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P23471 (PTPRZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=R-PTP-zeta
EC=3.1.3.48
Alternative name(s):
Protein-tyrosine phosphatase receptor type Z polypeptide 1
Protein-tyrosine phosphatase receptor type Z polypeptide 2
R-PTP-zeta-2
Gene names
Name:PTPRZ1
Synonyms:HTPZP2, PTPRZ, PTPRZ2, PTPZ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2315 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

The carbonic-anhydrase like domain interacts with CNTN1 (contactin). Ref.11

Subcellular location

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.

Isoform 2: Secreted Potential.

Tissue specificity

Specifically expressed in the central nervous system, where it is localized in the Purkinje cell layer of the cerebellum, the dentate gyrus, and the subependymal layer of the anterior horn of the lateral ventricle. Developmentally regulated in the brain. Ref.6

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 5 subfamily.

Contains 1 alpha-carbonic anhydrase domain.

Contains 1 fibronectin type-III domain.

Contains 2 tyrosine-protein phosphatase domains.

Caution

Was termed (Ref.2 and Ref.7) RPTPase beta.

The human genome was initially thought to contain 2 genes for PTPRZ: PTPRZ1 (on chr 7) and PTPRZ2 (on chr 1). However, PTPRZ2 probably does not exist and corresponds to PTPRZ1.

Sequence caution

The sequence AAC39934.1 differs from that shown. Reason: Contaminating sequence. The N-terminus may be contaminated with vector sequence.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxonogenesis

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Traceable author statement Ref.2. Source: ProtInc

learning or memory

Inferred from sequence or structural similarity. Source: UniProtKB

oligodendrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein dephosphorylation

Traceable author statement Ref.1. Source: ProtInc

regulation of oligodendrocyte progenitor proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentintegral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

perineuronal net

Inferred from electronic annotation. Source: Ensembl

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 17681947. Source: IntAct

protein tyrosine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine phosphatase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ALKQ9UM732EBI-2263175,EBI-357361

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P23471-1)

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.
Isoform 2 (identifier: P23471-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1723-1729: Missing.
Isoform 3 (identifier: P23471-3)

The sequence of this isoform differs from the canonical sequence as follows:
     755-1614: Missing.
     1723-1729: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Chain25 – 23152291Receptor-type tyrosine-protein phosphatase zeta
PRO_0000025468

Regions

Topological domain25 – 16361612Extracellular Potential
Transmembrane1637 – 166226Helical; Potential
Topological domain1663 – 2315653Cytoplasmic Potential
Domain36 – 300265Alpha-carbonic anhydrase
Domain314 – 413100Fibronectin type-III
Domain1717 – 1992276Tyrosine-protein phosphatase 1
Domain2023 – 2282260Tyrosine-protein phosphatase 2
Region1933 – 19397Substrate binding By similarity

Sites

Active site19331Phosphocysteine intermediate By similarity
Binding site19011Substrate By similarity
Binding site19771Substrate By similarity
Site22231Ancestral active site

Amino acid modifications

Modified residue20551Phosphoserine Ref.10
Glycosylation1051N-linked (GlcNAc...) Ref.9
Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation4971N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Glycosylation5521N-linked (GlcNAc...) Potential
Glycosylation5871O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation6021N-linked (GlcNAc...) Potential
Glycosylation6291N-linked (GlcNAc...) Potential
Glycosylation6371O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation6771N-linked (GlcNAc...) Potential
Glycosylation9971O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation10171N-linked (GlcNAc...) Potential
Glycosylation10501N-linked (GlcNAc...) Potential
Glycosylation10821N-linked (GlcNAc...) Potential
Glycosylation11221N-linked (GlcNAc...) Potential
Glycosylation14571N-linked (GlcNAc...) Potential
Glycosylation15491O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation15511O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation15621N-linked (GlcNAc...) Potential
Glycosylation16181N-linked (GlcNAc...) Potential
Disulfide bond56 ↔ 240 Ref.11
Disulfide bond133 ↔ 264 Ref.11

Natural variations

Alternative sequence755 – 1614860Missing in isoform 3.
VSP_054061
Alternative sequence1723 – 17297Missing in isoform 2 and isoform 3.
VSP_054062
Natural variant31I → S.
Corresponds to variant rs740965 [ dbSNP | Ensembl ].
VAR_038942
Natural variant61R → L.
Corresponds to variant rs11980387 [ dbSNP | Ensembl ].
VAR_038943
Natural variant14331G → D. Ref.1 Ref.4 Ref.5
Corresponds to variant rs1147504 [ dbSNP | Ensembl ].
VAR_038944

Experimental info

Sequence conflict3101V → A in AAC39934. Ref.6
Sequence conflict3121S → R in AAC39934. Ref.6
Sequence conflict14261Missing in AAA60225. Ref.1
Sequence conflict14261Missing Ref.2
Sequence conflict14261Missing in EAL24344. Ref.4
Sequence conflict14261Missing in EAW83561. Ref.5

Secondary structure

.................................................... 2315
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 24, 2009. Version 4.
Checksum: ED9DD98D4CCA2883

FASTA2,315254,587
        10         20         30         40         50         60 
MRILKRFLAC IQLLCVCRLD WANGYYRQQR KLVEEIGWSY TGALNQKNWG KKYPTCNSPK 

        70         80         90        100        110        120 
QSPINIDEDL TQVNVNLKKL KFQGWDKTSL ENTFIHNTGK TVEINLTNDY RVSGGVSEMV 

       130        140        150        160        170        180 
FKASKITFHW GKCNMSSDGS EHSLEGQKFP LEMQIYCFDA DRFSSFEEAV KGKGKLRALS 

       190        200        210        220        230        240 
ILFEVGTEEN LDFKAIIDGV ESVSRFGKQA ALDPFILLNL LPNSTDKYYI YNGSLTSPPC 

       250        260        270        280        290        300 
TDTVDWIVFK DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY 

       310        320        330        340        350        360 
TGKEEIHEAV CSSEPENVQA DPENYTSLLV TWERPRVVYD TMIEKFAVLY QQLDGEDQTK 

       370        380        390        400        410        420 
HEFLTDGYQD LGAILNNLLP NMSYVLQIVA ICTNGLYGKY SDQLIVDMPT DNPELDLFPE 

       430        440        450        460        470        480 
LIGTEEIIKE EEEGKDIEEG AIVNPGRDSA TNQIRKKEPQ ISTTTHYNRI GTKYNEAKTN 

       490        500        510        520        530        540 
RSPTRGSEFS GKGDVPNTSL NSTSQPVTKL ATEKDISLTS QTVTELPPHT VEGTSASLND 

       550        560        570        580        590        600 
GSKTVLRSPH MNLSGTAESL NTVSITEYEE ESLLTSFKLD TGAEDSSGSS PATSAIPFIS 

       610        620        630        640        650        660 
ENISQGYIFS SENPETITYD VLIPESARNA SEDSTSSGSE ESLKDPSMEG NVWFPSSTDI 

       670        680        690        700        710        720 
TAQPDVGSGR ESFLQTNYTE IRVDESEKTT KSFSAGPVMS QGPSVTDLEM PHYSTFAYFP 

       730        740        750        760        770        780 
TEVTPHAFTP SSRQQDLVST VNVVYSQTTQ PVYNGETPLQ PSYSSEVFPL VTPLLLDNQI 

       790        800        810        820        830        840 
LNTTPAASSS DSALHATPVF PSVDVSFESI LSSYDGAPLL PFSSASFSSE LFRHLHTVSQ 

       850        860        870        880        890        900 
ILPQVTSATE SDKVPLHASL PVAGGDLLLE PSLAQYSDVL STTHAASETL EFGSESGVLY 

       910        920        930        940        950        960 
KTLMFSQVEP PSSDAMMHAR SSGPEPSYAL SDNEGSQHIF TVSYSSAIPV HDSVGVTYQG 

       970        980        990       1000       1010       1020 
SLFSGPSHIP IPKSSLITPT ASLLQPTHAL SGDGEWSGAS SDSEFLLPDT DGLTALNISS 

      1030       1040       1050       1060       1070       1080 
PVSVAEFTYT TSVFGDDNKA LSKSEIIYGN ETELQIPSFN EMVYPSESTV MPNMYDNVNK 

      1090       1100       1110       1120       1130       1140 
LNASLQETSV SISSTKGMFP GSLAHTTTKV FDHEISQVPE NNFSVQPTHT VSQASGDTSL 

      1150       1160       1170       1180       1190       1200 
KPVLSANSEP ASSDPASSEM LSPSTQLLFY ETSASFSTEV LLQPSFQASD VDTLLKTVLP 

      1210       1220       1230       1240       1250       1260 
AVPSDPILVE TPKVDKISST MLHLIVSNSA SSENMLHSTS VPVFDVSPTS HMHSASLQGL 

      1270       1280       1290       1300       1310       1320 
TISYASEKYE PVLLKSESSH QVVPSLYSND ELFQTANLEI NQAHPPKGRH VFATPVLSID 

      1330       1340       1350       1360       1370       1380 
EPLNTLINKL IHSDEILTST KSSVTGKVFA GIPTVASDTF VSTDHSVPIG NGHVAITAVS 

      1390       1400       1410       1420       1430       1440 
PHRDGSVTST KLLFPSKATS ELSHSAKSDA GLVGGGEDGD TDDDGDDDDD DRGSDGLSIH 

      1450       1460       1470       1480       1490       1500 
KCMSCSSYRE SQEKVMNDSD THENSLMDQN NPISYSLSEN SEEDNRVTSV SSDSQTGMDR 

      1510       1520       1530       1540       1550       1560 
SPGKSPSANG LSQKHNDGKE ENDIQTGSAL LPLSPESKAW AVLTSDEESG SGQGTSDSLN 

      1570       1580       1590       1600       1610       1620 
ENETSTDFSF ADTNEKDADG ILAAGDSEIT PGFPQSPTSS VTSENSEVFH VSEAEASNSS 

      1630       1640       1650       1660       1670       1680 
HESRIGLAEG LESEKKAVIP LVIVSALTFI CLVVLVGILI YWRKCFQTAH FYLEDSTSPR 

      1690       1700       1710       1720       1730       1740 
VISTPPTPIF PISDDVGAIP IKHFPKHVAD LHASSGFTEE FETLKEFYQE VQSCTVDLGI 

      1750       1760       1770       1780       1790       1800 
TADSSNHPDN KHKNRYINIV AYDHSRVKLA QLAEKDGKLT DYINANYVDG YNRPKAYIAA 

      1810       1820       1830       1840       1850       1860 
QGPLKSTAED FWRMIWEHNV EVIVMITNLV EKGRRKCDQY WPADGSEEYG NFLVTQKSVQ 

      1870       1880       1890       1900       1910       1920 
VLAYYTVRNF TLRNTKIKKG SQKGRPSGRV VTQYHYTQWP DMGVPEYSLP VLTFVRKAAY 

      1930       1940       1950       1960       1970       1980 
AKRHAVGPVV VHCSAGVGRT GTYIVLDSML QQIQHEGTVN IFGFLKHIRS QRNYLVQTEE 

      1990       2000       2010       2020       2030       2040 
QYVFIHDTLV EAILSKETEV LDSHIHAYVN ALLIPGPAGK TKLEKQFQLL SQSNIQQSDY 

      2050       2060       2070       2080       2090       2100 
SAALKQCNRE KNRTSSIIPV ERSRVGISSL SGEGTDYINA SYIMGYYQSN EFIITQHPLL 

      2110       2120       2130       2140       2150       2160 
HTIKDFWRMI WDHNAQLVVM IPDGQNMAED EFVYWPNKDE PINCESFKVT LMAEEHKCLS 

      2170       2180       2190       2200       2210       2220 
NEEKLIIQDF ILEATQDDYV LEVRHFQCPK WPNPDSPISK TFELISVIKE EAANRDGPMI 

      2230       2240       2250       2260       2270       2280 
VHDEHGGVTA GTFCALTTLM HQLEKENSVD VYQVAKMINL MRPGVFADIE QYQFLYKVIL 

      2290       2300       2310 
SLVSTRQEEN PSTSLDSNGA ALPDGNIAES LESLV 

« Hide

Isoform 2 [UniParc].

Checksum: B18D669E478E9239
Show »

FASTA2,308253,677
Isoform 3 [UniParc].

Checksum: 07434438564290C4
Show »

FASTA1,448162,663

References

« Hide 'large scale' references
[1]"A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases."
Krueger N.X., Saito H.
Proc. Natl. Acad. Sci. U.S.A. 89:7417-7421(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-1433.
Tissue: Brain.
[2]"The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system."
Levy J.B., Canoll P.D., Silvennoinen O., Barnea G., Morse B., Honegger A.M., Huang J.-T., Cannizzaro L.A., Park S.-H., Druck T., Huebner K., Sap J., Ehrlich M., Musacchio J.M., Schlessinger J.
J. Biol. Chem. 268:10573-10581(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tissue: Brain stem.
[3]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-1433.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-1433.
[6]"Molecular cloning and expression analysis of five novel genes in chromosome 1p36."
Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.
Genomics 50:187-198(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-999 (ISOFORM 1), TISSUE SPECIFICITY.
[7]"Structural diversity and evolution of human receptor-like protein tyrosine phosphatases."
Krueger N.X., Streuli M., Saito H.
EMBO J. 9:3241-3252(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1480-2092 (ISOFORM 1).
Tissue: Liver.
[8]"Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain."
Kaplan R., Morse B., Huebner K., Croce C., Howk R., Ravera M., Ricca G., Jaye M., Schlessinger J.
Proc. Natl. Acad. Sci. U.S.A. 87:7000-7004(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1750-1991 AND 2048-2281 (ISOFORM 1).
Tissue: Brain stem.
[9]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
Tissue: Plasma.
[10]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2055, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules."
Bouyain S., Watkins D.J.
Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-302, INTERACTION WITH CNTN1, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93426 mRNA. Translation: AAA60225.1.
AC006020 Genomic DNA. Translation: AAF03527.1.
AC006353 Genomic DNA. No translation available.
AC073095 Genomic DNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24344.1.
CH471070 Genomic DNA. Translation: EAW83561.1.
U88967 mRNA. Translation: AAC39934.1. Sequence problems.
X54135 mRNA. Translation: CAA38070.1.
CCDSCCDS34740.1. [P23471-1]
PIRA46151.
RefSeqNP_001193767.1. NM_001206838.1.
NP_001193768.1. NM_001206839.1. [P23471-3]
NP_002842.2. NM_002851.2. [P23471-1]
XP_005250576.1. XM_005250519.1. [P23471-2]
UniGeneHs.489824.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3JXFX-ray2.00A/B34-302[»]
3S97X-ray2.30A/B34-302[»]
ProteinModelPortalP23471.
SMRP23471. Positions 34-301, 313-409, 1698-2284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111767. 8 interactions.
DIPDIP-42063N.
IntActP23471. 9 interactions.
MINTMINT-1350337.
STRING9606.ENSP00000377047.

PTM databases

PhosphoSiteP23471.

Polymorphism databases

DMDM229485537.

Proteomic databases

PaxDbP23471.
PRIDEP23471.

Protocols and materials databases

DNASU5803.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393386; ENSP00000377047; ENSG00000106278. [P23471-1]
ENST00000449182; ENSP00000410000; ENSG00000106278.
GeneID5803.
KEGGhsa:5803.
UCSCuc003vjy.3. human. [P23471-1]

Organism-specific databases

CTD5803.
GeneCardsGC07P121513.
HGNCHGNC:9685. PTPRZ1.
HPACAB025106.
HPA015103.
MIM176891. gene.
604008. gene.
neXtProtNX_P23471.
PharmGKBPA34029.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000090262.
HOVERGENHBG053760.
InParanoidP23471.
KOK08114.
OMAVMNDSDT.
OrthoDBEOG7K6PT4.
PhylomeDBP23471.
TreeFamTF351978.

Enzyme and pathway databases

SignaLinkP23471.

Gene expression databases

ArrayExpressP23471.
BgeeP23471.
CleanExHS_PTPRZ1.
GenevestigatorP23471.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.10.200.10. 1 hit.
3.90.190.10. 2 hits.
InterProIPR001148. 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]
PfamPF00194. Carb_anhydrase. 1 hit.
PF00041. fn3. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM01057. Carb_anhydrase. 1 hit.
SM00060. FN3. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF51069. SSF51069. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEPS51144. 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]
ProtoNetSearch...

Other

ChiTaRSPTPRZ1. human.
EvolutionaryTraceP23471.
GeneWikiPTPRZ1.
GenomeRNAi5803.
NextBio22622.
PROP23471.
SOURCESearch...

Entry information

Entry namePTPRZ_HUMAN
AccessionPrimary (citable) accession number: P23471
Secondary accession number(s): A4D0W5 expand/collapse secondary AC list , C9JFM0, O76043, Q9UDR6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: March 24, 2009
Last modified: July 9, 2014
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM