96B02.

PTM databases

PhosphoSiteiQ96B02.

Expressioni

Tissue specificityi

Widely expressed, with highest expression in brain, liver, pancreas and heart.1 Publication

Gene expression databases

BgeeiQ96B02.
CleanExiHS_UBE2W.
ExpressionAtlasiQ96B02. baseline and differential.
GenevisibleiQ96B02. HS.

Organism-specific databases

HPAiHPA045161.

Interactioni

Subunit structurei

Homodimer. Interacts with FANCL. Interacts with STUB1/CHIP (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MARCH5Q9NX474EBI-716589,EBI-2341610
PSTPIP1O435864EBI-716589,EBI-1050964
RNF5Q999424EBI-716589,EBI-348482
ROPN1Q9HAT03EBI-716589,EBI-1378139
USHBP1Q8N6Y03EBI-716589,EBI-739895

Protein-protein interaction databases

BioGridi120572. 74 interactions.
IntActiQ96B02. 69 interactions.
MINTiMINT-1428082.
STRINGi9606.ENSP00000454445.

Structurei

Secondary structure

1
151
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1712Combined sources
Beta strandi23 – 286Combined sources
Beta strandi35 – 428Combined sources
Turni48 – 514Combined sources
Beta strandi53 – 608Combined sources
Turni62 – 665Combined sources
Beta strandi70 – 767Combined sources
Beta strandi88 – 903Combined sources
Helixi93 – 953Combined sources
Turni96 – 983Combined sources
Helixi105 – 11511Combined sources
Helixi128 – 1336Combined sources
Helixi134 – 1374Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A7LX-ray1.82A/B1-117[»]
2MT6NMR-A1-151[»]
ProteinModelPortaliQ96B02.
SMRiQ96B02. Positions 1-151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96B02.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233453.
HOVERGENiHBG063308.
InParanoidiQ96B02.
KOiK10688.
PhylomeDBiQ96B02.
TreeFamiTF314582.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. 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: Q96B02-1) [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
MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE
60 70 80 90 100
GEKFQLLFKF SSRYPFDSPQ VMFTGENIPV HPHVYSNGHI CLSILTEDWS
110 120 130 140 150
PALSVQSVCL SIISMLSSCK EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT

C
Length:151
Mass (Da):17,331
Last modified:December 1, 2001 - v1
Checksum:i276B585BBC4CEB71
GO
Isoform 2 (identifier: Q96B02-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     5-5: Q → QTTGRRVEVWFP

Show »
Length:162
Mass (Da):18,660
Checksum:iF41B440840AD0625
GO
Isoform 3 (identifier: Q96B02-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLSPRGVTRARQLLPLRLWPRRSWGDGSIM

Note: No experimental confirmation available.
Show »
Length:180
Mass (Da):20,689
Checksum:i3E0F0920D2F1AD9F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261N → S in BAB13883 (PubMed:14702039).Curated
Sequence conflicti45 – 451P → S in BAA91954 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLSPRGVTRARQLLPLRLWP RRSWGDGSIM in isoform 3. 1 PublicationVSP_042974
Alternative sequencei5 – 51Q → QTTGRRVEVWFP in isoform 2. 2 PublicationsVSP_017943

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY948289 mRNA. Translation: AAY24555.1.
AK001873 mRNA. Translation: BAA91954.1.
AK021735 mRNA. Translation: BAB13883.1.
AK024050 mRNA. Translation: BAB14800.1.
AK295792 mRNA. Translation: BAG58613.1.
CR457275 mRNA. Translation: CAG33556.1.
CH471068 Genomic DNA. Translation: EAW87009.1.
CH471068 Genomic DNA. Translation: EAW87011.1.
AC022826 Genomic DNA. No translation available.
BC016326 mRNA. Translation: AAH16326.1.
CCDSiCCDS47874.2. [Q96B02-3]
RefSeqiNP_001001481.2. NM_001001481.2.
NP_001257944.1. NM_001271015.1.
NP_060769.4. NM_018299.4. [Q96B02-3]
UniGeneiHs.128841.

Genome annotation databases

EnsembliENST00000517608; ENSP00000428813; ENSG00000104343. [Q96B02-3]
ENST00000602593; ENSP00000473561; ENSG00000104343.
GeneIDi55284.
KEGGihsa:55284.
UCSCiuc003xzt.3. human. [Q96B02-3]
uc003xzu.4. human. [Q96B02-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY948289 mRNA. Translation: AAY24555.1.
AK001873 mRNA. Translation: BAA91954.1.
AK021735 mRNA. Translation: BAB13883.1.
AK024050 mRNA. Translation: BAB14800.1.
AK295792 mRNA. Translation: BAG58613.1.
CR457275 mRNA. Translation: CAG33556.1.
CH471068 Genomic DNA. Translation: EAW87009.1.
CH471068 Genomic DNA. Translation: EAW87011.1.
AC022826 Genomic DNA. No translation available.
BC016326 mRNA. Translation: AAH16326.1.
CCDSiCCDS47874.2. [Q96B02-3]
RefSeqiNP_001001481.2. NM_001001481.2.
NP_001257944.1. NM_001271015.1.
NP_060769.4. NM_018299.4. [Q96B02-3]
UniGeneiHs.128841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A7LX-ray1.82A/B1-117[»]
2MT6NMR-A1-151[»]
ProteinModelPortaliQ96B02.
SMRiQ96B02. Positions 1-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120572. 74 interactions.
IntActiQ96B02. 69 interactions.
MINTiMINT-1428082.
STRINGi9606.ENSP00000454445.

PTM databases

PhosphoSiteiQ96B02.

Polymorphism and mutation databases

DMDMi74751754.

Proteomic databases

MaxQBiQ96B02.
PRIDEiQ96B02.

Protocols and materials databases

DNASUi55284.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000517608; ENSP00000428813; ENSG00000104343. [Q96B02-3]
ENST00000602593; ENSP00000473561; ENSG00000104343.
GeneIDi55284.
KEGGihsa:55284.
UCSCiuc003xzt.3. human. [Q96B02-3]
uc003xzu.4. human. [Q96B02-2]

Organism-specific databases

CTDi55284.
GeneCardsiGC08M074692.
HGNCiHGNC:25616. UBE2W.
HPAiHPA045161.
MIMi614277. gene.
neXtProtiNX_Q96B02.
PharmGKBiPA142670657.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233453.
HOVERGENiHBG063308.
InParanoidiQ96B02.
KOiK10688.
PhylomeDBiQ96B02.
TreeFamiTF314582.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B6. 2681.
2.3.2.B7. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ96B02.

Miscellaneous databases

ChiTaRSiUBE2W. human.
EvolutionaryTraceiQ96B02.
GenomeRNAii55284.
NextBioi59442.
PROiQ96B02.
SOURCEiSearch...

Gene expression databases

BgeeiQ96B02.
CleanExiHS_UBE2W.
ExpressionAtlasiQ96B02. baseline and differential.
GenevisibleiQ96B02. HS.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, characterization and subcellular localization of a gene encoding a human Ubiquitin-conjugating enzyme (E2) homologous to the Arabidopsis thaliana UBC-16 gene product."
    Yin G., Ji C., Wu T., Shen Z., Xu X., Xie Y., Mao Y.
    Front. Biosci. 11:1500-1507(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-91.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Embryo, Hippocampus and Placenta.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Urinary bladder.
  7. "Mechanistic insight into site-restricted monoubiquitination of FANCD2 by Ube2t, FANCL, and FANCI."
    Alpi A.F., Pace P.E., Babu M.M., Patel K.J.
    Mol. Cell 32:767-777(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FANCL.
  8. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
    David Y., Ziv T., Admon A., Navon A.
    J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi anemia protein FANCD2."
    Zhang Y., Zhou X., Zhao L., Li C., Zhu H., Xu L., Shan L., Liao X., Guo Z., Huang P.
    Mol. Cells 31:113-122(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini."
    Tatham M.H., Plechanovova A., Jaffray E.G., Salmen H., Hay R.T.
    Biochem. J. 453:137-145(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION AT MET-1, SUBSTRATE SPECIFICITY.
  11. "The ubiquitin-conjugating enzyme (E2) Ube2w ubiquitinates the N terminus of substrates."
    Scaglione K.M., Basrur V., Ashraf N.S., Konen J.R., Elenitoba-Johnson K.S., Todi S.V., Paulson H.L.
    J. Biol. Chem. 288:18784-18788(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY, MUTAGENESIS OF HIS-83.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 1-117, SUBUNIT.

Entry informationi

Entry nameiUBE2W_HUMAN
AccessioniPrimary (citable) accession number: Q96B02
Secondary accession number(s): B4DIV1
, Q1XBE0, Q9H823, Q9HAG6, Q9NV07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: December 1, 2001
Last modified: July 22, 2015
This is version 131 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 8
    Human chromosome 8: 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

External Data

Dasty 3

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 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.