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Q62656

- PTPRZ_RAT

UniProt

Q62656 - PTPRZ_RAT

Protein

Receptor-type tyrosine-protein phosphatase zeta

Gene

Ptprz1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades By similarity.By similarity
    Isoform 3 (phosphacan), previously designated 3F8 chondroitin sulfate proteoglycan or 3H1 keratan sulfate proteoglycan depending on the glycosylation status, is a soluble nervous tissue-specific proteoglycan. It is synthesized by glia and binds to neurons and to the neural cell adhesion molecules tenascin, N-CAM or NG-CAM but not to laminin and fibronectin. Phosphacan acts as a potent inhibitor of cell adhesion and neurite outgrowth.

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1902 – 19021SubstrateBy similarity
    Active sitei1934 – 19341Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei1978 – 19781SubstrateBy similarity
    Sitei2224 – 22241Ancestral active site

    GO - Molecular functioni

    1. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. learning or memory Source: UniProtKB
    2. oligodendrocyte differentiation Source: UniProtKB
    3. peptidyl-tyrosine dephosphorylation Source: UniProtKB
    4. regulation of oligodendrocyte progenitor proliferation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase zeta (EC:3.1.3.48)
    Short name:
    R-PTP-zeta
    Alternative name(s):
    3F8 chondroitin sulfate proteoglycan
    3H1 keratan sulfate proteoglycan
    Phosphacan
    Gene namesi
    Name:Ptprz1
    Synonyms:Ptprz, Ptpz
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3455. Ptprz1.

    Subcellular locationi

    Isoform 1 : Cell membrane; Single-pass type I membrane protein. Secreted By similarity
    Note: A secreted form is apparently generated by shedding of the extracellular domain.By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 23162292Receptor-type tyrosine-protein phosphatase zetaPRO_0000025469Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi56 ↔ 240By similarity
    Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi133 ↔ 264By similarity
    Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi497 – 4971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi595 – 5951O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi610 – 6101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi645 – 6451O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi685 – 6851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi786 – 7861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1005 – 10051O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi1025 – 10251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1058 – 10581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1463 – 14631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1550 – 15501O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi1552 – 15521O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi1563 – 15631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1611 – 16111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1619 – 16191N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2056 – 20561PhosphoserineBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ62656.
    PRIDEiQ62656.

    PTM databases

    PhosphoSiteiQ62656.

    Expressioni

    Tissue specificityi

    Nervous tissue specific.

    Gene expression databases

    GenevestigatoriQ62656.

    Interactioni

    Subunit structurei

    The carbonic-anhydrase like domain interacts with CNTN1 (contactin).3 Publications

    Protein-protein interaction databases

    DIPiDIP-59715N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62656.
    SMRiQ62656. Positions 1699-2285.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 16371613ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1664 – 2316653CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1638 – 166326HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 300265Alpha-carbonic anhydraseAdd
    BLAST
    Domaini314 – 413100Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST
    Domaini1718 – 1993276Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2024 – 2283260Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1934 – 19407Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi951 – 9544Poly-Ser
    Compositional biasi1225 – 12306Poly-Ser
    Compositional biasi1426 – 143914Poly-AspAdd
    BLAST

    Sequence similaritiesi

    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
    Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000090262.
    HOVERGENiHBG053760.
    InParanoidiQ62656.
    KOiK08114.
    PhylomeDBiQ62656.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.10.200.10. 1 hit.
    3.90.190.10. 2 hits.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00194. Carb_anhydrase. 1 hit.
    PF00041. fn3. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    SM00060. FN3. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF51069. SSF51069. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEiPS51144. ALPHA_CA_2. 1 hit.
    PS50853. FN3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q62656-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MRILQSFLAC VQLLCVCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG     50
    KKYPICNSPK QSPINIDEDL TQVNVNLKKL KFQGWEKPSL ENTFIHNTGK 100
    TVEINLTNDY YLSGGLSEKV FKASKMTFHW GKCNVSSEGS EHSLEGQKFP 150
    LEMQIYCFDA DRFSSFEETV KGKGRLRALS ILFEIGVEEN LDYKAIIDGT 200
    ESVSRFGKQA ALDPFILQNL LPNSTDKYYI YNGSLTSPPC TDTVEWIVFK 250
    DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY 300
    TGKEEIHEAV CSSEPENVQA DPENYTSLLI TWERPRVVYD TMIEKFAVLY 350
    QPLEGNDQTK HEFLTDGYQD LGAILNNLIP NMSYVLQIVA ICSNGLYGKY 400
    SDQLIVDMPT EDAELDLFPE LIGTEEIIKE ENYGKGNEED TGLNPGRDSA 450
    TNQIRKKEPQ VSTTTHYNHM GTKYNEAKTN RSPTRGSEFS GKSDVLNTSL 500
    NPTSQQVAEF NPEREMSLPS QIGTNLPPHS VEGTSASLNS GSKTLLVFPQ 550
    MNLSGTAESL NMVSITEYKE VSADLSEEEN LLTDFKLDSG ADDSSGSSPA 600
    SSTVPFSTDN LSHGYTSSSD TPEAVTYDVL RPESTRNALE DSAPSGSEES 650
    LKDPSLEGSV WFPGSTDLTT QSETGSGREG FLQVNSTDFQ VDESRETTET 700
    FSPDATASRG PSVTDMEMPH YSTFAYPPTE VTSHAFTPSS RPLDLAPTSN 750
    ILHSQTTQPV YNGETPLQPS YSSEVFPLVT PLLLDNQTLN TTPAASSSDS 800
    ALHATPVFPS VGVSFDSILS SYDDAPLLPF SSASFSSDLF HHLHTVSQTL 850
    PQVTSAAERD ELSLHASLLV AGGDLLLEPS LVQYSDVMSH QVTIHAASDT 900
    LEFGSESAVL YKTSMVSQIE SPSSDVVMHA YSSGPETSYA IEGSHHVLTV 950
    SSSSAIPVHD SVGVADQGSL LINPSHISLP ESSFITPTAS LLQLPPALSG 1000
    DGEWSGASSD SELLLPDTDG LRTLNMSSPV SVADFTYTTS VSGDDIKPLS 1050
    KGEMMYGNET ELKMSSFSDM AYPSKSTVVP KMSDIVNKWS ESLKETSVSV 1100
    SSINSVFTES LVYPITKVFD QEISRVPEII FPVKPTHTAS QASGDTWLKP 1150
    GLSTNSEPAL SDTASSEVSH PSTQPLLYEA ASPFNTEALL QPSFPASDVD 1200
    TLLKTALPSG PRDPVLTETP MVEQSSSSVS LPLASESASS KSTLHFTSVP 1250
    VLNMSPSDVH PTSLQRLTVP HSREEYFEQG LLKSKSPQQV LPSLHSHDEF 1300
    FQTAHLDISQ AYPPKGRHAF ATPILSINEP QNTLINRLVY SEDIFMHPEI 1350
    SITDKALTGL PTTVSDVLIA TDHSVPLGSG PISMTTVSPN RDDSVTTTKL 1400
    LLPSKATSKP THSARSDADL VGGGEDGDDY DDDDYDDIDS DRFPVNKCMS 1450
    CSPYRESQEK VMNDSDTQES SLVDQSDPIS HLLSENTEEE NGGTGVTRVD 1500
    KSPDKSPPPS MLPQKHNDGR EDRDIQMGSA VLPHTPGSKA WAVLTSDEES 1550
    GSGQGTSDSL NDNETSTDFS FPDVNEKDAD GVLEADDTGI APGSPRSSTP 1600
    SVTSGHSGVS NSSEAEASNS SHESRIGLAE GLESEKKAVI PLVIVSALTF 1650
    ICLVVLVGIL IYWRKCFQTA HFYLEDNTSP RVISTPPTPI FPISDDIGAI 1700
    PIKHFPKHVA DLHASNGFTE EFETLKEFYQ EVQSCTVDLG ITADSSNHPD 1750
    NKHKNRYVNI VAYDHSRVKL TQLAEKDGKL TDYINANYVD GYNRPKAYIA 1800
    AQGPLKSTAE DFWRMIWEHN VEVIVMITNL VEKGRRKCDQ YWPTDGSEEY 1850
    GSFLVNQKNV QVLAYYTVRN FTLRNTKIKK GSQKGRSSGR LVTQYHYTQW 1900
    PDMGVPEYSL PVLAFVRKTA QAKRHAVGPV VVHCSAGVGR TGTYIVLDSM 1950
    LQQIQHEGTV NIFGFLKHIR SQRNYLVQTE EQYVFIHDTL VEAILSKETE 2000
    VPDSHIHSYV NTLLIPGPSG KTKLEKQFQL LSQSNILQSD YSTALKQCNR 2050
    EKNRTSSIIP VERSRVGISS LSGEGTDYIN ASYIMGYYQS NEFIITQHPL 2100
    LHTIKDFWRM IWDHNAQLVV MIPDGQNMAE DEFVYWPNKD EPINCESFKV 2150
    TLMSEEHKCL SNEEKLIVQD FILEATQDDY VLEVRHFQCP KWPNPDSPIS 2200
    KTFELISIIK EEAANRDGPM IVHDEHGGVT AGTFCALTTL MHQLEKENSM 2250
    DVYQVAKMIN LMRPGVFTDI EQYQFLYKVV LSLVSTRQEE NPSTSLDSNG 2300
    AALPDGNIAE SLESLV 2316
    Length:2,316
    Mass (Da):255,342
    Last modified:November 1, 1996 - v1
    Checksum:i419EA9B89BDD165F
    GO
    Isoform 2 (identifier: Q62656-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         763-1615: Missing.

    Show »
    Length:1,463
    Mass (Da):164,596
    Checksum:iFF524D7DA90C4BE0
    GO
    Isoform 3 (identifier: Q62656-3) [UniParc]FASTAAdd to Basket

    Also known as: Phosphacan

    The sequence of this isoform differs from the canonical sequence as follows:
         1616-1616: E → G
         1617-2316: Missing.

    Show »
    Length:1,616
    Mass (Da):175,839
    Checksum:i6F02DDE391A41117
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei763 – 1615853Missing in isoform 2. 1 PublicationVSP_005152Add
    BLAST
    Alternative sequencei1616 – 16161E → G in isoform 3. 1 PublicationVSP_005153
    Alternative sequencei1617 – 2316700Missing in isoform 3. 1 PublicationVSP_005154Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09357 mRNA. Translation: AAC52207.1.
    U04998 mRNA. Translation: AAC52383.1.
    PIRiA40169.
    RefSeqiNP_001164156.1. NM_001170685.1.
    NP_037212.2. NM_013080.2.
    UniGeneiRn.10088.

    Genome annotation databases

    GeneIDi25613.
    KEGGirno:25613.
    UCSCiRGD:3455. rat. [Q62656-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09357 mRNA. Translation: AAC52207.1 .
    U04998 mRNA. Translation: AAC52383.1 .
    PIRi A40169.
    RefSeqi NP_001164156.1. NM_001170685.1.
    NP_037212.2. NM_013080.2.
    UniGenei Rn.10088.

    3D structure databases

    ProteinModelPortali Q62656.
    SMRi Q62656. Positions 1699-2285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59715N.

    PTM databases

    PhosphoSitei Q62656.

    Proteomic databases

    PaxDbi Q62656.
    PRIDEi Q62656.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25613.
    KEGGi rno:25613.
    UCSCi RGD:3455. rat. [Q62656-1 ]

    Organism-specific databases

    CTDi 5803.
    RGDi 3455. Ptprz1.

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000090262.
    HOVERGENi HBG053760.
    InParanoidi Q62656.
    KOi K08114.
    PhylomeDBi Q62656.

    Miscellaneous databases

    NextBioi 607359.
    PROi Q62656.

    Gene expression databases

    Genevestigatori Q62656.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.10.200.10. 1 hit.
    3.90.190.10. 2 hits.
    InterProi IPR001148. Carbonic_anhydrase_a.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00194. Carb_anhydrase. 1 hit.
    PF00041. fn3. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM01057. Carb_anhydrase. 1 hit.
    SM00060. FN3. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF51069. SSF51069. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEi PS51144. ALPHA_CA_2. 1 hit.
    PS50853. FN3. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and molecular variants of rat receptor-type protein tyrosine phosphatase-zeta/beta."
      Maurel P., Meyer-Puttlitz B., Flad M., Margolis R.U., Margolis R.K.
      DNA Seq. 5:323-328(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Strain: Sprague-Dawley.
      Tissue: Brain.
    2. "Phosphacan, a chondroitin sulfate proteoglycan of brain that interacts with neurons and neural cell-adhesion molecules, is an extracellular variant of a receptor-type protein tyrosine phosphatase."
      Maurel P., Rauch U., Flad M., Margolis R.K., Margolis R.U.
      Proc. Natl. Acad. Sci. U.S.A. 91:2512-2516(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PARTIAL PROTEIN SEQUENCE.
      Strain: Sprague-Dawley.
      Tissue: Brain.
    3. "Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules."
      Milev P., Friedlander D.R., Sakurai T., Karthikeyan L., Flad M., Margolis R.K., Grumet M., Margolis R.U.
      J. Cell Biol. 127:1703-1715(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH N-CAM AND NG-CAM.
    4. "Interactions with tenascin and differential effects on cell adhesion of neurocan and phosphacan, two major chondroitin sulfate proteoglycans of nervous tissue."
      Grumet M., Milev P., Sakurai T., Karthikeyan L., Bourdon M., Margolis R.K., Margolis R.U.
      J. Biol. Chem. 269:12142-12146(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TENASCIN.
    5. "The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin."
      Peles E., Nativ M., Campbell P.L., Sakurai T., Martinez R., Lev S., Clary D.O., Schilling J., Barnea G., Plowman G.D., Grumet M., Schlessinger J.
      Cell 82:251-260(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CONTACTIN.

    Entry informationi

    Entry nameiPTPRZ_RAT
    AccessioniPrimary (citable) accession number: Q62656
    Secondary accession number(s): Q62621
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 134 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3