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Protein

Ubiquitin-protein ligase E3A

Gene

Ube3a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates. Several substrates have been identified including the RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B. Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins. Finally, UBE3A also promotes its own degradation in vivo (By similarity). Plays an important role in the regulation of the circadian clock: involved in the ubiquitination of the core clock component ARNTL/BMAL1, leading to its proteasomal degradation (PubMed:24728990).By similarity1 Publication

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei838 – 8381Glycyl thioester intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri42 – 8140C4-type; atypicalBy similarityAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • transcription coactivator activity Source: MGI
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  • androgen receptor signaling pathway Source: MGI
  • ovarian follicle development Source: MGI
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: MGI
  • positive regulation of protein ubiquitination Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • prostate gland growth Source: MGI
  • protein autoubiquitination Source: MGI
  • protein K48-linked ubiquitination Source: UniProtKB
  • protein ubiquitination Source: MGI
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  • sperm entry Source: MGI
  • ubiquitin-dependent protein catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Biological rhythms, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi6.3.2.19. 3474.
ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-protein ligase E3A (EC:6.3.2.-)
Alternative name(s):
Oncogenic protein-associated protein E6-AP
Gene namesi
Name:Ube3a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:105098. Ube3a.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

GO - Cellular componenti

  • cytosol Source: MGI
  • nucleus Source: MGI
  • proteasome complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 870870Ubiquitin-protein ligase E3APRO_0000194981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphoserineCombined sources
Modified residuei213 – 2131PhosphoserineCombined sources
Modified residuei654 – 6541Phosphotyrosine; by ABL1By similarity

Post-translational modificationi

Phosphorylation at Tyr-654 by ABL1 impairs E3 ligase activity.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO08759.
MaxQBiO08759.
PaxDbiO08759.
PRIDEiO08759.

PTM databases

iPTMnetiO08759.
PhosphoSiteiO08759.
SwissPalmiO08759.

Expressioni

Tissue specificityi

Widely expressed. Most abundant in brain, heart and thymus.2 Publications

Gene expression databases

BgeeiE9QKT1.
CleanExiMM_UBE3A.
ExpressionAtlasiO08759. baseline and differential.
GenevisibleiO08759. MM.

Interactioni

Subunit structurei

The active form is probably a homotrimer. Binds UBQLN1 and UBQLN2. Interacts with the 26S proteasome. Interacts with BPY2. Interacts with HIF1AN, MAPK6 AND NEURL4; interaction with MAPK6 may be mediated by NEURL4. Interacts with the proteasomal subunit PSMD4. Interacts with ARNTL/BMAL1.By similarity

Protein-protein interaction databases

IntActiO08759. 2 interactions.
MINTiMINT-4139156.
STRINGi10090.ENSMUSP00000103161.

Structurei

3D structure databases

ProteinModelPortaliO08759.
SMRiO08759. Positions 22-85, 515-864.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini542 – 870329HECTPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi389 – 3946Asp/Glu-rich (acidic)

Sequence similaritiesi

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri42 – 8140C4-type; atypicalBy similarityAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0941. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00830000128260.
HOGENOMiHOG000261634.
HOVERGENiHBG059326.
InParanoidiO08759.
KOiK10587.
OMAiVEEDMMI.
TreeFamiTF315189.

Family and domain databases

InterProiIPR032353. AZUL.
IPR000569. HECT_dom.
IPR017134. UBE3A.
[Graphical view]
PfamiPF16558. AZUL. 1 hit.
PF00632. HECT. 1 hit.
[Graphical view]
PIRSFiPIRSF037201. Ubiquitin-protein_ligase_E6-AP. 1 hit.
SMARTiSM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMiSSF56204. SSF56204. 1 hit.
PROSITEiPS50237. HECT. 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: O08759-1) [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
MATACKRSPG ESQSEDIEAS RMKRAAAKHL IERYYHQLTE GCGNEACTNE
60 70 80 90 100
FCASCPTFLR MDNNAAAIKA LELYKINAKL CDPHPSKKGA SSAYLENSKG
110 120 130 140 150
ASNNSEIKMN KKEGKDFKDV IYLTEEKVYE IYEFCRESED YSPLIRVIGR
160 170 180 190 200
IFSSAEALVL SFRKVKQHTK EELKSLQEKD EDKDEDEKEK AACSAAAMEE
210 220 230 240 250
DSEASSSRMG DSSQGDNNVQ KLGPDDVTVD IDAIRRVYSS LLANEKLETA
260 270 280 290 300
FLNALVYLSP NVECDLTYHN VYTRDPNYLN LFIIVMENSN LHSPEYLEMA
310 320 330 340 350
LPLFCKAMCK LPLEAQGKLI RLWSKYSADQ IRRMMETFQQ LITYKVISNE
360 370 380 390 400
FNSRNLVNDD DAIVAASKCL KMVYYANVVG GDVDTNHNEE DDEEPIPESS
410 420 430 440 450
ELTLQELLGD ERRNKKGPRV DPLETELGVK TLDCRKPLIS FEEFINEPLN
460 470 480 490 500
DVLEMDKDYT FFKVETENKF SFMTCPFILN AVTKNLGLYY DNRIRMYSER
510 520 530 540 550
RITVLYSLVQ GQQLNPYLRL KVRRDHIIDD ALVRLEMIAM ENPADLKKQL
560 570 580 590 600
YVEFEGEQGV DEGGVSKEFF QLVVEEIFNP DIGMFTYDEA TKLFWFNPSS
610 620 630 640 650
FETEGQFTLI GIVLGLAIYN NCILDVHFPM VVYRKLMGKK GTFRDLGDSH
660 670 680 690 700
PVLYQSLKDL LEYEGSVEDD MMITFQISQT DLFGNPMMYD LKENGDKIPI
710 720 730 740 750
TNENRKEFVN LYSDYILNKS VEKQFKAFRR GFHMVTNESP LKYLFRPEEI
760 770 780 790 800
ELLICGSRNL DFQALEETTE YDGGYTRESV VIREFWEIVH SFTDEQKRLF
810 820 830 840 850
LQFTTGTDRA PVGGLGKLKM IIAKNGPDTE RLPTSHTCFN VLLLPEYSSK
860 870
EKLKERLLKA ITYAKGFGML
Length:870
Mass (Da):99,819
Last modified:April 1, 2015 - v2
Checksum:iCC6BBDDD5AE9C164
GO
Isoform 2 (identifier: O08759-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Show »
Length:849
Mass (Da):97,584
Checksum:i840AD5E681DBB45E
GO
Isoform 3 (identifier: O08759-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     784-870: Missing.

Show »
Length:762
Mass (Da):87,700
Checksum:iBB189D5380C3F25B
GO

Sequence cautioni

The sequence AAB47756.1 differs from that shown. Reason: Frameshift at positions 561, 567, 607 and 612. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71R → S in AAB63361 (PubMed:9182527).Curated
Sequence conflicti171 – 1711E → D in AAB63361 (PubMed:9182527).Curated
Sequence conflicti285 – 2851V → L in AAB63361 (PubMed:9182527).Curated
Sequence conflicti327 – 3271S → T in AAB63361 (PubMed:9182527).Curated
Sequence conflicti368 – 3681K → N in AAB63361 (PubMed:9182527).Curated
Sequence conflicti444 – 4441F → S in AAB63361 (PubMed:9182527).Curated
Sequence conflicti470 – 4701F → G in AAB63361 (PubMed:9182527).Curated
Sequence conflicti519 – 5191R → T in AAB63361 (PubMed:9182527).Curated
Sequence conflicti581 – 5811D → N in AAB47756 (PubMed:9110176).Curated
Sequence conflicti613 – 6131Missing in AAB63361 (PubMed:9182527).Curated
Sequence conflicti710 – 7112NL → IS in AAB63361 (PubMed:9182527).Curated
Sequence conflicti802 – 8021Q → L in AAB63361 (PubMed:9182527).Curated
Sequence conflicti854 – 8552KE → NV in AAB63361 (PubMed:9182527).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121Missing in isoform 2 and isoform 3. VSP_057563Add
BLAST
Alternative sequencei784 – 87087Missing in isoform 3. VSP_057564Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96636 mRNA. Translation: AAB63361.1.
U82122 mRNA. Translation: AAB47756.1. Frameshift.
AK029133 mRNA. Translation: BAC26314.1.
AC167971 Genomic DNA. No translation available.
BC131658 mRNA. Translation: AAI31659.1.
BC131659 mRNA. Translation: AAI31660.1.
CCDSiCCDS39973.1. [O08759-1]
CCDS80733.1. [O08759-2]
CCDS80734.1. [O08759-3]
RefSeqiNP_035798.2. NM_011668.2. [O08759-1]
NP_766598.1. NM_173010.3. [O08759-3]
XP_006540862.1. XM_006540799.2. [O08759-1]
XP_011249149.1. XM_011250847.1. [O08759-2]
UniGeneiMm.9002.

Genome annotation databases

EnsembliENSMUST00000107537; ENSMUSP00000103161; ENSMUSG00000025326. [O08759-2]
ENSMUST00000200758; ENSMUSP00000143859; ENSMUSG00000025326. [O08759-1]
ENSMUST00000202945; ENSMUSP00000143962; ENSMUSG00000025326. [O08759-3]
GeneIDi22215.
KEGGimmu:22215.
UCSCiuc009heg.1. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96636 mRNA. Translation: AAB63361.1.
U82122 mRNA. Translation: AAB47756.1. Frameshift.
AK029133 mRNA. Translation: BAC26314.1.
AC167971 Genomic DNA. No translation available.
BC131658 mRNA. Translation: AAI31659.1.
BC131659 mRNA. Translation: AAI31660.1.
CCDSiCCDS39973.1. [O08759-1]
CCDS80733.1. [O08759-2]
CCDS80734.1. [O08759-3]
RefSeqiNP_035798.2. NM_011668.2. [O08759-1]
NP_766598.1. NM_173010.3. [O08759-3]
XP_006540862.1. XM_006540799.2. [O08759-1]
XP_011249149.1. XM_011250847.1. [O08759-2]
UniGeneiMm.9002.

3D structure databases

ProteinModelPortaliO08759.
SMRiO08759. Positions 22-85, 515-864.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08759. 2 interactions.
MINTiMINT-4139156.
STRINGi10090.ENSMUSP00000103161.

PTM databases

iPTMnetiO08759.
PhosphoSiteiO08759.
SwissPalmiO08759.

Proteomic databases

EPDiO08759.
MaxQBiO08759.
PaxDbiO08759.
PRIDEiO08759.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000107537; ENSMUSP00000103161; ENSMUSG00000025326. [O08759-2]
ENSMUST00000200758; ENSMUSP00000143859; ENSMUSG00000025326. [O08759-1]
ENSMUST00000202945; ENSMUSP00000143962; ENSMUSG00000025326. [O08759-3]
GeneIDi22215.
KEGGimmu:22215.
UCSCiuc009heg.1. mouse.

Organism-specific databases

CTDi7337.
MGIiMGI:105098. Ube3a.

Phylogenomic databases

eggNOGiKOG0941. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00830000128260.
HOGENOMiHOG000261634.
HOVERGENiHBG059326.
InParanoidiO08759.
KOiK10587.
OMAiVEEDMMI.
TreeFamiTF315189.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 3474.
ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiUbe3a. mouse.
NextBioi302217.
PROiO08759.
SOURCEiSearch...

Gene expression databases

BgeeiE9QKT1.
CleanExiMM_UBE3A.
ExpressionAtlasiO08759. baseline and differential.
GenevisibleiO08759. MM.

Family and domain databases

InterProiIPR032353. AZUL.
IPR000569. HECT_dom.
IPR017134. UBE3A.
[Graphical view]
PfamiPF16558. AZUL. 1 hit.
PF00632. HECT. 1 hit.
[Graphical view]
PIRSFiPIRSF037201. Ubiquitin-protein_ligase_E6-AP. 1 hit.
SMARTiSM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMiSSF56204. SSF56204. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases."
    Hatakeyama S., Jensen J.P., Weissman A.M.
    J. Biol. Chem. 272:15085-15092(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    Strain: C57BL/6 X CBA.
  2. "The E6-Ap ubiquitin-protein ligase (UBE3A) gene is localized within a narrowed Angelman syndrome critical region."
    Sutcliffe J.S., Jiang Y.-H., Galjaard R.-J., Matsuura T., Fang P., Kubota T., Christian S.L., Bressler J., Cattanach B., Ledbetter D.H., Beaudet A.L.
    Genome Res. 7:368-377(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Skin.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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 3).
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "The E3 ubiquitin ligase UBE3A is an integral component of the molecular circadian clock through regulating the BMAL1 transcription factor."
    Gossan N.C., Zhang F., Guo B., Jin D., Yoshitane H., Yao A., Glossop N., Zhang Y.Q., Fukada Y., Meng Q.J.
    Nucleic Acids Res. 42:5765-5775(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiUBE3A_MOUSE
AccessioniPrimary (citable) accession number: O08759
Secondary accession number(s): E9QKT1, P97482, Q8CE29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 1, 2015
Last modified: May 11, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.