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P23471

- PTPRZ_HUMAN

UniProt

P23471 - PTPRZ_HUMAN

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Protein

Receptor-type tyrosine-protein phosphatase zeta

Gene

PTPRZ1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1901 – 19011SubstrateBy similarity
Active sitei1933 – 19331Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei1977 – 19771SubstrateBy similarity
Sitei2223 – 22231Ancestral active site

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: UniProtKB
  2. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  1. axonogenesis Source: Ensembl
  2. central nervous system development Source: ProtInc
  3. hematopoietic progenitor cell differentiation Source: Ensembl
  4. learning or memory Source: UniProtKB
  5. oligodendrocyte differentiation Source: UniProtKB
  6. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  7. protein dephosphorylation Source: ProtInc
  8. regulation of oligodendrocyte progenitor proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SignaLinkiP23471.

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):
Protein-tyrosine phosphatase receptor type Z polypeptide 1
Protein-tyrosine phosphatase receptor type Z polypeptide 2
R-PTP-zeta-2
Gene namesi
Name:PTPRZ1
Synonyms:HTPZP2, PTPRZ, PTPRZ2, PTPZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:9685. 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. integral component of plasma membrane Source: ProtInc
  2. perineuronal net Source: Ensembl
  3. proteinaceous extracellular matrix Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34029.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424By similarityAdd
BLAST
Chaini25 – 23152291Receptor-type tyrosine-protein phosphatase zetaPRO_0000025468Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 2401 Publication
Glycosylationi105 – 1051N-linked (GlcNAc...)1 Publication
Disulfide bondi133 ↔ 2641 Publication
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
Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi587 – 5871O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi602 – 6021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi629 – 6291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi637 – 6371O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi997 – 9971O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi1017 – 10171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1050 – 10501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1082 – 10821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1122 – 11221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1457 – 14571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1549 – 15491O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi1551 – 15511O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi1562 – 15621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1618 – 16181N-linked (GlcNAc...)Sequence Analysis
Modified residuei2055 – 20551Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP23471.
PRIDEiP23471.

PTM databases

PhosphoSiteiP23471.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiP23471.
CleanExiHS_PTPRZ1.
GenevestigatoriP23471.

Organism-specific databases

HPAiCAB025106.
HPA015103.

Interactioni

Subunit structurei

The carbonic-anhydrase like domain interacts with CNTN1 (contactin).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ALKQ9UM732EBI-2263175,EBI-357361

Protein-protein interaction databases

BioGridi111767. 9 interactions.
DIPiDIP-42063N.
IntActiP23471. 9 interactions.
MINTiMINT-1350337.
STRINGi9606.ENSP00000377047.

Structurei

Secondary structure

1
2315
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 423
Helixi46 – 483
Helixi49 – 524
Helixi54 – 574
Beta strandi58 – 603
Helixi68 – 703
Beta strandi71 – 733
Beta strandi78 – 847
Beta strandi94 – 974
Beta strandi102 – 1054
Beta strandi111 – 1166
Beta strandi121 – 13414
Beta strandi141 – 1444
Beta strandi150 – 1589
Turni160 – 1623
Helixi166 – 1716
Beta strandi176 – 18510
Helixi191 – 1933
Helixi194 – 2029
Beta strandi209 – 2113
Helixi217 – 2204
Beta strandi226 – 2338
Beta strandi244 – 2518
Beta strandi253 – 2553
Helixi257 – 2615
Helixi262 – 2654
Beta strandi267 – 2726
Beta strandi275 – 2806

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JXFX-ray2.00A/B34-302[»]
3S97X-ray2.30A/B34-302[»]
ProteinModelPortaliP23471.
SMRiP23471. Positions 34-301, 313-406, 1698-2284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23471.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 16361612ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1663 – 2315653CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1637 – 166226HelicalSequence 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
Domaini1717 – 1992276Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
BLAST
Domaini2023 – 2282260Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1933 – 19397Substrate bindingBy similarity

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.
GeneTreeiENSGT00760000118900.
HOGENOMiHOG000090262.
HOVERGENiHBG053760.
InParanoidiP23471.
KOiK08114.
OMAiVMNDSDT.
OrthoDBiEOG7K6PT4.
PhylomeDBiP23471.
TreeFamiTF351978.

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: P23471-1) [UniParc]FASTAAdd to Basket

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

        10         20         30         40         50
MRILKRFLAC IQLLCVCRLD WANGYYRQQR KLVEEIGWSY TGALNQKNWG
60 70 80 90 100
KKYPTCNSPK QSPINIDEDL TQVNVNLKKL KFQGWDKTSL ENTFIHNTGK
110 120 130 140 150
TVEINLTNDY RVSGGVSEMV FKASKITFHW GKCNMSSDGS EHSLEGQKFP
160 170 180 190 200
LEMQIYCFDA DRFSSFEEAV KGKGKLRALS ILFEVGTEEN LDFKAIIDGV
210 220 230 240 250
ESVSRFGKQA ALDPFILLNL LPNSTDKYYI YNGSLTSPPC TDTVDWIVFK
260 270 280 290 300
DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY
310 320 330 340 350
TGKEEIHEAV CSSEPENVQA DPENYTSLLV TWERPRVVYD TMIEKFAVLY
360 370 380 390 400
QQLDGEDQTK HEFLTDGYQD LGAILNNLLP NMSYVLQIVA ICTNGLYGKY
410 420 430 440 450
SDQLIVDMPT DNPELDLFPE LIGTEEIIKE EEEGKDIEEG AIVNPGRDSA
460 470 480 490 500
TNQIRKKEPQ ISTTTHYNRI GTKYNEAKTN RSPTRGSEFS GKGDVPNTSL
510 520 530 540 550
NSTSQPVTKL ATEKDISLTS QTVTELPPHT VEGTSASLND GSKTVLRSPH
560 570 580 590 600
MNLSGTAESL NTVSITEYEE ESLLTSFKLD TGAEDSSGSS PATSAIPFIS
610 620 630 640 650
ENISQGYIFS SENPETITYD VLIPESARNA SEDSTSSGSE ESLKDPSMEG
660 670 680 690 700
NVWFPSSTDI TAQPDVGSGR ESFLQTNYTE IRVDESEKTT KSFSAGPVMS
710 720 730 740 750
QGPSVTDLEM PHYSTFAYFP TEVTPHAFTP SSRQQDLVST VNVVYSQTTQ
760 770 780 790 800
PVYNGETPLQ PSYSSEVFPL VTPLLLDNQI LNTTPAASSS DSALHATPVF
810 820 830 840 850
PSVDVSFESI LSSYDGAPLL PFSSASFSSE LFRHLHTVSQ ILPQVTSATE
860 870 880 890 900
SDKVPLHASL PVAGGDLLLE PSLAQYSDVL STTHAASETL EFGSESGVLY
910 920 930 940 950
KTLMFSQVEP PSSDAMMHAR SSGPEPSYAL SDNEGSQHIF TVSYSSAIPV
960 970 980 990 1000
HDSVGVTYQG SLFSGPSHIP IPKSSLITPT ASLLQPTHAL SGDGEWSGAS
1010 1020 1030 1040 1050
SDSEFLLPDT DGLTALNISS PVSVAEFTYT TSVFGDDNKA LSKSEIIYGN
1060 1070 1080 1090 1100
ETELQIPSFN EMVYPSESTV MPNMYDNVNK LNASLQETSV SISSTKGMFP
1110 1120 1130 1140 1150
GSLAHTTTKV FDHEISQVPE NNFSVQPTHT VSQASGDTSL KPVLSANSEP
1160 1170 1180 1190 1200
ASSDPASSEM LSPSTQLLFY ETSASFSTEV LLQPSFQASD VDTLLKTVLP
1210 1220 1230 1240 1250
AVPSDPILVE TPKVDKISST MLHLIVSNSA SSENMLHSTS VPVFDVSPTS
1260 1270 1280 1290 1300
HMHSASLQGL TISYASEKYE PVLLKSESSH QVVPSLYSND ELFQTANLEI
1310 1320 1330 1340 1350
NQAHPPKGRH VFATPVLSID EPLNTLINKL IHSDEILTST KSSVTGKVFA
1360 1370 1380 1390 1400
GIPTVASDTF VSTDHSVPIG NGHVAITAVS PHRDGSVTST KLLFPSKATS
1410 1420 1430 1440 1450
ELSHSAKSDA GLVGGGEDGD TDDDGDDDDD DRGSDGLSIH KCMSCSSYRE
1460 1470 1480 1490 1500
SQEKVMNDSD THENSLMDQN NPISYSLSEN SEEDNRVTSV SSDSQTGMDR
1510 1520 1530 1540 1550
SPGKSPSANG LSQKHNDGKE ENDIQTGSAL LPLSPESKAW AVLTSDEESG
1560 1570 1580 1590 1600
SGQGTSDSLN ENETSTDFSF ADTNEKDADG ILAAGDSEIT PGFPQSPTSS
1610 1620 1630 1640 1650
VTSENSEVFH VSEAEASNSS HESRIGLAEG LESEKKAVIP LVIVSALTFI
1660 1670 1680 1690 1700
CLVVLVGILI YWRKCFQTAH FYLEDSTSPR VISTPPTPIF PISDDVGAIP
1710 1720 1730 1740 1750
IKHFPKHVAD LHASSGFTEE FETLKEFYQE VQSCTVDLGI TADSSNHPDN
1760 1770 1780 1790 1800
KHKNRYINIV AYDHSRVKLA QLAEKDGKLT DYINANYVDG YNRPKAYIAA
1810 1820 1830 1840 1850
QGPLKSTAED FWRMIWEHNV EVIVMITNLV EKGRRKCDQY WPADGSEEYG
1860 1870 1880 1890 1900
NFLVTQKSVQ VLAYYTVRNF TLRNTKIKKG SQKGRPSGRV VTQYHYTQWP
1910 1920 1930 1940 1950
DMGVPEYSLP VLTFVRKAAY AKRHAVGPVV VHCSAGVGRT GTYIVLDSML
1960 1970 1980 1990 2000
QQIQHEGTVN IFGFLKHIRS QRNYLVQTEE QYVFIHDTLV EAILSKETEV
2010 2020 2030 2040 2050
LDSHIHAYVN ALLIPGPAGK TKLEKQFQLL SQSNIQQSDY SAALKQCNRE
2060 2070 2080 2090 2100
KNRTSSIIPV ERSRVGISSL SGEGTDYINA SYIMGYYQSN EFIITQHPLL
2110 2120 2130 2140 2150
HTIKDFWRMI WDHNAQLVVM IPDGQNMAED EFVYWPNKDE PINCESFKVT
2160 2170 2180 2190 2200
LMAEEHKCLS NEEKLIIQDF ILEATQDDYV LEVRHFQCPK WPNPDSPISK
2210 2220 2230 2240 2250
TFELISVIKE EAANRDGPMI VHDEHGGVTA GTFCALTTLM HQLEKENSVD
2260 2270 2280 2290 2300
VYQVAKMINL MRPGVFADIE QYQFLYKVIL SLVSTRQEEN PSTSLDSNGA
2310
ALPDGNIAES LESLV
Length:2,315
Mass (Da):254,587
Last modified:March 24, 2009 - v4
Checksum:iED9DD98D4CCA2883
GO
Isoform 2 (identifier: P23471-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:2,308
Mass (Da):253,677
Checksum:iB18D669E478E9239
GO
Isoform 3 (identifier: P23471-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,448
Mass (Da):162,663
Checksum:i07434438564290C4
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti310 – 3101V → A in AAC39934. (PubMed:9653645)Curated
Sequence conflicti312 – 3121S → R in AAC39934. (PubMed:9653645)Curated
Sequence conflicti1426 – 14261Missing in AAA60225. (PubMed:1323835)Curated
Sequence conflicti1426 – 14261Missing(PubMed:8387522)Curated
Sequence conflicti1426 – 14261Missing in EAL24344. (PubMed:12690205)Curated
Sequence conflicti1426 – 14261Missing in EAW83561. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31I → S.
Corresponds to variant rs740965 [ dbSNP | Ensembl ].
VAR_038942
Natural varianti6 – 61R → L.
Corresponds to variant rs11980387 [ dbSNP | Ensembl ].
VAR_038943
Natural varianti1433 – 14331G → D.3 Publications
Corresponds to variant rs1147504 [ dbSNP | Ensembl ].
VAR_038944

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei755 – 1614860Missing in isoform 3. 1 PublicationVSP_054061Add
BLAST
Alternative sequencei1723 – 17297Missing in isoform 2 and isoform 3. 1 PublicationVSP_054062

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34740.1. [P23471-1]
CCDS56505.1. [P23471-3]
PIRiA46151.
RefSeqiNP_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]
UniGeneiHs.489824.

Genome annotation databases

EnsembliENST00000393386; ENSP00000377047; ENSG00000106278. [P23471-1]
ENST00000449182; ENSP00000410000; ENSG00000106278. [P23471-3]
GeneIDi5803.
KEGGihsa:5803.
UCSCiuc003vjy.3. human. [P23471-1]

Polymorphism databases

DMDMi229485537.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34740.1. [P23471-1 ]
CCDS56505.1. [P23471-3 ]
PIRi A46151.
RefSeqi NP_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 ]
UniGenei Hs.489824.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3JXF X-ray 2.00 A/B 34-302 [» ]
3S97 X-ray 2.30 A/B 34-302 [» ]
ProteinModelPortali P23471.
SMRi P23471. Positions 34-301, 313-406, 1698-2284.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111767. 9 interactions.
DIPi DIP-42063N.
IntActi P23471. 9 interactions.
MINTi MINT-1350337.
STRINGi 9606.ENSP00000377047.

PTM databases

PhosphoSitei P23471.

Polymorphism databases

DMDMi 229485537.

Proteomic databases

PaxDbi P23471.
PRIDEi P23471.

Protocols and materials databases

DNASUi 5803.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000393386 ; ENSP00000377047 ; ENSG00000106278 . [P23471-1 ]
ENST00000449182 ; ENSP00000410000 ; ENSG00000106278 . [P23471-3 ]
GeneIDi 5803.
KEGGi hsa:5803.
UCSCi uc003vjy.3. human. [P23471-1 ]

Organism-specific databases

CTDi 5803.
GeneCardsi GC07P121513.
HGNCi HGNC:9685. PTPRZ1.
HPAi CAB025106.
HPA015103.
MIMi 176891. gene.
604008. gene.
neXtProti NX_P23471.
PharmGKBi PA34029.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118900.
HOGENOMi HOG000090262.
HOVERGENi HBG053760.
InParanoidi P23471.
KOi K08114.
OMAi VMNDSDT.
OrthoDBi EOG7K6PT4.
PhylomeDBi P23471.
TreeFami TF351978.

Enzyme and pathway databases

SignaLinki P23471.

Miscellaneous databases

ChiTaRSi PTPRZ1. human.
EvolutionaryTracei P23471.
GeneWikii PTPRZ1.
GenomeRNAii 5803.
NextBioi 22622.
PROi P23471.
SOURCEi Search...

Gene expression databases

Bgeei P23471.
CleanExi HS_PTPRZ1.
Genevestigatori P23471.

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

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiPTPRZ_HUMAN
AccessioniPrimary (citable) accession number: P23471
Secondary accession number(s): A4D0W5
, C9JFM0, O76043, Q9UDR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: March 24, 2009
Last modified: October 29, 2014
This is version 166 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Was termed (PubMed:8387522 and PubMed:2170109) RPTPase beta.Curated
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.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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