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Protein

E3 ubiquitin-protein ligase UBR1

Gene

Ubr1

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 is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (By similarity).By similarity3 Publications

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri97 – 16872UBR-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1101 – 1204104RING-type; atypicalAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase UBR1 (EC:6.3.2.-)
Alternative name(s):
N-recognin-1
Ubiquitin-protein ligase E3-alpha-1
Ubiquitin-protein ligase E3-alpha-I
Gene namesi
Name:Ubr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1277977. Ubr1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB-SubCell
  • proteasome complex Source: MGI
  • ubiquitin ligase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile, but show a decreased mass of skeletal muscle and adipose tissue. They have exocrine pancreatic insufficiency with impaired stimulus-secretion coupling and increased susceptibiliy to pancreatic injury. UBR1 and UBR2 double knockout embryos die at midgestation, with defects in neurogenesis and cardiovascular development. These defects included reduced proliferation as well as precocious migration and differentiation of neural progenitor cells.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 17571756E3 ubiquitin-protein ligase UBR1PRO_0000056137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei1182 – 11821PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO70481.
MaxQBiO70481.
PaxDbiO70481.
PRIDEiO70481.

PTM databases

iPTMnetiO70481.
PhosphoSiteiO70481.

Expressioni

Tissue specificityi

Present in skeletal muscle and liver (at protein level). Broadly expressed, with highest levels in skeletal muscle and heart. Expressed in acinar cells of the pancreas. In testes, expressed primarily in spermatogonia.5 Publications

Developmental stagei

Expressed in limb buds at E9.5-E11.5.1 Publication

Inductioni

In models of cancer cachexia, induced in muscle during the progression of wasting.1 Publication

Gene expression databases

BgeeiO70481.
GenevisibleiO70481. MM.

Interactioni

Subunit structurei

Interacts with RECQL4.By similarity

Protein-protein interaction databases

BioGridi204422. 3 interactions.
IntActiO70481. 2 interactions.
MINTiMINT-1580129.
STRINGi10090.ENSMUSP00000028728.

Structurei

3D structure databases

ProteinModelPortaliO70481.
SMRiO70481. Positions 97-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi864 – 8696Poly-Pro

Domaini

The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif.
The UBR-type zinc finger forms a pocket that mediates recognition of type 1 N-degrons. It exhibits preference for Arginine in first position, has poor affinity for histidine, and doesn't bind acetylated peptides (By similarity).By similarity

Sequence similaritiesi

Belongs to the UBR1 family.Curated
Contains 1 RING-type zinc finger.Curated
Contains 1 UBR-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri97 – 16872UBR-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1101 – 1204104RING-type; atypicalAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1140. Eukaryota.
ENOG410XPQU. LUCA.
GeneTreeiENSGT00530000063055.
HOGENOMiHOG000231769.
HOVERGENiHBG080426.
InParanoidiO70481.
KOiK10625.
OMAiHESTILR.
OrthoDBiEOG7RNJZB.
TreeFamiTF323875.

Family and domain databases

Gene3Di3.30.1390.10. 1 hit.
InterProiIPR003769. ClpS_core.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR011991. WHTH_DNA-bd_dom.
IPR003126. Znf_UBR.
[Graphical view]
PfamiPF02617. ClpS. 1 hit.
PF02207. zf-UBR. 1 hit.
[Graphical view]
SMARTiSM00396. ZnF_UBR1. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF54736. SSF54736. 1 hit.
PROSITEiPS51157. ZF_UBR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O70481-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEEMDGAE RMDVSPEPPL APQRPASWWD QQVDFYTAFL HHLAQLVPEI
60 70 80 90 100
YFAEMDPDLE KQEESVQMSI LTPLEWYLFG EDPDICLEKL KHSGAFQLCG
110 120 130 140 150
KVFKSGETTY SCRDCAIDPT CVLCMDCFQS SVHKNHRYKM HTSTGGGFCD
160 170 180 190 200
CGDTEAWKTG PFCVDHEPGR AGTTKESLHC PLNEEVIAQA RRIFPSVIKY
210 220 230 240 250
IVEMTIWEEE KELPPELQIR EKNERYYCVL FNDEHHSYDH VIYSLQRALD
260 270 280 290 300
CELAEAQLHT TAIDKEGRRA VKAGVYATCQ EAKEDIKSHS ENVSQHPLHV
310 320 330 340 350
EVLHSVVMAH QKFALRLGSW MNKIMSYSSD FRQIFCQACL VEEPGSENPC
360 370 380 390 400
LISRLMLWDA KLYKGARKIL HELIFSSFFM EMEYKKLFAM EFVKYYKQLQ
410 420 430 440 450
KEYISDDHER SISITALSVQ MLTVPTLARH LIEEQNVISV ITETLLEVLP
460 470 480 490 500
EYLDRNNKFN FQGYSQDKLG RVYAVICDLK YILISKPVIW TERLRAQFLE
510 520 530 540 550
GFRSFLKILT CMQGMEEIRR QVGQHIEVDP DWEAAIAIQM QLKNILLMFQ
560 570 580 590 600
EWCACDEDLL LVAYKECHKA VMRCSTNFMS STKTVVQLCG HSLETKSYKV
610 620 630 640 650
SEDLVSIHLP LSRTLAGLHV RLSRLGAISR LHEFVPFDGF QVEVLVEYPL
660 670 680 690 700
RCLVLVAQVV AEMWRRNGLS LISQVFYYQD VKCREEMYDK DIIMLQIGAS
710 720 730 740 750
IMDPNKFLLL VLQRYELTDA FNKTISTKDQ DLIKQYNTLI EEMLQVLIYI
760 770 780 790 800
VGERYVPGVG NVTREEVIMR EITHLLCIEP MPHSAIARNL PENENNETGL
810 820 830 840 850
ENVINKVATF KKPGVSGHGV YELKDESLKD FNMYFYHYSK TQHSKAEHMQ
860 870 880 890 900
KKRRKQENKD EALPPPPPPE FCPAFSKVVN LLSCDVMMYI LRTIFERAVD
910 920 930 940 950
MESNLWTEGM LQMAFHILAL GLLEEKQQLQ KAPEEEVAFD FYHKASRLGS
960 970 980 990 1000
SAMNAQNIQM LLEKLKGIPQ LESQKDMITW ILQMFDTVKR LREKSCLVVA
1010 1020 1030 1040 1050
TTSGLECVKS EEITHDKEKA ERKRKAEAAR LHRQKIMAQM SALQKNFIET
1060 1070 1080 1090 1100
HKLMYDNTSE VTGKEDSIME EESTSAVSEA SRIALGPKRG PAVTEKEVLT
1110 1120 1130 1140 1150
CILCQEEQEV KLENNAMVLS ACVQKSTALT QHRGKPVDHL GETLDPLFMD
1160 1170 1180 1190 1200
PDLAHGTYTG SCGHVMHAVC WQKYFEAVQL SSQQRIHVDL FDLESGEYLC
1210 1220 1230 1240 1250
PLCKSLCNTV IPIIPLQPQK INSENAEALA QLLTLARWIQ TVLARISGYN
1260 1270 1280 1290 1300
IKHAKGEAPA VPVLFNQGMG DSTFEFHSIL SFGVQSSVKY SNSIKEMVIL
1310 1320 1330 1340 1350
FATTIYRIGL KVPPDELDPR VPMMTWSTCA FTIQAIENLL GDEGKPLFGA
1360 1370 1380 1390 1400
LQNRQHNGLK ALMQFAVAQR TTCPQVLIHK HLARLLSVIL PNLQSENTPG
1410 1420 1430 1440 1450
LLSVDLFHVL VGAVLAFPSL YWDDTVDLQP SPLSSSYNHL YLFHLITMAH
1460 1470 1480 1490 1500
MLQILLTTDT DLSSGPPLAE GEEDSEEARC ASAFFVEVSQ HTDGLAGCGA
1510 1520 1530 1540 1550
PGWYLWLSLR NGITPYLRCA ALLFHYLLGV APPEELFANS AEGEFSALCS
1560 1570 1580 1590 1600
YLSLPTNLFL LFQEYWDTIR PLLQRWCGDP ALLKSLKQKS AVVRYPRKRN
1610 1620 1630 1640 1650
SLIELPEDYS CLLNQASHFR CPRSADDERK HPVLCLFCGA ILCSQNICCQ
1660 1670 1680 1690 1700
EIVNGEEVGA CVFHALHCGA GVCIFLKIRE CRVVLVEGKA RGCAYPAPYL
1710 1720 1730 1740 1750
DEYGETDPGL KRGNPLHLSR ERYRKLHLVW QQHCIIEEIA RSQETNQMLF

GFNWQLL
Length:1,757
Mass (Da):200,240
Last modified:July 27, 2011 - v2
Checksum:i935C0531A5F25A66
GO

Sequence cautioni

The sequence AAH90969.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti639 – 6391G → S in AAC40165 (PubMed:9653112).Curated
Sequence conflicti639 – 6391G → S in BAC40933 (PubMed:16141072).Curated
Sequence conflicti888 – 8881M → I in AAC40165 (PubMed:9653112).Curated
Sequence conflicti901 – 9011M → T in AAC40165 (PubMed:9653112).Curated
Sequence conflicti964 – 9641K → R in AAC40165 (PubMed:9653112).Curated
Sequence conflicti973 – 9731S → G in AAC40165 (PubMed:9653112).Curated
Sequence conflicti1008 – 10081V → I in AAC40165 (PubMed:9653112).Curated
Sequence conflicti1357 – 13571N → S in AAC40165 (PubMed:9653112).Curated
Sequence conflicti1371 – 13711T → A in AAC40165 (PubMed:9653112).Curated
Sequence conflicti1464 – 14641S → P in AAC40165 (PubMed:9653112).Curated
Sequence conflicti1496 – 14961A → T in AAC40165 (PubMed:9653112).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061555 mRNA. Translation: AAC40165.1.
AH006182 Genomic DNA. Translation: AAC23678.1.
AL844548, AL935168 Genomic DNA. Translation: CAM19009.1.
AL935168, AL844548 Genomic DNA. Translation: CAM21400.1.
AK078173 mRNA. Translation: BAC37160.1.
AK089616 mRNA. Translation: BAC40933.1.
BC090969 mRNA. Translation: AAH90969.1. Sequence problems.
CCDSiCCDS16628.1.
PIRiT14318.
RefSeqiNP_033487.2. NM_009461.2.
UniGeneiMm.389330.

Genome annotation databases

EnsembliENSMUST00000028728; ENSMUSP00000028728; ENSMUSG00000027272.
GeneIDi22222.
KEGGimmu:22222.
UCSCiuc008lxb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061555 mRNA. Translation: AAC40165.1.
AH006182 Genomic DNA. Translation: AAC23678.1.
AL844548, AL935168 Genomic DNA. Translation: CAM19009.1.
AL935168, AL844548 Genomic DNA. Translation: CAM21400.1.
AK078173 mRNA. Translation: BAC37160.1.
AK089616 mRNA. Translation: BAC40933.1.
BC090969 mRNA. Translation: AAH90969.1. Sequence problems.
CCDSiCCDS16628.1.
PIRiT14318.
RefSeqiNP_033487.2. NM_009461.2.
UniGeneiMm.389330.

3D structure databases

ProteinModelPortaliO70481.
SMRiO70481. Positions 97-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204422. 3 interactions.
IntActiO70481. 2 interactions.
MINTiMINT-1580129.
STRINGi10090.ENSMUSP00000028728.

PTM databases

iPTMnetiO70481.
PhosphoSiteiO70481.

Proteomic databases

EPDiO70481.
MaxQBiO70481.
PaxDbiO70481.
PRIDEiO70481.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028728; ENSMUSP00000028728; ENSMUSG00000027272.
GeneIDi22222.
KEGGimmu:22222.
UCSCiuc008lxb.1. mouse.

Organism-specific databases

CTDi197131.
MGIiMGI:1277977. Ubr1.

Phylogenomic databases

eggNOGiKOG1140. Eukaryota.
ENOG410XPQU. LUCA.
GeneTreeiENSGT00530000063055.
HOGENOMiHOG000231769.
HOVERGENiHBG080426.
InParanoidiO70481.
KOiK10625.
OMAiHESTILR.
OrthoDBiEOG7RNJZB.
TreeFamiTF323875.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi302239.
PROiO70481.
SOURCEiSearch...

Gene expression databases

BgeeiO70481.
GenevisibleiO70481. MM.

Family and domain databases

Gene3Di3.30.1390.10. 1 hit.
InterProiIPR003769. ClpS_core.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR011991. WHTH_DNA-bd_dom.
IPR003126. Znf_UBR.
[Graphical view]
PfamiPF02617. ClpS. 1 hit.
PF02207. zf-UBR. 1 hit.
[Graphical view]
SMARTiSM00396. ZnF_UBR1. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF54736. SSF54736. 1 hit.
PROSITEiPS51157. ZF_UBR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: 129/SvJ.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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 1-849 AND 1529-1757.
    Strain: NOD.
    Tissue: Olfactory bulb and Spleen.
  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 1-852.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Construction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3alpha) of the N-end rule pathway."
    Kwon Y.T., Xia Z., Davydov I.V., Lecker S.H., Varshavsky A.
    Mol. Cell. Biol. 21:8007-8021(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, FUNCTION.
  6. "Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway."
    Kwon Y.T., Xia Z., An J.Y., Tasaki T., Davydov I.V., Seo J.W., Sheng J., Xie Y., Varshavsky A.
    Mol. Cell. Biol. 23:8255-8271(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, FUNCTION.
  7. "Regulation of protein catabolism by muscle-specific and cytokine-inducible ubiquitin ligase E3alpha-II during cancer cachexia."
    Kwak K.S., Zhou X., Solomon V., Baracos V.E., Davis J., Bannon A.W., Boyle W.J., Lacey D.L., Han H.Q.
    Cancer Res. 64:8193-8198(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  8. Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  9. "Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway."
    An J.Y., Seo J.W., Tasaki T., Lee M.J., Varshavsky A., Kwon Y.T.
    Proc. Natl. Acad. Sci. U.S.A. 103:6212-6217(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiUBR1_MOUSE
AccessioniPrimary (citable) accession number: O70481
Secondary accession number(s): A2AQ54
, Q5BKR8, Q792M3, Q8BN40, Q8C5K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 122 of the entry and version 2 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.