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Protein

E3 ubiquitin-protein ligase TRIP12

Gene

Trip12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes (By similarity).By similarity

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 sitei1992 – 19921Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIP12 (EC:6.3.2.-)
Alternative name(s):
Thyroid receptor-interacting protein 12
Short name:
TR-interacting protein 12
Short name:
TRIP-12
Gene namesi
Name:Trip12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1309481. Trip12.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality in the middle stage of development. Embryos exhibit growth arrest, while ES cells are viable. ES cells show decreased proliferation, but maintain both the undifferentiated state and the ability to differentiate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 20252024E3 ubiquitin-protein ligase TRIP12PRO_0000419689Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei77 – 771PhosphoserineBy similarity
Modified residuei85 – 851PhosphoserineCombined sources
Modified residuei181 – 1811N6-acetyllysineCombined sources
Modified residuei310 – 3101PhosphoserineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources
Modified residuei975 – 9751PhosphoserineCombined sources
Modified residuei1024 – 10241PhosphoserineCombined sources
Modified residuei1030 – 10301PhosphoserineCombined sources
Modified residuei1049 – 10491PhosphoserineBy similarity
Modified residuei1063 – 10631PhosphoserineBy similarity
Modified residuei1350 – 13501PhosphoserineCombined sources
Modified residuei1355 – 13551PhosphoserineCombined sources
Modified residuei1362 – 13621PhosphoserineCombined sources
Modified residuei1409 – 14091PhosphoserineBy similarity
Modified residuei1410 – 14101PhosphothreonineBy similarity
Modified residuei1458 – 14581N6-acetyllysineCombined sources
Modified residuei1460 – 14601PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiG5E870.
MaxQBiG5E870.
PaxDbiG5E870.
PRIDEiG5E870.

PTM databases

iPTMnetiG5E870.

Expressioni

Gene expression databases

BgeeiG5E870.
ExpressionAtlasiG5E870. baseline and differential.
GenevisibleiG5E870. MM.

Interactioni

Subunit structurei

Interacts with MYC; leading to disrupt interaction with isoform p19ARF/ARF of CDKN2A. Interacts with TRADD; leading to disrupt interaction with isoform p19ARF/ARF of CDKN2A. Interacts with SMARCC1; leading to disrupt interaction with SMARCE1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200117. 3 interactions.
IntActiG5E870. 2 interactions.
MINTiMINT-4116730.
STRINGi10090.ENSMUSP00000027421.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini755 – 869115WWEPROSITE-ProRule annotationAdd
BLAST
Domaini1918 – 2025108HECTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1529 – 160375K-boxBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the UPL family. K-HECT subfamily.Curated
Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
Contains 1 WWE domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0168. Eukaryota.
KOG0170. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00530000063470.
HOGENOMiHOG000030410.
InParanoidiG5E870.
KOiK10590.
OMAiTHFDISH.
OrthoDBiEOG7H791G.
TreeFamiTF323674.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000569. HECT_dom.
IPR004170. WWE-dom.
IPR018123. WWE-dom_subgr.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
PF02825. WWE. 1 hit.
[Graphical view]
SMARTiSM00119. HECTc. 1 hit.
SM00678. WWE. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
PS50918. WWE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

G5E870-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNRPNNNPG GSLRRSQRNT AGAQPQDDSI GGRSCSSSSA VIVPQPEDPD
60 70 80 90 100
RANTSERQKT GQVPKKDNSR GVKRSASPDY NRTNSPSSAK KPRAFQHIES
110 120 130 140 150
FSETNKPHSK SKKRHLDQEQ QLKSAQLPST SKAHTRKSVA AGSSRNQKRK
160 170 180 190 200
RTESSCVKSG SGSESTGAEE RSAKPIKLAS KSATSAKAGC STITDSSSAA
210 220 230 240 250
STSSSSSAIA SASSTVPAGA RVKQGKDQNK ARRSRSASSP SPRRSSREKE
260 270 280 290 300
QSKTGGSSKF DWAARFSPKV SLPKTKLSLP GSSKSETSKP GPSGLQAKLA
310 320 330 340 350
SLRKSTKKRS ESPPAELPSL RRSTRQKTTG SCASTSRRGS GLGKRGAAEA
360 370 380 390 400
RRQEKMADPE SNQETVNSSA ARTDEAPQGA AASSSVAGAV GMTTSGESES
410 420 430 440 450
DDSEMGRLQA LLEARGLPPH LFGPLGPRMS QLFHRTIGSG ASSKAQQLLQ
460 470 480 490 500
GLQASDESQQ LQAVIEMCQL LVMGNEETLG GFPVKSVVPA LITLLQMEHN
510 520 530 540 550
FDIMNHACRA LTYMMEALPR SSAVVVDAIP VFLEKLQVIQ CIDVAEQALT
560 570 580 590 600
ALEMLSRRHS KAILQAGGLA DCLLYLEFFS INAQRNALAI AANCCQSITP
610 620 630 640 650
DEFHFVADSL PLLTQRLTHQ DKKSVESTCL CFARLVDNFQ HEENLLQQVA
660 670 680 690 700
SKDLLTNVQQ LLVVTPPILS SGMFIMVVRM FSLMCSNCPT LAVQLMKQNI
710 720 730 740 750
AETLHFLLCG ASNGSCQEQI DLVPRSPQEL YELTSLICEL MPCLPKEGIF
760 770 780 790 800
AVDTMLKKGN AQNTDGAIWQ WRDDRGLWHP YNRIDSRIIE AAHQVGEDEI
810 820 830 840 850
SLSTLGRVYT IDFNSMQQIN EDTGTARAIQ RKPNPLANSN TSGYSELKKD
860 870 880 890 900
DARAQLMKED PELAKSFIKT LFGVLYEVYS SSAGPAVRHK CLRAILRIIY
910 920 930 940 950
FADAELLKDV LKNHAVSSHI ASMLSSQDLK IVVGALQMAE ILMQKLPDIF
960 970 980 990 1000
SVYFRREGVM HQVKHLAESE SLLTSPPKAC TNGSGSLGST TPASSGTATA
1010 1020 1030 1040 1050
ATNASADLGS PSLQHSRDDS LDLSPQGRLS DVLKRKRLPK RGPRRPKYSP
1060 1070 1080 1090 1100
PRDDDKVDNQ AKSPTTTQSP KSSFLASLNP KTWGRLSAQS NSNNIEPART
1110 1120 1130 1140 1150
AGVSGLARAA SKDTISNNRE KIKGWIKEQA HKFVERYFSS ENMDGSNPAL
1160 1170 1180 1190 1200
NVLQRLCAAT EQLNLQVDGG AECLVEIRSI VSESDVSSFE IQHSGFVKQL
1210 1220 1230 1240 1250
LLYLTSKNEK DAVGREIRLK RFLHVFFSSP LPGEEPVGRV EPVGHAPLLA
1260 1270 1280 1290 1300
LVHKMNNCLS QMEQFPVKVH DFPSGNGAGG SFSLNRGSQA LKFFNTHQLK
1310 1320 1330 1340 1350
CQLQRHPDCA NVKQWKGGPV KIDPLALVQA IERYLVVRGY GRVREDDEDS
1360 1370 1380 1390 1400
DDDGSDEEID ESLAAQFLNS GNVRHRLQFY IGEHLLPYNM TVYQAVRQFS
1410 1420 1430 1440 1450
VQAEDEREST DDESNPLGRA GIWTKTHTIW YKPVREDEES TKDCVGGKRG
1460 1470 1480 1490 1500
RAQTAPTKTS PRNAKKHDEL WHDGVCPSVA NPLEVYLIPT PPENITFEDP
1510 1520 1530 1540 1550
SLDVILLLRV LHAISRYWYY LYDNAMCKEI IPTSEFINSK LTAKANRQLQ
1560 1570 1580 1590 1600
DPLVIMTGNI PTWLTELGKT CPFFFPFDTR QMLFYVTAFD RDRAMQRLLD
1610 1620 1630 1640 1650
TNPEINQSDS QDSRVAPRLD RKKRTVNREE LLKQAESVMQ DLGSSRAMLE
1660 1670 1680 1690 1700
IQYENEVGTG LGPTLEFYAL VSQELQRADL CLWRGEEVTL SNPKGSQEGT
1710 1720 1730 1740 1750
KYIQNLQGLF ALPFGRTAKP AHIAKVKMKF RFLGKLMAKA IMDFRLVDLP
1760 1770 1780 1790 1800
LGLPFYKWML RQETSLTSHD LFDIDPVVAR SVYHLEDIVR QKKRLEQDKS
1810 1820 1830 1840 1850
QTKESLQYAL ETLTMNGCSV EDLGLDFTLP GFPNIELKKG GKDIPVTIHN
1860 1870 1880 1890 1900
LEEYLRLVIF WALNEGVCRQ FDSFRDGFES VFPLCHLQYF YPEELDQLLC
1910 1920 1930 1940 1950
GSKADTWDAK TLMECCRPDH GYTHDSRAVK FLFEILSSFD NEQQRLFLQF
1960 1970 1980 1990 2000
VTGSPRLPVG GFRSLNPPLT IVRKTFESTE NPDDFLPSVM TCVNYLKLPD
2010 2020
YSSIDIMRDK LLIAAREGQQ SFHLS
Length:2,025
Mass (Da):224,128
Last modified:December 14, 2011 - v1
Checksum:i25A71E35838DF64C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC123882 Genomic DNA. No translation available.
CH466629 Genomic DNA. Translation: EDL02171.1.
CH466629 Genomic DNA. Translation: EDL02178.1.
CH466629 Genomic DNA. Translation: EDL02182.1.
AK034814 mRNA. Translation: BAC28839.1.
AK134397 mRNA. Translation: BAE22126.1.
AK158807 mRNA. Translation: BAE34675.1.
BC034113 mRNA. Translation: AAH34113.2.
CCDSiCCDS35633.1.
RefSeqiNP_598736.4. NM_133975.4.
UniGeneiMm.209265.

Genome annotation databases

EnsembliENSMUST00000027421; ENSMUSP00000027421; ENSMUSG00000026219.
ENSMUST00000186465; ENSMUSP00000140224; ENSMUSG00000026219.
GeneIDi14897.
KEGGimmu:14897.
UCSCiuc007bsy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC123882 Genomic DNA. No translation available.
CH466629 Genomic DNA. Translation: EDL02171.1.
CH466629 Genomic DNA. Translation: EDL02178.1.
CH466629 Genomic DNA. Translation: EDL02182.1.
AK034814 mRNA. Translation: BAC28839.1.
AK134397 mRNA. Translation: BAE22126.1.
AK158807 mRNA. Translation: BAE34675.1.
BC034113 mRNA. Translation: AAH34113.2.
CCDSiCCDS35633.1.
RefSeqiNP_598736.4. NM_133975.4.
UniGeneiMm.209265.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200117. 3 interactions.
IntActiG5E870. 2 interactions.
MINTiMINT-4116730.
STRINGi10090.ENSMUSP00000027421.

PTM databases

iPTMnetiG5E870.

Proteomic databases

EPDiG5E870.
MaxQBiG5E870.
PaxDbiG5E870.
PRIDEiG5E870.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027421; ENSMUSP00000027421; ENSMUSG00000026219.
ENSMUST00000186465; ENSMUSP00000140224; ENSMUSG00000026219.
GeneIDi14897.
KEGGimmu:14897.
UCSCiuc007bsy.1. mouse.

Organism-specific databases

CTDi9320.
MGIiMGI:1309481. Trip12.

Phylogenomic databases

eggNOGiKOG0168. Eukaryota.
KOG0170. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00530000063470.
HOGENOMiHOG000030410.
InParanoidiG5E870.
KOiK10590.
OMAiTHFDISH.
OrthoDBiEOG7H791G.
TreeFamiTF323674.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiTrip12. mouse.
NextBioi287187.
PROiG5E870.
SOURCEiSearch...

Gene expression databases

BgeeiG5E870.
ExpressionAtlasiG5E870. baseline and differential.
GenevisibleiG5E870. MM.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000569. HECT_dom.
IPR004170. WWE-dom.
IPR018123. WWE-dom_subgr.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
PF02825. WWE. 1 hit.
[Graphical view]
SMARTiSM00119. HECTc. 1 hit.
SM00678. WWE. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
PS50918. WWE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] OF 1-983 AND 1669-2025.
    Strain: C57BL/6J.
    Tissue: Embryo, Testis and Visual cortex.
  4. "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] OF 824-2025.
    Tissue: Eye.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-975, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-310; SER-312; SER-975; SER-1024; SER-1030; SER-1350; SER-1355; SER-1362 AND SER-1460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. Cited for: DISRUPTION PHENOTYPE.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-181 AND LYS-1458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTRIPC_MOUSE
AccessioniPrimary (citable) accession number: G5E870
Secondary accession number(s): Q3TY88
, Q3UYT5, Q8BM59, Q8K051
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: December 14, 2011
Last modified: May 11, 2016
This is version 43 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. 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.