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Protein

Receptor-type tyrosine-protein phosphatase zeta

Gene

PTPRZ1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei1901SubstrateBy similarity1
Active sitei1933Phosphocysteine intermediatePROSITE-ProRule annotation1
Binding sitei1977SubstrateBy similarity1
Sitei2223Ancestral active site1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciZFISH:HS11250-MONOMER.
BRENDAi3.1.3.48. 2681.
SignaLinkiP23471.
SIGNORiP23471.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase zeta (EC:3.1.3.48By similarity)
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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9685. PTPRZ1.

Subcellular locationi

Isoform 1 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 1636ExtracellularSequence analysisAdd BLAST1612
Transmembranei1637 – 1662HelicalSequence analysisAdd BLAST26
Topological domaini1663 – 2315CytoplasmicSequence analysisAdd BLAST653

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi5803.
MalaCardsiPTPRZ1.
OpenTargetsiENSG00000106278.
PharmGKBiPA34029.

Polymorphism and mutation databases

BioMutaiPTPRZ1.
DMDMi229485537.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24By similarityAdd BLAST24
ChainiPRO_000002546825 – 2315Receptor-type tyrosine-protein phosphatase zetaAdd BLAST2291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi56 ↔ 2401 Publication
Glycosylationi105N-linked (GlcNAc...)1 Publication1
Disulfide bondi133 ↔ 2641 Publication
Glycosylationi134N-linked (GlcNAc...)Sequence analysis1
Glycosylationi223N-linked (GlcNAc...)Sequence analysis1
Glycosylationi232N-linked (GlcNAc...)Sequence analysis1
Glycosylationi324N-linked (GlcNAc...)Sequence analysis1
Glycosylationi381N-linked (GlcNAc...)Sequence analysis1
Glycosylationi497N-linked (GlcNAc...)Sequence analysis1
Glycosylationi501N-linked (GlcNAc...)Sequence analysis1
Glycosylationi552N-linked (GlcNAc...)Sequence analysis1
Glycosylationi587O-linked (Xyl...) (chondroitin sulfate)Sequence analysis1
Glycosylationi602N-linked (GlcNAc...)Sequence analysis1
Glycosylationi629N-linked (GlcNAc...)Sequence analysis1
Modified residuei637Phosphoserine; alternateBy similarity1
Glycosylationi637O-linked (Xyl...) (chondroitin sulfate); alternateSequence analysis1
Modified residuei639PhosphoserineBy similarity1
Glycosylationi677N-linked (GlcNAc...)Sequence analysis1
Glycosylationi997O-linked (Xyl...) (chondroitin sulfate)Sequence analysis1
Glycosylationi1017N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1050N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1082N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1122N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1457N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1549O-linked (Xyl...) (chondroitin sulfate)Sequence analysis1
Glycosylationi1551O-linked (Xyl...) (chondroitin sulfate)Sequence analysis1
Glycosylationi1562N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1618N-linked (GlcNAc...)Sequence analysis1
Modified residuei1684PhosphothreonineBy similarity1
Modified residuei1687PhosphothreonineBy similarity1
Modified residuei2055PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP23471.
PaxDbiP23471.
PeptideAtlasiP23471.
PRIDEiP23471.

PTM databases

DEPODiP23471.
iPTMnetiP23471.
PhosphoSitePlusiP23471.

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

BgeeiENSG00000106278.
CleanExiHS_PTPRZ1.
GenevisibleiP23471. HS.

Organism-specific databases

HPAiCAB025106.
HPA015103.

Interactioni

Subunit structurei

The carbonic-anhydrase like domain interacts with CNTN1 (contactin) (PubMed:20133774). Interacts with PTN (PubMed:16814777). Interaction with PTN promotes formation of homooligomers; oligomerization impairs phosphatase activity (By similarity).By similarity2 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

12315
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 42Combined sources3
Helixi46 – 48Combined sources3
Helixi49 – 52Combined sources4
Helixi54 – 57Combined sources4
Beta strandi58 – 60Combined sources3
Helixi68 – 70Combined sources3
Beta strandi71 – 73Combined sources3
Beta strandi78 – 84Combined sources7
Beta strandi94 – 97Combined sources4
Beta strandi102 – 105Combined sources4
Beta strandi111 – 116Combined sources6
Beta strandi121 – 134Combined sources14
Beta strandi141 – 144Combined sources4
Beta strandi150 – 158Combined sources9
Turni160 – 162Combined sources3
Helixi166 – 171Combined sources6
Beta strandi176 – 185Combined sources10
Helixi191 – 193Combined sources3
Helixi194 – 202Combined sources9
Beta strandi209 – 211Combined sources3
Helixi217 – 220Combined sources4
Beta strandi226 – 233Combined sources8
Beta strandi244 – 251Combined sources8
Beta strandi253 – 255Combined sources3
Helixi257 – 261Combined sources5
Helixi262 – 265Combined sources4
Beta strandi267 – 272Combined sources6
Beta strandi275 – 280Combined sources6
Helixi1701 – 1703Combined sources3
Helixi1704 – 1713Combined sources10
Turni1714 – 1716Combined sources3
Helixi1717 – 1722Combined sources6
Helixi1730 – 1733Combined sources4
Turni1734 – 1737Combined sources4
Turni1743 – 1746Combined sources4
Helixi1748 – 1753Combined sources6
Turni1763 – 1765Combined sources3
Beta strandi1766 – 1768Combined sources3
Beta strandi1781 – 1790Combined sources10
Beta strandi1793 – 1800Combined sources8
Helixi1805 – 1807Combined sources3
Helixi1808 – 1817Combined sources10
Beta strandi1822 – 1825Combined sources4
Beta strandi1829 – 1831Combined sources3
Beta strandi1843 – 1849Combined sources7
Beta strandi1852 – 1861Combined sources10
Beta strandi1863 – 1874Combined sources12
Beta strandi1889 – 1896Combined sources8
Beta strandi1901 – 1903Combined sources3
Helixi1908 – 1921Combined sources14
Turni1922 – 1924Combined sources3
Beta strandi1929 – 1932Combined sources4
Beta strandi1934 – 1937Combined sources4
Helixi1938 – 1956Combined sources19
Beta strandi1957 – 1959Combined sources3
Helixi1961 – 1968Combined sources8
Turni1969 – 1971Combined sources3
Helixi1979 – 1994Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JXFX-ray2.00A/B34-302[»]
3S97X-ray2.30A/B34-302[»]
5AWXX-ray1.86A1698-2000[»]
ProteinModelPortaliP23471.
SMRiP23471.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23471.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 300Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST265
Domaini314 – 413Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST100
Domaini1717 – 1992Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd BLAST276
Domaini2023 – 2282Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd BLAST260

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1933 – 1939Substrate bindingBy similarity7

Sequence similaritiesi

Contains 1 alpha-carbonic anhydrase domain.PROSITE-ProRule annotation
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

eggNOGiKOG4228. Eukaryota.
COG3338. LUCA.
COG5599. LUCA.
GeneTreeiENSGT00760000118900.
HOGENOMiHOG000231465.
HOVERGENiHBG053760.
InParanoidiP23471.
KOiK08114.
OMAiVVSHQTT.
OrthoDBiEOG091G018S.
PhylomeDBiP23471.
TreeFamiTF351978.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 1 hit.
3.10.200.10. 1 hit.
3.90.190.10. 2 hits.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[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.
SM00404. PTPc_motif. 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. AlignAdd to basket

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 differs from that shown. Contaminating sequence. The N-terminus may be contaminated with vector sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti310V → A in AAC39934 (PubMed:9653645).Curated1
Sequence conflicti312S → R in AAC39934 (PubMed:9653645).Curated1
Sequence conflicti1426Missing in AAA60225 (PubMed:1323835).Curated1
Sequence conflicti1426Missing (PubMed:8387522).Curated1
Sequence conflicti1426Missing in EAL24344 (PubMed:12690205).Curated1
Sequence conflicti1426Missing in EAW83561 (Ref. 5) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0389423I → S.Corresponds to variant rs740965dbSNPEnsembl.1
Natural variantiVAR_0389436R → L.Corresponds to variant rs11980387dbSNPEnsembl.1
Natural variantiVAR_0389441433G → D.3 PublicationsCorresponds to variant rs1147504dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054061755 – 1614Missing in isoform 3. 1 PublicationAdd BLAST860
Alternative sequenceiVSP_0540621723 – 1729Missing in isoform 2 and isoform 3. 1 Publication7

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [P23471-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JXFX-ray2.00A/B34-302[»]
3S97X-ray2.30A/B34-302[»]
5AWXX-ray1.86A1698-2000[»]
ProteinModelPortaliP23471.
SMRiP23471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

DEPODiP23471.
iPTMnetiP23471.
PhosphoSitePlusiP23471.

Polymorphism and mutation databases

BioMutaiPTPRZ1.
DMDMi229485537.

Proteomic databases

EPDiP23471.
PaxDbiP23471.
PeptideAtlasiP23471.
PRIDEiP23471.

Protocols and materials databases

DNASUi5803.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393386; ENSP00000377047; ENSG00000106278. [P23471-1]
ENST00000449182; ENSP00000410000; ENSG00000106278. [P23471-3]
GeneIDi5803.
KEGGihsa:5803.
UCSCiuc003vjy.4. human. [P23471-1]

Organism-specific databases

CTDi5803.
DisGeNETi5803.
GeneCardsiPTPRZ1.
HGNCiHGNC:9685. PTPRZ1.
HPAiCAB025106.
HPA015103.
MalaCardsiPTPRZ1.
MIMi176891. gene.
604008. gene.
neXtProtiNX_P23471.
OpenTargetsiENSG00000106278.
PharmGKBiPA34029.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4228. Eukaryota.
COG3338. LUCA.
COG5599. LUCA.
GeneTreeiENSGT00760000118900.
HOGENOMiHOG000231465.
HOVERGENiHBG053760.
InParanoidiP23471.
KOiK08114.
OMAiVVSHQTT.
OrthoDBiEOG091G018S.
PhylomeDBiP23471.
TreeFamiTF351978.

Enzyme and pathway databases

BioCyciZFISH:HS11250-MONOMER.
BRENDAi3.1.3.48. 2681.
SignaLinkiP23471.
SIGNORiP23471.

Miscellaneous databases

ChiTaRSiPTPRZ1. human.
EvolutionaryTraceiP23471.
GeneWikiiPTPRZ1.
GenomeRNAii5803.
PROiP23471.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106278.
CleanExiHS_PTPRZ1.
GenevisibleiP23471. HS.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 1 hit.
3.10.200.10. 1 hit.
3.90.190.10. 2 hits.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[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.
SM00404. PTPc_motif. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 187 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.