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B2RU80 (PTPRB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase beta
Short name=Protein-tyrosine phosphatase beta
Short name=R-PTP-beta
EC=3.1.3.48
Alternative name(s):
Vascular endothelial protein tyrosine phosphatase
Short name=VE-PTP
Gene names
Name:Ptprb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1998 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Monomer By similarity. Interacts with TEK. Interacts via fibronectin type-III 17 domain with CDH5. Ref.1 Ref.6 Ref.9 Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Expression is very high in the vasculature of lung, spleen, and kidney, as well as in the heart valves, and is also present in the endothelium of arterioles and venules. Also expressed in tumor vasculature. Ref.6 Ref.7 Ref.8

Developmental stage

Expressed in both arterial and venous vascular endothelium in embryos, although more strongly in arterial vessels. Highly expressed in the developing outflow tract of the heart and later is expressed in developing heart valves. Ref.6 Ref.7 Ref.8

Disruption phenotype

Mice show severe cardiovascular defects and embryonic lethality by E10. Vasculogenesis occurs normally however, angiogenesis is abnormal. Angiogenic defects are most pronounced in the yolk sac and include a complete failure to elaborate the primitive vascular scaffold into higher-order branched arteries, veins, and capillaries. Ref.8

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 3 subfamily.

Contains 17 fibronectin type-III domains.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Biological processAngiogenesis
   Cellular componentMembrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from direct assay Ref.10. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from electronic annotation. Source: GOC

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 19981976Receptor-type tyrosine-protein phosphatase beta
PRO_0000390401

Regions

Topological domain23 – 16221600Extracellular Potential
Transmembrane1623 – 164321Helical; Potential
Topological domain1644 – 1997354Cytoplasmic Potential
Domain23 – 10987Fibronectin type-III 1
Domain111 – 20292Fibronectin type-III 2
Domain204 – 28986Fibronectin type-III 3
Domain290 – 37687Fibronectin type-III 4
Domain378 – 46689Fibronectin type-III 5
Domain468 – 55386Fibronectin type-III 6
Domain555 – 64288Fibronectin type-III 7
Domain644 – 73188Fibronectin type-III 8
Domain732 – 81887Fibronectin type-III 9
Domain820 – 90788Fibronectin type-III 10
Domain908 – 99487Fibronectin type-III 11
Domain996 – 108489Fibronectin type-III 12
Domain1086 – 117388Fibronectin type-III 13
Domain1174 – 126188Fibronectin type-III 14
Domain1262 – 135493Fibronectin type-III 15
Domain1356 – 144489Fibronectin type-III 16
Domain1449 – 1551103Fibronectin type-III 17
Domain1704 – 1964261Tyrosine-protein phosphatase
Region1905 – 19117Substrate binding By similarity

Sites

Active site19051Phosphocysteine intermediate By similarity
Binding site18711Substrate By similarity
Binding site19491Substrate By similarity

Amino acid modifications

Glycosylation281N-linked (GlcNAc...) Potential
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation1991N-linked (GlcNAc...) Potential
Glycosylation2681N-linked (GlcNAc...) Potential
Glycosylation4151N-linked (GlcNAc...) Potential
Glycosylation4221N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential
Glycosylation5751N-linked (GlcNAc...) Potential
Glycosylation5991N-linked (GlcNAc...) Potential
Glycosylation6531N-linked (GlcNAc...) Potential
Glycosylation8301N-linked (GlcNAc...) Potential
Glycosylation10411N-linked (GlcNAc...) Potential
Glycosylation10971N-linked (GlcNAc...) Potential
Glycosylation11641N-linked (GlcNAc...) Potential
Glycosylation11861N-linked (GlcNAc...) Potential
Glycosylation12131N-linked (GlcNAc...) Potential
Glycosylation12751N-linked (GlcNAc...) Potential
Glycosylation13681N-linked (GlcNAc...) Potential
Glycosylation14711N-linked (GlcNAc...) Potential
Glycosylation14751N-linked (GlcNAc...) Potential
Glycosylation15191N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis19111R → A: Loss of activity and dephosphorylation of CDH5. Ref.1
Sequence conflict6471V → A in BAE28060. Ref.3
Sequence conflict6471V → A in BAE27912. Ref.3
Sequence conflict9061T → P in AAL75813. Ref.1
Sequence conflict10371L → F in BAE28060. Ref.3
Sequence conflict10371L → F in BAE27912. Ref.3
Sequence conflict11681I → V in BAE28060. Ref.3
Sequence conflict11681I → V in BAE27912. Ref.3
Sequence conflict17481C → S in AAL75813. Ref.1

Sequences

Sequence LengthMass (Da)Tools
B2RU80 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 066EE7141F942887

FASTA1,998224,495
        10         20         30         40         50         60 
MLRHGALTAL WITLSVVQTG VAEQVKCNFT LLESRVSSLS ASIQWRTFAS PCNFSLIYSS 

        70         80         90        100        110        120 
DTSGPMWCHP IRIDNFTYGC NPKDLQAGTV YNFRIVSLDG EESTLVLQTD PLPPARFEVN 

       130        140        150        160        170        180 
REKTASTTLQ VRWTPSSGKV SWYEVQLFDH NNQKIQEVQV QESTTWSQYT FLNLTEGNSY 

       190        200        210        220        230        240 
KVAITAVSGE KRSFPVYING STVPSPVKDL GISPNPNSLL ISWSRGSGNV EQYRLVLMDK 

       250        260        270        280        290        300 
GAIVQDTNVD RRDTSYAFHE LTPGHLYNLT IVTMASGLQN SRWKLVRTAP MEVSNLKVTN 

       310        320        330        340        350        360 
DGRLTSLNVK WQKPPGDVDS YSITLSHQGT IKESKTLAPP VTETQFKDLV PGRLYQVTIS 

       370        380        390        400        410        420 
CISGELSAEK SAAGRTVPEK VRNLVSYNEI WMKSFTVNWT PPAGDWEHYR IVLFNESLVL 

       430        440        450        460        470        480 
LNTTVGKEET HYALDGLELI PGRQYEIEVI VESGNLRNSE RCQGRTVPLA VLQLRVKHAN 

       490        500        510        520        530        540 
ETSLGITWRA PLGEWEKYII SLMDRELLVI HKSLSKDAKE FTFTDLMPGR NYKATVTSMS 

       550        560        570        580        590        600 
GDLKQSSSIK GRTVPAQVTD LHVNNQGMTS SLFTNWTKAL GDVEFYQVLL IHENVVVKNE 

       610        620        630        640        650        660 
SVSSDTSRYS FRALKPGSLY SVVVTTVSGG ISSRQVVAEG RTVPSSVSGV TVNNSGRNDY 

       670        680        690        700        710        720 
LSVSWLPAPG EVDHYVVSLS HEGKVDQFLI IAKSVSECSF SSLTPGRLYN VTVTTKSGNY 

       730        740        750        760        770        780 
ASHSFTEERT VPDKVQGISV SNSARSDYLK VSWVHATGDF DHYEVTIKNR ESFIQTKTIP 

       790        800        810        820        830        840 
KSENECEFIE LVPGRLYSVT VSTKSGQYEA SEQGTGRTIP EPVKDLTLLN RSTEDLHVTW 

       850        860        870        880        890        900 
SRANGDVDQY EVQLLFNDMK VFPHIHLVNT ATEYKFTALT PGRHYKILVL TISGDVQQSA 

       910        920        930        940        950        960 
FIEGLTVPST VKNIHISANG ATDRLMVTWS PGGGDVDSYV VSAFRQDEKV DSQTIPKHAS 

       970        980        990       1000       1010       1020 
EHTFHRLEAG AKYRIAIVSV SGSLRNQIDA LGQTVPASVQ GVVAANAYSS NSLTVSWQKA 

      1030       1040       1050       1060       1070       1080 
LGVAERYDIL LLNENGLLLS NVSEPATARQ HKFEDLTPGK KYKMQILTVS GGLFSKESQA 

      1090       1100       1110       1120       1130       1140 
EGRTVPAAVT NLRITENSSR YLSFGWTASE GELSWYNIFL YNPDRTLQER AQVDPLVQSF 

      1150       1160       1170       1180       1190       1200 
SFQNLLQGRM YKMVIVTHSG ELSNESFIFG RTVPAAVNHL KGSHRNTTDS LWFSWSPASG 

      1210       1220       1230       1240       1250       1260 
DFDFYELILY NPNGTKKENW KEKDVTEWRF QGLVPGRKYT LYVVTHSGDL SNKVTGEGRT 

      1270       1280       1290       1300       1310       1320 
APSPPSLLSF ADVANTSLAI TWKGPPDWTD YNDFELQWFP GDALTIFNPY SSRKSEGRIV 

      1330       1340       1350       1360       1370       1380 
YGLHPGRSYQ FSVKTVSGDS WKTYSKPISG SVRTKPDKIQ NLHCRPQNST AIACSWIPPD 

      1390       1400       1410       1420       1430       1440 
SDFDGYSIEC RKMDTQEIEF SRKLEKEKSL LNIMMLVPHK RYLVSIKVQS AGMTSEVVED 

      1450       1460       1470       1480       1490       1500 
STITMIDRPP QPPPHIRVNE KDVLISKSSI NFTVNCSWFS DTNGAVKYFA VVVREADSMD 

      1510       1520       1530       1540       1550       1560 
ELKPEQQHPL PSYLEYRHNA SIRVYQTNYF ASKCAESPDS SSKSFNIKLG AEMDSLGGKC 

      1570       1580       1590       1600       1610       1620 
DPSQQKFCDG PLKPHTAYRI SIRAFTQLFD EDLKEFTKPL YSDTFFSMPI TTESEPLFGV 

      1630       1640       1650       1660       1670       1680 
IEGVSAGLFL IGMLVALVAF FICRQKASHS RERPSARLSI RRDRPLSVHL NLGQKGNRKT 

      1690       1700       1710       1720       1730       1740 
SCPIKINQFE GHFMKLQADS NYLLSKEYED LKDVGRSQSC DIALLPENRG KNRYNNILPY 

      1750       1760       1770       1780       1790       1800 
DASRVKLCNV DDDPCSDYIN ASYIPGNNFR REYIATQGPL PGTKDDFWKM AWEQNVHNIV 

      1810       1820       1830       1840       1850       1860 
MVTQCVEKGR VKCDHYWPAD QDPLYYGDLI LQMVSESVLP EWTIREFKIC SEEQLDAHRL 

      1870       1880       1890       1900       1910       1920 
IRHFHYTVWP DHGVPETTQS LIQFVRTVRD YINRSPGAGP TVVHCSAGVG RTGTFVALDR 

      1930       1940       1950       1960       1970       1980 
ILQQLDSKDS VDIYGAVHDL RLHRVHMVQT ECQYVYLHQC VRDVLRAKKL RNEQENPLFP 

      1990 
IYENVNPEYH RDAIYSRH

« Hide

References

« Hide 'large scale' references
[1]"VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts."
Nawroth R., Poell G., Ranft A., Kloep S., Samulowitz U., Fachinger G., Golding M., Shima D.T., Deutsch U., Vestweber D.
EMBO J. 21:4885-4895(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CDH5, DOMAIN, MUTAGENESIS OF ARG-1911.
Strain: Swiss Webster / NIH.
[2]Erratum
Nawroth R., Poell G., Ranft A., Kloep S., Samulowitz U., Fachinger G., Golding M., Shima D.T., Deutsch U., Vestweber D.
EMBO J. 24:3158-3158(2005)
[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. expand/collapse author list , 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].
Strain: C57BL/6 and C57BL/6J.
Tissue: Brain.
[4]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].
[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].
Tissue: Brain.
[6]"Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2."
Fachinger G., Deutsch U., Risau W.
Oncogene 18:5948-5953(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TEK, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development."
Bauemer S., Keller L., Holtmann A., Funke R., August B., Gamp A., Wolburg H., Wolburg-Buchholz K., Deutsch U., Vestweber D.
Blood 107:4754-4762(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]"Vascular endothelial tyrosine phosphatase (VE-PTP)-null mice undergo vasculogenesis but die embryonically because of defects in angiogenesis."
Dominguez M.G., Hughes V.C., Pan L., Simmons M., Daly C., Anderson K., Noguera-Troise I., Murphy A.J., Valenzuela D.M., Davis S., Thurston G., Yancopoulos G.D., Gale N.W.
Proc. Natl. Acad. Sci. U.S.A. 104:3243-3248(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[9]"VE-PTP maintains the endothelial barrier via plakoglobin and becomes dissociated from VE-cadherin by leukocytes and by VEGF."
Nottebaum A.F., Cagna G., Winderlich M., Gamp A.C., Linnepe R., Polaschegg C., Filippova K., Lyck R., Engelhardt B., Kamenyeva O., Bixel M.G., Butz S., Vestweber D.
J. Exp. Med. 205:2929-2945(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDH5.
[10]"VE-PTP controls blood vessel development by balancing Tie-2 activity."
Winderlich M., Keller L., Cagna G., Broermann A., Kamenyeva O., Kiefer F., Deutsch U., Nottebaum A.F., Vestweber D.
J. Cell Biol. 185:657-671(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TEK.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY077755 mRNA. Translation: AAL75813.1.
AK147439 mRNA. Translation: BAE27912.1.
AK147668 mRNA. Translation: BAE28060.1.
CH466539 Genomic DNA. Translation: EDL21786.1.
BC141006 mRNA. Translation: AAI41007.1.
BC145111 mRNA. Translation: AAI45112.1.
IPIIPI00229935.
RefSeqNP_084204.2. NM_029928.2.
UniGeneMm.37213.
Mm.489025.

3D structure databases

ProteinModelPortalB2RU80.
SMRB2RU80. Positions 31-1426, 1688-1968.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-8298798.

PTM databases

PhosphoSiteB2RU80.

Proteomic databases

PaxDbB2RU80.
PRIDEB2RU80.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092167; ENSMUSP00000089805; ENSMUSG00000020154.
GeneID19263.
KEGGmmu:19263.
UCSCuc007hbv.2. mouse.

Organism-specific databases

CTD5787.
MGIMGI:97809. Ptprb.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00700000104166.
HOGENOMHOG000060224.
HOVERGENHBG053759.
InParanoidQ3UGZ7.
KOK05694.
OMAFTVNCSW.

Gene expression databases

ArrayExpressB2RU80.
BgeeB2RU80.
GenevestigatorB2RU80.

Family and domain databases

Gene3D2.60.40.10. 15 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 15 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 16 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF49265. FN_III-like. 16 hits.
PROSITEPS50853. FN3. 16 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296128.
SOURCESearch...

Entry information

Entry namePTPRB_MOUSE
AccessionPrimary (citable) accession number: B2RU80
Secondary accession number(s): Q3UGZ7, Q8CIW2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: July 1, 2008
Last modified: May 29, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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