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Protein

Histone-lysine N-methyltransferase SETD2

Gene

Setd2

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

Functioni

Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate. Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation. Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A. Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction. H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A. H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase. Required during angiogenesis.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

Enzyme regulationi

Specifically inhibited by sinefungin derivatives.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1599InhibitorBy similarity1
Binding sitei1650Inhibitor; alternateBy similarity1
Binding sitei1650S-adenosyl-L-methionine; alternatePROSITE-ProRule annotation1
Binding sitei1653Inhibitor; via amide nitrogen; alternateBy similarity1
Binding sitei1653S-adenosyl-L-methionine; via amide nitrogen; alternatePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: MGI
  • cell migration involved in vasculogenesis Source: MGI
  • coronary vasculature morphogenesis Source: MGI
  • embryonic cranial skeleton morphogenesis Source: MGI
  • embryonic organ development Source: MGI
  • embryonic placenta morphogenesis Source: MGI
  • forebrain development Source: MGI
  • histone H3-K36 dimethylation Source: MGI
  • histone H3-K36 methylation Source: MGI
  • histone H3-K36 trimethylation Source: UniProtKB
  • mesoderm morphogenesis Source: MGI
  • mismatch repair Source: UniProtKB
  • morphogenesis of a branching structure Source: MGI
  • neural tube closure Source: MGI
  • nucleosome organization Source: UniProtKB
  • peptidyl-lysine trimethylation Source: MGI
  • pericardium development Source: MGI
  • regulation of gene expression Source: MGI
  • regulation of mRNA export from nucleus Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • stem cell development Source: MGI
  • transcription elongation from RNA polymerase II promoter Source: UniProtKB
  • vasculogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-MMU-3214841. PKMTs methylate histone lysines.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SETD2 (EC:2.1.1.43)
Alternative name(s):
Lysine N-methyltransferase 3A
SET domain-containing protein 2
Gene namesi
Name:Setd2
Synonyms:Kiaa1732, Kmt3a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1918177. Setd2.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosome 1 Publication

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality at E10.5-E11.5. Embryos show severe vascular defects in embryo, yolk sac and placenta. Capillaries are abnormally dilated in embryos and yolk sacs and cannot be remodeled into large blood vessels or intricate networks. The embryonic vessels fail to invade the labyrinthine layer of placenta, which impair the embryonic-maternal vascular connection. Defects are not caused by the extraembryonic tissues. Impaired H3K36me3, but not H3K36me2 or H3K36me1.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004235531 – 2537Histone-lysine N-methyltransferase SETD2Add BLAST2537

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei132PhosphoserineCombined sources1
Modified residuei242PhosphoserineCombined sources1
Modified residuei322PhosphoserineCombined sources1
Modified residuei324PhosphoserineCombined sources1
Modified residuei345PhosphoserineBy similarity1
Modified residuei423PhosphoserineBy similarity1
Modified residuei532PhosphoserineBy similarity1
Modified residuei614PhosphoserineBy similarity1
Modified residuei624PhosphoserineCombined sources1
Modified residuei626PhosphothreonineBy similarity1
Modified residuei633PhosphoserineCombined sources1
Cross-linki637Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei697PhosphoserineCombined sources1
Modified residuei707PhosphoserineBy similarity1
Modified residuei743PhosphoserineBy similarity1
Modified residuei753PhosphoserineBy similarity1
Modified residuei1077PhosphoserineBy similarity1
Modified residuei1201PhosphoserineBy similarity1
Modified residuei1387PhosphoserineCombined sources1
Modified residuei1389PhosphoserineCombined sources1
Modified residuei1391PhosphoserineCombined sources1
Modified residuei1670PhosphoserineBy similarity1
Modified residuei1818PhosphoserineCombined sources1
Modified residuei1819PhosphoserineCombined sources1
Modified residuei1827PhosphothreonineCombined sources1
Modified residuei1846PhosphothreonineBy similarity1
Modified residuei1862PhosphoserineBy similarity1
Modified residuei1926PhosphoserineBy similarity1
Modified residuei1954PhosphoserineCombined sources1
Modified residuei1962PhosphoserineCombined sources1
Modified residuei1969PhosphoserineCombined sources1
Modified residuei2053PhosphoserineBy similarity1
Modified residuei2055PhosphoserineBy similarity1

Post-translational modificationi

May be automethylated.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiE9Q5F9.
PaxDbiE9Q5F9.
PeptideAtlasiE9Q5F9.
PRIDEiE9Q5F9.

PTM databases

iPTMnetiE9Q5F9.
PhosphoSitePlusiE9Q5F9.

Expressioni

Gene expression databases

BgeeiENSMUSG00000044791.
ExpressionAtlasiE9Q5F9. baseline and differential.
GenevisibleiE9Q5F9. MM.

Interactioni

Subunit structurei

Specifically interacts with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A): binds to CTD heptad repeats doubly phosphorylated on 'Ser-2' and 'Ser-5' of each heptad. Interacts with HTT and IWS1. Interacts with p53/TP53; leading to regulate p53/TP53 target genes. Component of a complex with HNRNPL (By similarity).By similarity

Protein-protein interaction databases

BioGridi231695. 8 interactors.
IntActiE9Q5F9. 8 interactors.
STRINGi10090.ENSMUSP00000116313.

Structurei

3D structure databases

ProteinModelPortaliE9Q5F9.
SMRiE9Q5F9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1468 – 1522AWSPROSITE-ProRule annotationAdd BLAST55
Domaini1524 – 1641SETPROSITE-ProRule annotationAdd BLAST118
Domaini1648 – 1664Post-SETPROSITE-ProRule annotationAdd BLAST17
Domaini2362 – 2395WWPROSITE-ProRule annotationAdd BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1534 – 1536Inhibitor bindingBy similarity3
Regioni1534 – 1536S-adenosyl-L-methionine bindingBy similarity3
Regioni1577 – 1579Inhibitor bindingBy similarity3
Regioni1577 – 1579S-adenosyl-L-methionine bindingBy similarity3
Regioni1602 – 1603Inhibitor bindingBy similarity2
Regioni1602 – 1603S-adenosyl-L-methionine bindingBy similarity2
Regioni2110 – 2339Low charge regionBy similarityAdd BLAST230
Regioni2430 – 2537Interaction with POLR2ABy similarityAdd BLAST108

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili2090 – 2119Sequence analysisAdd BLAST30

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi167 – 231Pro-richAdd BLAST65
Compositional biasi294 – 439Ser-richAdd BLAST146
Compositional biasi369 – 457Arg-richAdd BLAST89
Compositional biasi2233 – 2338Gln-richAdd BLAST106

Domaini

The low charge region mediates the transcriptional activation activity.By similarity

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.PROSITE-ProRule annotation
Contains 1 AWS domain.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation
Contains 1 WW domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4442. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000081757.
InParanoidiE9Q5F9.
KOiK11423.
OMAiFIGHDSH.
OrthoDBiEOG091G040P.
TreeFamiTF106477.

Family and domain databases

InterProiIPR006560. AWS_dom.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
IPR013257. SRI.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00856. SET. 1 hit.
PF08236. SRI. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00570. AWS. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS51215. AWS. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_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: E9Q5F9-1) [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
MKPLPSQQPP PKMGDFYDPE HPTPEEEENE AKIENVQKTG FIKGPVFKGV
60 70 80 90 100
ASSRFLPKGT KTKVNLEEQG RQKVSFSFSF TKKTLQNRFL TALSNEKQSD
110 120 130 140 150
SPNSPAPPLQ VDSNPKVKMD AGDTFPATEE SSPPKSRVEL GRIHFKKHLL
160 170 180 190 200
HVTSRPQLAA STTAASPLPP TTQLPAVLAE SMIDSPPSSP PPPPPPPQAS
210 220 230 240 250
SPSPPAQISE PVALPQPPAT ALMTSPPGPL PGDVAVRAQK ESPVKSGPEV
260 270 280 290 300
LEVDTKQDIV SNSLEEHTVQ TLKEQADHLL QKEDSHIGKE EEVSDGSKIS
310 320 330 340 350
LSSKKASSKK KSSQFEGTFL GSESDEDSVR TSSSQRSHDL KSSTSIDKER
360 370 380 390 400
DFKKSSAPSK SEDLGKSSRS KTERDDRYCS YSKLERDTRY VSSRCRSERD
410 420 430 440 450
RRRSRSRSRS DRASRTSLSY SRSERSHYYD SERRYHRSSP YRERTRYSRP
460 470 480 490 500
YTDNRARESS DSEDEYKKTY PRRTSAHSYR DLRTSSSYSK FDRDCKTETS
510 520 530 540 550
YLEMERRGKY TSKLERESKR TSEHETIKRC CSPPNELGFR RGSSYSKHDN
560 570 580 590 600
STSRYKSALS KSISKNDKFK NSFCCTELNE ENKQSHSFSL QTPCSKGSEL
610 620 630 640 650
RTINKISERE KTGSPTPSNQ LNDSPTFKKL DESPVLKPEF IGHDGRESIK
660 670 680 690 700
ELELSKVKND QLRNFCSIEL NVNGSPETEA DVATFCTSKT DAISMTSDDS
710 720 730 740 750
VTGSEVSPLI KACMLSSNGF QNVGRCRERD SDDTCRQHNT SKSPFREMEP
760 770 780 790 800
LLSPHHDKLM SLPVKTIDYP KTLIKEPVDK RHSCCKTKDS DIYCSPNENP
810 820 830 840 850
EAENAEPSAM TISSHSFVNV HLESKTVICD NREPTDRHSE NTCDEYKQSI
860 870 880 890 900
GSTSSASHNH FDGLYEPIGS SGISSLQSPP SGIRCEENTS PTLDAVESKK
910 920 930 940 950
GIDFLKYARK ETDVGSALPD SGKGFSWENR HNNVLSGQSL QEAQEEGNSI
960 970 980 990 1000
LHERRGRPEI PLDEEQRGHT HISDDSEVVF PYDLNLTMED SDGITYTLKC
1010 1020 1030 1040 1050
DSSGNAPEIV STVHEDYSGS SASSSDESDS EDTESDDSSI PRNRLQSVVV
1060 1070 1080 1090 1100
VPKNSTLPME ETSPCSSRSS QSYKHYSDRW EDGLETRRHA YEEEYESKGC
1110 1120 1130 1140 1150
SQTEKYFLHK GTERSAESCY SQFGRKADNH LPDIAHAQSD GVDSTSQTDS
1160 1170 1180 1190 1200
RSDHLGHLNP EDTLRAKTSR PQELPVYSDD FEDLPNKSRQ QMIFSNRPDS
1210 1220 1230 1240 1250
SRLGKTELSF SSSCDISRMD GLHSSEELRN LGWDFSQQER PTTTYQQPDS
1260 1270 1280 1290 1300
SYGTCGTHKY QQSTEHYGGT HNYWQGNGYW DPRSAGRPPG TGLAYDRIQG
1310 1320 1330 1340 1350
QVPDSLTDDR EEEEHWDQRS GSHFSSPSNK FFFHQKDKGS VQAPEISSNS
1360 1370 1380 1390 1400
IKDALVMNER KDFSKNFEKN DIKERGPPKK RRQELESDSE SDGELQARKK
1410 1420 1430 1440 1450
VRVEMEQGES SVPQHSELMG PSCAMDDFRD PQRWKEFAKL GKMPCYFDLI
1460 1470 1480 1490 1500
EENVYLTERK KNKSHRDIKR MQCECTPLSK DERAQGEVAC GEDCLNRLLM
1510 1520 1530 1540 1550
IECSSRCPNG DYCSNRRFQR KQHADVEVIL TEKKGWGLRA AKDLPSNTFV
1560 1570 1580 1590 1600
LEYCGEVLDH KEFKARVKEY ARNKNIHYYF MALKNDEIID ATQKGNCSRF
1610 1620 1630 1640 1650
MNHSCEPNCE TQKWTVNGQL RVGFFTTKLV PSGSELTFDY QFQRYGKEAQ
1660 1670 1680 1690 1700
KCFCGSANCR GYLGGENRVS IRAAGGKMKK ERSRKKDSVD GELEALMENG
1710 1720 1730 1740 1750
EGLSDKNQVL SLSRLMVRIE TLEQKLTCLK LIQNTHSQSC LKSFLERHGL
1760 1770 1780 1790 1800
SLLWIWMAEL GDGRESNQKL QEEIIKTLEH LPIPTKNMLE ESKVLPIIQR
1810 1820 1830 1840 1850
WSQTKTAVPQ LSEGDGYSSE NTSRAHTPLN TPDPSAKPST EMDTDTPKKL
1860 1870 1880 1890 1900
IFRRLKIISE NSMDSAVSDV TSELECKDGK EDLDQLETVT VEEDEELQSQ
1910 1920 1930 1940 1950
QLLPQQLCES KVESEATIEV SKLPTSEPEA DTETEPKDSN GTKLEETIAE
1960 1970 1980 1990 2000
ETPSQDEEEG VSDVESERSQ EPPDKTVDIS DLATKLLDSW KDLKEVYRIP
2010 2020 2030 2040 2050
KKSQTEKEST VAERGRDAAA FRDQTAPKTP NRSRERDPDK QSQNKEKRKR
2060 2070 2080 2090 2100
RGSLSPPSSA YERGTKRPDD RYDTPTSKKK VRIKDRNKLS TEERRKLFEQ
2110 2120 2130 2140 2150
EVAQREAQKQ QQQMQNLGMT SPLPFDSLGY NASHHPFAGY PPGYPMQAYV
2160 2170 2180 2190 2200
DPSNPNAGKV LLPTPSMDPV CSPAPYDHAQ PLVGHSTESL AAPPSVPVVP
2210 2220 2230 2240 2250
HVAASVEVSS SQYVAQNESV VHQDSNVPVM PVQAPGPVQG QNYNVWESNQ
2260 2270 2280 2290 2300
QSVSVQQQYS PAQSQTTIYY QGQTCSTVYS VTSPYSQTTP PIVQSYAQPS
2310 2320 2330 2340 2350
LQYIQGQQIF TAHPQGVVVQ PTAAVTSIVA PGQPQSLQPP EMVVTNNLLD
2360 2370 2380 2390 2400
LPPPSPPKPK TIVLPPNWKT ARDPEGKIYY YHVITRQTQW DPPTWESPGD
2410 2420 2430 2440 2450
DASLEHEAEM DLGTPTYDEN PMKTSKKPKT AEADTSSELA KKSKEVFRKE
2460 2470 2480 2490 2500
MSQFIVQCLN PYRKPDCKVG RITTTEDFKH LARKLTHGVM NKELKYCKNP
2510 2520 2530
EDLECNENVK HKTKEYIKKY MQKFGAVYKP KEDTELE
Length:2,537
Mass (Da):285,663
Last modified:April 5, 2011 - v1
Checksum:i4ED47D778291DA9D
GO
Isoform 2 (identifier: E9Q5F9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2011-2011: Missing.

Note: No experimental confirmation available.
Show »
Length:2,536
Mass (Da):285,564
Checksum:i990ECF2CD8D56008
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0479462011Missing in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC132103 Genomic DNA. No translation available.
BC031601 mRNA. Translation: AAH31601.1.
BC059049 mRNA. Translation: AAH59049.1.
AK173246 mRNA. Translation: BAD32524.1.
CCDSiCCDS40781.2. [E9Q5F9-1]
RefSeqiNP_001074809.2. NM_001081340.2. [E9Q5F9-1]
UniGeneiMm.288949.

Genome annotation databases

EnsembliENSMUST00000153838; ENSMUSP00000116313; ENSMUSG00000044791. [E9Q5F9-1]
GeneIDi235626.
KEGGimmu:235626.
UCSCiuc009rug.2. mouse. [E9Q5F9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC132103 Genomic DNA. No translation available.
BC031601 mRNA. Translation: AAH31601.1.
BC059049 mRNA. Translation: AAH59049.1.
AK173246 mRNA. Translation: BAD32524.1.
CCDSiCCDS40781.2. [E9Q5F9-1]
RefSeqiNP_001074809.2. NM_001081340.2. [E9Q5F9-1]
UniGeneiMm.288949.

3D structure databases

ProteinModelPortaliE9Q5F9.
SMRiE9Q5F9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231695. 8 interactors.
IntActiE9Q5F9. 8 interactors.
STRINGi10090.ENSMUSP00000116313.

PTM databases

iPTMnetiE9Q5F9.
PhosphoSitePlusiE9Q5F9.

Proteomic databases

MaxQBiE9Q5F9.
PaxDbiE9Q5F9.
PeptideAtlasiE9Q5F9.
PRIDEiE9Q5F9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000153838; ENSMUSP00000116313; ENSMUSG00000044791. [E9Q5F9-1]
GeneIDi235626.
KEGGimmu:235626.
UCSCiuc009rug.2. mouse. [E9Q5F9-1]

Organism-specific databases

CTDi29072.
MGIiMGI:1918177. Setd2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG4442. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000081757.
InParanoidiE9Q5F9.
KOiK11423.
OMAiFIGHDSH.
OrthoDBiEOG091G040P.
TreeFamiTF106477.

Enzyme and pathway databases

ReactomeiR-MMU-3214841. PKMTs methylate histone lysines.

Miscellaneous databases

ChiTaRSiSetd2. mouse.
PROiE9Q5F9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000044791.
ExpressionAtlasiE9Q5F9. baseline and differential.
GenevisibleiE9Q5F9. MM.

Family and domain databases

InterProiIPR006560. AWS_dom.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
IPR013257. SRI.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00856. SET. 1 hit.
PF08236. SRI. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00570. AWS. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS51215. AWS. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSETD2_MOUSE
AccessioniPrimary (citable) accession number: E9Q5F9
Secondary accession number(s): Q69ZC0, Q6PCY9, Q8K0F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 18, 2013
Last sequence update: April 5, 2011
Last modified: November 2, 2016
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.