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P49446 (PTPRE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase epsilon

Short name=Protein-tyrosine phosphatase epsilon
Short name=R-PTP-epsilon
EC=3.1.3.48
Gene names
Name:Ptpre
Synonyms:Ptpe
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length699 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1 acts as a negative regulator of insulin receptor (IR) signaling and is involved in insulin-induced glucose metabolism mainly through direct dephosphorylation and inactivation of IR in hepatocytes and liver By similarity. Plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function. Ref.3 Ref.15 Ref.16 Ref.18

Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake. Ref.3 Ref.15 Ref.16 Ref.18

Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca2+. Ref.3 Ref.15 Ref.16 Ref.18

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulation

Isoform 1 is inhibited by alendronate (ALN), orthovanadate, and phenylarsine oxide (PAO). Ref.3

Subunit structure

Monomer By similarity. Isoform 2:Homodimer. Can form oligomers. Dimerization is increased by oxidative stress and decreased by EGFR. Isoform 2 interacts with GRB2 By similarity. Ref.13

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.12 Ref.15.

Isoform 2: Cytoplasm Ref.12 Ref.15. Note: Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin can induce translocation to the membrane. Ref.12 Ref.15

Isoform 3: Cytoplasm Ref.12 Ref.15.

Tissue specificity

Isoform 2 is expressed in the spleen and thymus (at protein level). Detected in fibroblasts, myeloid cells, macrophages, and T-cells but not in B-cell lines. Isoform 1 and isoform 2 are expressed predominantly in the brain, testes, and lungs, with lower levels present in lymph nodes, thymus, spleen, heart and mammary glands. Isoform 1 is expressed in osteoclasts and not in osteoblasts and its expression is related to osteoclast differentiation. It is also expressed in the erythrocytes. Isoform 2 is strongly expressed in skeletal muscle and L6 skeletal muscle cell line. Ref.2 Ref.3 Ref.9 Ref.15 Ref.16

Induction

Isoform 2 is induced by 12-O-tetradecanoylphorbol-13-acetate (TPA) and its induction is dependent upon PKC activity. Ref.2 Ref.3

Domain

The tyrosine-protein phosphatase 2 domain (D2) mediates dimerization. The extreme N- and C- termini of the D2 domain act to inhibit dimerization and removal of these sequences increases dimerization and inhibits enzyme activity. Ref.13

Post-translational modification

A catalytically active cytoplasmic form (p65) is produced by proteolytic cleavage of either isoform 1, isoform 2 or isoform 3.

Isoform 1 and isoform 2 are phosphorylated on tyrosine residues by tyrosine kinase Neu By similarity.

Isoform 1 is glycosylated By similarity.

Disruption phenotype

Mice show greater insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1) in the skeletal muscle. Antigen- and IgE-mediated passive systemic anaphylactic reactions are enhanced. Erythrocytes exhibit abnormal morphology, increased Ca2+-activated-K+ channel activity and marked perturbation of the erythrocyte membrane tyrosine phosphoproteome. Ref.15 Ref.16 Ref.18

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 4 subfamily.

Contains 2 tyrosine-protein phosphatase domains.

Biophysicochemical properties

Kinetic parameters:

KM=70 µM for fluorescein diphosphate (isoform 1) Ref.3

Vmax=6 µmol/min/mg enzyme for fluorescein diphosphate (isoform 1)

Alternative products

This entry describes 3 isoforms produced by alternative promoter usage and alternative initiation. [Align] [Select]
Isoform 1 (identifier: P49446-1)

Also known as: PTPeM; RPTPe; tm-PTPe;

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.
Note: Produced by alternative promoter usage.
Isoform 2 (identifier: P49446-2)

Also known as: PTPeC; cyt-PTPe;

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: MEPFCPLLLA...LFLLAAYFFR → MSSRKNFSRLTW
Note: Produced by alternative promoter usage.
Isoform 3 (identifier: P49446-3)

Also known as: p67;

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.
Note: Produced by alternative initiation at Met-85 of isoform 1.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 699680Receptor-type tyrosine-protein phosphatase epsilon
PRO_0000025440

Regions

Topological domain20 – 4526Extracellular Potential
Transmembrane46 – 6823Helical; Potential
Topological domain69 – 699631Cytoplasmic Potential
Domain134 – 393260Tyrosine-protein phosphatase 1
Domain425 – 688264Tyrosine-protein phosphatase 2
Region334 – 3407Substrate binding By similarity

Sites

Active site3341Phosphocysteine intermediate By similarity
Active site6291Phosphocysteine intermediate By similarity
Binding site3021Substrate By similarity
Binding site3781Substrate By similarity

Amino acid modifications

Modified residue6951Phosphotyrosine Ref.14 Ref.17
Glycosylation231N-linked (GlcNAc...) Potential
Glycosylation311N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 8484Missing in isoform 3.
VSP_038491
Alternative sequence1 – 6969MEPFC…AYFFR → MSSRKNFSRLTW in isoform 2.
VSP_038492

Experimental info

Sequence conflict1371E → K in BAE32920. Ref.6
Sequence conflict5001G → A in BAA11927. Ref.4
Sequence conflict5061V → G in AAC52281. Ref.1
Sequence conflict5061V → G in AAC52331. Ref.2
Sequence conflict5061V → G in AAB04553. Ref.5
Sequence conflict521 – 5222IV → ML in BAA11927. Ref.4
Sequence conflict6061M → I in AAC52281. Ref.1
Sequence conflict6061M → I in AAC52331. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PTPeM) (RPTPe) (tm-PTPe) [UniParc].

Last modified December 15, 2009. Version 3.
Checksum: 581EF9CB881BC05B

FASTA69980,688
        10         20         30         40         50         60 
MEPFCPLLLA SFSLSLARAG QGNDTTPTES NWTSTTAGPP DPGASQPLLT WLLLPLLLLL 

        70         80         90        100        110        120 
FLLAAYFFRF RKQRKAVVSS NDKKMPNGIL EEQEQQRVML LSRSPSGPKK FFPIPVEHLE 

       130        140        150        160        170        180 
EEIRVRSADD CKRFREEFNS LPSGHIQGTF ELANKEENRE KNRYPNILPN DHCRVILSQV 

       190        200        210        220        230        240 
DGIPCSDYIN ASYIDGYKEK NKFIAAQGPK QETVNDFWRM VWEQRSATIV MLTNLKERKE 

       250        260        270        280        290        300 
EKCYQYWPDQ GCWTYGNIRV CVEDCVVLVD YTIRKFCIHP QLPDSCKAPR LVSQLHFTSW 

       310        320        330        340        350        360 
PDFGVPFTPI GMLKFLKKVK TLNPSHAGPI VVHCSAGVGR TGTFIVIDAM MDMIHSEQKV 

       370        380        390        400        410        420 
DVFEFVSRIR NQRPQMVQTD VQYTFIYQAL LEYYLYGDTE LDVSSLERHL QTLHSTATHF 

       430        440        450        460        470        480 
DKIGLEEEFR KLTNVRIMKE NMRTGNLPAN MKKARVIQII PYDFNRVILS MKRGQEFTDY 

       490        500        510        520        530        540 
INASFIDGYR QKDYFMATQG PLAHTVEDFW RMVWEWKSHT IVMLTEVQER EQDKCYQYWP 

       550        560        570        580        590        600 
TEGSVTHGDI TIEIKSDTLS EAISVRDFLV TFKQPLARQE EQVRMVRQFH FHGWPEVGIP 

       610        620        630        640        650        660 
AEGKGMIDLI AAVQKQQQQT GNHPITVHCS AGAGRTGTFI ALSNILERVK AEGLLDVFQA 

       670        680        690 
VKSLRLQRPH MVQTLEQYEF CYKVVQDFID IFSDYANFK 

« Hide

Isoform 2 (PTPeC) (cyt-PTPe) [UniParc].

Checksum: 92F99E9729D8F1F3
Show »

FASTA64274,735
Isoform 3 (p67) [UniParc].

Checksum: 56E0BE70BB2BB59C
Show »

FASTA61571,467

References

« Hide 'large scale' references
[1]"Protein-tyrosine phosphatase epsilon. An isoform specifically expressed in mouse mammary tumors initiated by v-Ha-ras OR neu."
Elson A., Leder P.
J. Biol. Chem. 270:26116-26122(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: FVB/N.
[2]"Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon."
Elson A., Leder P.
Proc. Natl. Acad. Sci. U.S.A. 92:12235-12239(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, TISSUE SPECIFICITY.
[3]"Protein-tyrosine phosphatase activity regulates osteoclast formation and function: inhibition by alendronate."
Schmidt A., Rutledge S.J., Endo N., Opas E., Tanaka H., Wesolowski G., Leu C.T., Huang Z., Ramachandaran C., Rodan S.B., Rodan G.A.
Proc. Natl. Acad. Sci. U.S.A. 93:3068-3073(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY.
Tissue: Osteoclast.
[4]Mukouyama Y.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: DBA/2.
[5]Hou E.W., Li S.L.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain and Lung.
[6]"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] (ISOFORM 2).
Strain: NOD.
[7]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].
[8]"Identification and typing of members of the protein-tyrosine phosphatase gene family expressed in mouse brain."
Schepens J., Zeeuwen P., Wieringa B., Hendriks W.
Mol. Biol. Rep. 16:241-248(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-332.
Strain: BALB/c.
Tissue: Brain.
[9]"Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification."
Yi T., Cleveland J.L., Ihle J.N.
Blood 78:2222-2228(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-332, TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Myeloid leukemia cell.
[10]"A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain."
Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.
Biochem. J. 305:499-504(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-332.
Strain: BALB/c.
Tissue: Brain.
[11]"Distinct promoters control transmembrane and cytosolic protein tyrosine phosphatase epsilon expression during macrophage differentiation."
Tanuma N., Nakamura K., Kikuchi K.
Eur. J. Biochem. 259:46-54(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE PROMOTER USAGE.
[12]"Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control."
Gil-Henn H., Volohonsky G., Toledano-Katchalski H., Gandre S., Elson A.
Oncogene 19:4375-4384(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION (ISOFORM 3), ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
[13]"Dimerization in vivo and inhibition of the nonreceptor form of protein tyrosine phosphatase epsilon."
Toledano-Katchalski H., Tiran Z., Sines T., Shani G., Granot-Attas S., den Hertog J., Elson A.
Mol. Cell. Biol. 23:5460-5471(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, DOMAIN.
[14]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[15]"Cytosolic protein tyrosine phosphatase-epsilon is a negative regulator of insulin signaling in skeletal muscle."
Aga-Mizrachi S., Brutman-Barazani T., Jacob A.I., Bak A., Elson A., Sampson S.R.
Endocrinology 149:605-614(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[16]"PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells."
De Franceschi L., Biondani A., Carta F., Turrini F., Laudanna C., Deana R., Brunati A.M., Turretta L., Iolascon A., Perrotta S., Elson A., Bulato C., Brugnara C.
Proteomics 8:4695-4708(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM 1), DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[17]"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 TYR-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Protein tyrosine phosphatase epsilon is a negative regulator of FcepsilonRI-mediated mast cell responses."
Akimoto M., Mishra K., Lim K.-T., Tani N., Hisanaga S.-I., Katagiri T., Elson A., Mizuno K., Yakura H.
Scand. J. Immunol. 69:401-411(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U35368 mRNA. Translation: AAC52281.1.
U36758 mRNA. Translation: AAC52331.1.
U40280 mRNA. Translation: AAB02190.1.
D83484 mRNA. Translation: BAA11927.1.
U62387 mRNA. Translation: AAB04553.1.
AK154910 mRNA. Translation: BAE32920.1.
CH466531 Genomic DNA. Translation: EDL17805.1.
CH466531 Genomic DNA. Translation: EDL17807.1.
Z23052 mRNA. Translation: CAA80587.1.
Z23053 mRNA. Translation: CAA80588.1.
PIRB61180.
JC6132.
S40284.
RefSeqNP_035342.3. NM_011212.3.
XP_006507522.1. XM_006507459.1.
XP_006507523.1. XM_006507460.1.
XP_006507524.1. XM_006507461.1.
UniGeneMm.945.

3D structure databases

ProteinModelPortalP49446.
SMRP49446. Positions 110-690.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202496. 1 interaction.
IntActP49446. 6 interactions.

PTM databases

PhosphoSiteP49446.

Proteomic databases

PaxDbP49446.
PRIDEP49446.

Protocols and materials databases

DNASU19267.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000073961; ENSMUSP00000073616; ENSMUSG00000041836. [P49446-1]
GeneID19267.
KEGGmmu:19267.
UCSCuc009kee.1. mouse. [P49446-1]
uc009kek.1. mouse. [P49446-2]

Organism-specific databases

CTD5791.
MGIMGI:97813. Ptpre.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00590000082937.
HOVERGENHBG053758.
InParanoidQ61042.
KOK18033.
OMAPDGCKAP.
OrthoDBEOG7B31M8.
PhylomeDBP49446.
TreeFamTF351829.

Gene expression databases

BgeeP49446.
CleanExMM_PTPRE.
GenevestigatorP49446.

Family and domain databases

InterProIPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR016336. Tyr_Pase_rcpt_a/e-type.
[Graphical view]
PfamPF00102. Y_phosphatase. 2 hits.
[Graphical view]
PIRSFPIRSF002006. PTPR_alpha_epsilon. 1 hit.
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 2 hits.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPRE. mouse.
NextBio296146.
PROP49446.
SOURCESearch...

Entry information

Entry namePTPRE_MOUSE
AccessionPrimary (citable) accession number: P49446
Secondary accession number(s): Q3U369 expand/collapse secondary AC list , Q60986, Q61042, Q62134, Q62444, Q64496
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 15, 2009
Last modified: April 16, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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