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Q9UMZ3 (PTPRQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol phosphatase PTPRQ

EC=3.1.3.-
Alternative name(s):
Receptor-type tyrosine-protein phosphatase Q
Short name=PTP-RQ
Short name=R-PTP-Q
EC=3.1.3.48
Gene names
Name:PTPRQ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphatidylinositol phosphatase required for auditory function. May act by regulating the level of phosphatidylinositol 4,5-bisphosphate (PIP2) level in the basal region of hair bundles. Can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates. Phosphate can be hydrolyzed from the D3 and D5 positions in the inositol ring. Has low tyrosine-protein phosphatase activity; however, the relevance of such activity in vivo is unclear. Plays an important role in adipogenesis of mesenchymal stem cells (MSCs). Regulates the phosphorylation state of AKT1 by suppressing the phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCs and preadipocyte cells. Ref.4

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Membrane; Single-pass type I membrane protein Ref.3.

Tissue specificity

In developing kidney, it localizes to the basal membrane of podocytes, beginning when podocyte progenitors can first be identified in the embryonic kidney (at protein level). Expressed in lung and kidney. Ref.3 Ref.5

Developmental stage

Expressed at highest levels in fetal kidney, followed by fetal lung and fetal cochlea. Ref.5

Induction

Down-regulated during adipogenesis of mesenchymal stem cells. Ref.4

Involvement in disease

Deafness, autosomal recessive, 84A (DFNB84A) [MIM:613391]: A form of non-syndromic deafness characterized by progressive, sensorineural hearing loss and vestibular dysfunction.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.6

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily.

Contains 18 fibronectin type-III domains.

Contains 1 tyrosine-protein phosphatase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 23322297Phosphatidylinositol phosphatase PTPRQ
PRO_0000302850

Regions

Topological domain36 – 19471912Extracellular Potential
Transmembrane1948 – 196821Helical; Potential
Topological domain1969 – 2332364Cytoplasmic Potential
Domain36 – 9964Fibronectin type-III 1
Domain100 – 19596Fibronectin type-III 2
Domain199 – 29496Fibronectin type-III 3
Domain350 – 43889Fibronectin type-III 4
Domain441 – 53999Fibronectin type-III 5
Domain514 – 60693Fibronectin type-III 6
Domain610 – 70596Fibronectin type-III 7
Domain710 – 79990Fibronectin type-III 8
Domain804 – 89491Fibronectin type-III 9
Domain899 – 98890Fibronectin type-III 10
Domain993 – 1093101Fibronectin type-III 11
Domain1098 – 119093Fibronectin type-III 12
Domain1192 – 128291Fibronectin type-III 13
Domain1287 – 138094Fibronectin type-III 14
Domain1384 – 147087Fibronectin type-III 15
Domain1474 – 1578105Fibronectin type-III 16
Domain1583 – 168199Fibronectin type-III 17
Domain1686 – 1787102Fibronectin type-III 18
Domain2036 – 2292257Tyrosine-protein phosphatase

Sites

Active site22331Phosphocysteine intermediate By similarity

Amino acid modifications

Glycosylation181N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation3941N-linked (GlcNAc...) Potential
Glycosylation9441N-linked (GlcNAc...) Potential
Glycosylation10381N-linked (GlcNAc...) Potential
Glycosylation10801N-linked (GlcNAc...) Potential
Glycosylation11011N-linked (GlcNAc...) Potential
Glycosylation12901N-linked (GlcNAc...) Potential
Glycosylation12951N-linked (GlcNAc...) Potential
Glycosylation18441N-linked (GlcNAc...) Potential

Natural variations

Natural variant2811R → G in DFNB84A. Ref.5
VAR_063526
Natural variant4711Q → E. Ref.6
Corresponds to variant rs61729287 [ dbSNP | Ensembl ].
VAR_069041
Natural variant10401T → I.
Corresponds to variant rs12316867 [ dbSNP | Ensembl ].
VAR_034970
Natural variant10981F → L.
Corresponds to variant rs6539524 [ dbSNP | Ensembl ].
VAR_034971
Natural variant11201A → P.
Corresponds to variant rs7975340 [ dbSNP | Ensembl ].
VAR_034972
Natural variant12441N → D.
Corresponds to variant rs17713202 [ dbSNP | Ensembl ].
VAR_034973
Natural variant17341I → T.
Corresponds to variant rs7963963 [ dbSNP | Ensembl ].
VAR_034974
Natural variant21211R → K.
Corresponds to variant rs1163042 [ dbSNP | Ensembl ].
VAR_034975

Secondary structure

.............................................. 2332
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UMZ3 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: 999D87AA00BA04C2

FASTA2,332260,924
        10         20         30         40         50         60 
MKKVPIKPEQ PEKLRAFNIS THSFSLHWSL PSGHVERYQV DLVPDSGFVT IRDLGGGEYQ 

        70         80         90        100        110        120 
VDVSNVVPGT RYDITISSIS TTYTSPVTRI VTTNVTKPGP PVFLAGERVG SAGILLSWNT 

       130        140        150        160        170        180 
PPNPNGRIIS YIVKYKEVCP WMQTVYTQVR SKPDSLEVLL TNLNPGTTYE IKVAAENSAG 

       190        200        210        220        230        240 
IGVFSDPFLF QTAESAPGKV VNLTVEAYNA SAVKLIWYLP RQPNGKITSF KISVKHARSG 

       250        260        270        280        290        300 
IVVKDVSIRV EDILTGKLPE CNENSESFLW STASPSPTLG RVTPPSRTTH SSSTLTQNEI 

       310        320        330        340        350        360 
SSVWKEPISF VVTHLRPYTT YLFEVSAVTT EAGYIDSTIV RTPESVPEGP PQNCVTGNIT 

       370        380        390        400        410        420 
GKSFSILWDP PTIVTGKFSY RVELYGPSGR ILDNSTKDLK FAFTNLTPFT MYDVYIAAET 

       430        440        450        460        470        480 
SAGTGPKSNI SVFTPPDVPG AVFDLQLAEV ESTQVRITWK KPRQPNGIIN QYRVKVLVPE 

       490        500        510        520        530        540 
TGIILENTLL TGNNEYINDP MAPEIVNIVE PMVGLYEGSA EMSSDLHSLA TFIYNSHPDK 

       550        560        570        580        590        600 
NFPARNRAED QTSPVVTTRN QYITDIAAEQ LSYVIRRLVP FTEHMISVSA FTIMGEGPPT 

       610        620        630        640        650        660 
VLSVRTRQQV PSSIKIINYK NISSSSILLY WDPPEYPNGK ITHYTIYAME LDTNRAFQIT 

       670        680        690        700        710        720 
TIDNSFLITG LKKYTKYKMR VAASTHVGES SLSEENDIFV RTSEDEPESS PQDVEVIDVT 

       730        740        750        760        770        780 
ADEIRLKWSP PEKPNGIIIA YEVLYKNIDT LYMKNTSTTD IILRNLRPHT LYNISVRSYT 

       790        800        810        820        830        840 
RFGHGNQVSS LLSVRTSETV PDSAPENITY KNISSGEIEL SFLPPSSPNG IIKKYTIYLK 

       850        860        870        880        890        900 
RSNGNEERTI NTTSLTQNIK VLKKYTQYII EVSASTLKGE GVRSAPISIL TEEDAPDSPP 

       910        920        930        940        950        960 
QDFSVKQLSG VTVKLSWQPP LEPNGIILYY TVYVWNRSSL KTINVTETSL ELSDLDYNVE 

       970        980        990       1000       1010       1020 
YSAYVTASTR FGDGKTRSNI ISFQTPEGAP SDPPKDVYYA NLSSSSIILF WTPPSKPNGI 

      1030       1040       1050       1060       1070       1080 
IQYYSVYYRN TSGTFMQNFT LHEVTNDFDN MTVSTIIDKL TIFSYYTFWL TASTSVGNGN 

      1090       1100       1110       1120       1130       1140 
KSSDIIEVYT DQDIPEGFVG NLTYESISST AINVSWVPPA QPNGLVFYYV SLILQQTPRH 

      1150       1160       1170       1180       1190       1200 
VRPPLVTYER SIYFDNLEKY TDYILKITPS TEKGFSDTYT AQLYIKTEED VPETSPIINT 

      1210       1220       1230       1240       1250       1260 
FKNLSSTSVL LSWDPPVKPN GAIISYDLTL QGPNENYSFI TSDNYIILEE LSPFTLYSFF 

      1270       1280       1290       1300       1310       1320 
AAARTRKGLG PSSILFFYTD ESVPLAPPQN LTLINCTSDF VWLKWSPSPL PGGIVKVYSF 

      1330       1340       1350       1360       1370       1380 
KIHEHETDTI YYKNISGFKT EAKLVGLEPV STYSIRVSAF TKVGNGNQFS NVVKFTTQES 

      1390       1400       1410       1420       1430       1440 
VPDVVQNMQC MATSWQSVLV KWDPPKKANG IITQYMVTVE RNSTKVSPQD HMYTFIKLLA 

      1450       1460       1470       1480       1490       1500 
NTSYVFKVRA STSAGEGDES TCHVSTLPET VPSVPTNIAF SDVQSTSATL TWIRPDTILG 

      1510       1520       1530       1540       1550       1560 
YFQNYKITTQ LRAQKCKEWE SEECVEYQKI QYLYEAHLTE ETVYGLKKFR WYRFQVAAST 

      1570       1580       1590       1600       1610       1620 
NAGYGNASNW ISTKTLPGPP DGPPENVHVV ATSPFSISIS WSEPAVITGP TCYLIDVKSV 

      1630       1640       1650       1660       1670       1680 
DNDEFNISFI KSNEENKTIE IKDLEIFTRY SVVITAFTGN ISAAYVEGKS SAEMIVTTLE 

      1690       1700       1710       1720       1730       1740 
SAPKDPPNNM TFQKIPDEVT KFQLTFLPPS QPNGNIQVYQ ALVYREDDPT AVQIHNLSII 

      1750       1760       1770       1780       1790       1800 
QKTNTFVIAM LEGLKGGHTY NISVYAVNSA GAGPKVPMRI TMDIKAPARP KTKPTPIYDA 

      1810       1820       1830       1840       1850       1860 
TGKLLVTSTT ITIRMPICYY SDDHGPIKNV QVLVTETGAQ HDGNVTKWYD AYFNKARPYF 

      1870       1880       1890       1900       1910       1920 
TNEGFPNPPC TEGKTKFSGN EEIYIIGADN ACMIPGNEDK ICNGPLKPKK QYLFKFRATN 

      1930       1940       1950       1960       1970       1980 
IMGQFTDSDY SDPVKTLGEG LSERTVEIIL SVTLCILSII LLGTAIFAFA RIRQKQKEGG 

      1990       2000       2010       2020       2030       2040 
TYSPQDAEII DTKLKLDQLI TVADLELKDE RLTRPISKKS FLQHVEELCT NNNLKFQEEF 

      2050       2060       2070       2080       2090       2100 
SELPKFLQDL SSTDADLPWN RAKNRFPNIK PYNNNRVKLI ADASVPGSDY INASYISGYL 

      2110       2120       2130       2140       2150       2160 
CPNEFIATQG PLPGTVGDFW RMVWETRAKT LVMLTQCFEK GRIRCHQYWP EDNKPVTVFG 

      2170       2180       2190       2200       2210       2220 
DIVITKLMED VQIDWTIRDL KIERHGDCMT VRQCNFTAWP EHGVPENSAP LIHFVKLVRA 

      2230       2240       2250       2260       2270       2280 
SRAHDTTPMI VHCSAGVGRT GVFIALDHLT QHINDHDFVD IYGLVAELRS ERMCMVQNLA 

      2290       2300       2310       2320       2330 
QYIFLHQCIL DLLSNKGSNQ PICFVNYSAL QKMDSLDAME GDVELEWEET TM 

« Hide

References

« Hide 'large scale' references
[1]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Differential expression of PTPase RNAs resulting from K562 differentiation induced by PMA."
Dayton M.A., Blanchard K.L.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2133-2266.
[3]"PTPRQ is a novel phosphatidylinositol phosphatase that can be expressed as a cytoplasmic protein or as a subcellularly localized receptor-like protein."
Seifert R.A., Coats S.A., Oganesian A., Wright M.B., Dishmon M., Booth C.J., Johnson R.J., Alpers C.E., Bowen-Pope D.F.
Exp. Cell Res. 287:374-386(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Involvement of PTP-RQ in differentiation during adipogenesis of human mesenchymal stem cells."
Jung H., Kim W.K., Kim do H., Cho Y.S., Kim S.J., Park S.G., Park B.C., Lim H.M., Bae K.H., Lee S.C.
Biochem. Biophys. Res. Commun. 383:252-257(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[5]"Mutations in PTPRQ are a cause of autosomal-recessive nonsyndromic hearing impairment DFNB84 and associated with vestibular dysfunction."
Schraders M., Oostrik J., Huygen P.L., Strom T.M., van Wijk E., Kunst H.P., Hoefsloot L.H., Cremers C.W., Admiraal R.J., Kremer H.
Am. J. Hum. Genet. 86:604-610(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANT DFNB84A GLY-281.
[6]"Nonsense mutation of the stereociliar membrane protein gene PTPRQ in human hearing loss DFNB84."
Shahin H., Rahil M., Abu Rayan A., Avraham K.B., King M.C., Kanaan M., Walsh T.
J. Med. Genet. 47:643-645(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DFNB84A, VARIANT GLU-471.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC083812 Genomic DNA. No translation available.
AC074031 Genomic DNA. No translation available.
AF169351 mRNA. Translation: AAD50277.1.
UniGeneHs.539284.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IKCX-ray1.56A2015-2293[»]
ProteinModelPortalQ9UMZ3.
SMRQ9UMZ3. Positions 11-232, 309-474, 572-1460, 1472-1576, 1583-1659, 1701-1776, 1988-2328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000393751.

PTM databases

PhosphoSiteQ9UMZ3.

Polymorphism databases

DMDM158563998.

Proteomic databases

PaxDbQ9UMZ3.
PRIDEQ9UMZ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266688; ENSP00000266688; ENSG00000139304.
UCSCuc001sze.2. human.

Organism-specific databases

GeneCardsGC12P080837.
H-InvDBHIX0201920.
HGNCHGNC:9679. PTPRQ.
HPAHPA053245.
MIM603317. gene.
613391. phenotype.
neXtProtNX_Q9UMZ3.
Orphanet90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000115793.
HOVERGENHBG108308.
InParanoidQ9UMZ3.
PhylomeDBQ9UMZ3.
TreeFamTF351926.

Gene expression databases

BgeeQ9UMZ3.
CleanExHS_PTPRQ.
GenevestigatorQ9UMZ3.

Family and domain databases

Gene3D2.60.40.10. 19 hits.
3.90.190.10. 1 hit.
InterProIPR003961. 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]
PfamPF00041. fn3. 14 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 17 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 11 hits.
SSF52799. SSF52799. 1 hit.
PROSITEPS50853. FN3. 17 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9UMZ3.
SOURCESearch...

Entry information

Entry namePTPRQ_HUMAN
AccessionPrimary (citable) accession number: Q9UMZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: June 11, 2014
This is version 92 of the entry and version 2 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 12

Human chromosome 12: entries, gene names and cross-references to MIM