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P28827 (PTPRM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. 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 mu

Short name=Protein-tyrosine phosphatase mu
Short name=R-PTP-mu
EC=3.1.3.48
Gene names
Name:PTPRM
Synonyms:PTPRL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control. Ref.8

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

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

Contains 4 fibronectin type-III domains.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 MAM domain.

Contains 2 tyrosine-protein phosphatase domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhomophilic cell adhesion

Inferred from direct assay PubMed 8393854. Source: UniProtKB

negative regulation of angiogenesis

Inferred from mutant phenotype PubMed 18566238. Source: UniProtKB

negative regulation of endothelial cell migration

Inferred from mutant phenotype PubMed 18566238. Source: UniProtKB

negative regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 18566238. Source: UniProtKB

neuron projection development

Inferred from direct assay PubMed 16380380. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from direct assay PubMed 10809770PubMed 17965016PubMed 18566238PubMed 8393854. Source: GOC

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Inferred from direct assay PubMed 10809770PubMed 8393854. Source: UniProtKB

response to drug

Inferred from direct assay PubMed 18566238. Source: UniProtKB

retina layer formation

Inferred from mutant phenotype PubMed 14623235. Source: UniProtKB

retinal ganglion cell axon guidance

Inferred from direct assay PubMed 15080886. Source: UniProtKB

signal transduction

Inferred from direct assay PubMed 15080886. Source: UniProtKB

   Cellular_componentcell-cell adherens junction

Inferred from direct assay PubMed 17965016. Source: UniProtKB

cell-cell junction

Inferred from direct assay PubMed 15491993PubMed 16380380. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 16380380. Source: UniProtKB

integral component of plasma membrane

Non-traceable author statement Ref.1. Source: UniProtKB

lamellipodium

Inferred from direct assay PubMed 15706045. Source: MGI

perinuclear region of cytoplasm

Inferred from direct assay PubMed 15491993. Source: UniProtKB

   Molecular_functioncadherin binding

Inferred from direct assay PubMed 9531566. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 10809770. Source: IntAct

protein binding

Inferred from physical interaction PubMed 11278757PubMed 16380380. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay PubMed 17965016PubMed 18566238PubMed 8393854. Source: UniProtKB

transmembrane receptor protein tyrosine phosphatase activity

Inferred from direct assay PubMed 10809770. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-2257317,EBI-2257317
Cdh1P098033EBI-2257317,EBI-984420From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28827-1)

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: P28827-2)

The sequence of this isoform differs from the canonical sequence as follows:
     842-842: P → PDPFVPTAILVPIN

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 14521432Receptor-type tyrosine-protein phosphatase mu
PRO_0000025448

Regions

Topological domain21 – 742722Extracellular Potential
Transmembrane743 – 76422Helical; Potential
Topological domain765 – 1452688Cytoplasmic Potential
Domain22 – 184163MAM
Domain186 – 27792Ig-like C2-type
Domain284 – 37996Fibronectin type-III 1
Domain382 – 48099Fibronectin type-III 2
Domain482 – 587106Fibronectin type-III 3
Domain589 – 67183Fibronectin type-III 4
Domain900 – 1154255Tyrosine-protein phosphatase 1
Domain1186 – 1448263Tyrosine-protein phosphatase 2
Region1095 – 11017Substrate binding By similarity

Sites

Active site10951Phosphocysteine intermediate By similarity
Active site13891Phosphocysteine intermediate By similarity
Binding site10631Substrate By similarity
Binding site11391Substrate By similarity

Amino acid modifications

Modified residue8211Phosphoserine Ref.6
Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1311N-linked (GlcNAc...) Ref.5
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Glycosylation4541N-linked (GlcNAc...) Potential
Glycosylation5341N-linked (GlcNAc...) Potential
Glycosylation5441N-linked (GlcNAc...) Potential
Glycosylation5981N-linked (GlcNAc...) Potential
Glycosylation6511N-linked (GlcNAc...) Potential
Glycosylation6811N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 36 Ref.8
Disulfide bond96 ↔ 182 Ref.8
Disulfide bond206 ↔ 260 Ref.8

Natural variations

Alternative sequence8421P → PDPFVPTAILVPIN in isoform 2.
VSP_046677
Natural variant391S → R.
Corresponds to variant rs35224276 [ dbSNP | Ensembl ].
VAR_046634

Experimental info

Sequence conflict31G → T in CAA41226. Ref.1
Sequence conflict681F → L in CAA41226. Ref.1
Sequence conflict13001P → L in AAI51843. Ref.4
Sequence conflict13841R → P in CAA41226. Ref.1

Secondary structure

.............................................................................................................................................. 1452
Helix Strand Turn

Details...

Sequences

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

Last modified September 23, 2008. Version 2.
Checksum: 8319E3D3A583E992

FASTA1,452163,682
        10         20         30         40         50         60 
MRGLGTCLAT LAGLLLTAAG ETFSGGCLFD EPYSTCGYSQ SEGDDFNWEQ VNTLTKPTSD 

        70         80         90        100        110        120 
PWMPSGSFML VNASGRPEGQ RAHLLLPQLK ENDTHCIDFH YFVSSKSNSP PGLLNVYVKV 

       130        140        150        160        170        180 
NNGPLGNPIW NISGDPTRTW NRAELAISTF WPNFYQVIFE VITSGHQGYL AIDEVKVLGH 

       190        200        210        220        230        240 
PCTRTPHFLR IQNVEVNAGQ FATFQCSAIG RTVAGDRLWL QGIDVRDAPL KEIKVTSSRR 

       250        260        270        280        290        300 
FIASFNVVNT TKRDAGKYRC MIRTEGGVGI SNYAELVVKE PPVPIAPPQL ASVGATYLWI 

       310        320        330        340        350        360 
QLNANSINGD GPIVAREVEY CTASGSWNDR QPVDSTSYKI GHLDPDTEYE ISVLLTRPGE 

       370        380        390        400        410        420 
GGTGSPGPAL RTRTKCADPM RGPRKLEVVE VKSRQITIRW EPFGYNVTRC HSYNLTVHYC 

       430        440        450        460        470        480 
YQVGGQEQVR EEVSWDTENS HPQHTITNLS PYTNVSVKLI LMNPEGRKES QELIVQTDED 

       490        500        510        520        530        540 
LPGAVPTESI QGSTFEEKIF LQWREPTQTY GVITLYEITY KAVSSFDPEI DLSNQSGRVS 

       550        560        570        580        590        600 
KLGNETHFLF FGLYPGTTYS FTIRASTAKG FGPPATNQFT TKISAPSMPA YELETPLNQT 

       610        620        630        640        650        660 
DNTVTVMLKP AHSRGAPVSV YQIVVEEERP RRTKKTTEIL KCYPVPIHFQ NASLLNSQYY 

       670        680        690        700        710        720 
FAAEFPADSL QAAQPFTIGD NKTYNGYWNT PLLPYKSYRI YFQAASRANG ETKIDCVQVA 

       730        740        750        760        770        780 
TKGAATPKPV PEPEKQTDHT VKIAGVIAGI LLFVIIFLGV VLVMKKRKLA KKRKETMSST 

       790        800        810        820        830        840 
RQEMTVMVNS MDKSYAEQGT NCDEAFSFMD THNLNGRSVS SPSSFTMKTN TLSTSVPNSY 

       850        860        870        880        890        900 
YPDETHTMAS DTSSLVQSHT YKKREPADVP YQTGQLHPAI RVADLLQHIT QMKCAEGYGF 

       910        920        930        940        950        960 
KEEYESFFEG QSAPWDSAKK DENRMKNRYG NIIAYDHSRV RLQTIEGDTN SDYINGNYID 

       970        980        990       1000       1010       1020 
GYHRPNHYIA TQGPMQETIY DFWRMVWHEN TASIIMVTNL VEVGRVKCCK YWPDDTEIYK 

      1030       1040       1050       1060       1070       1080 
DIKVTLIETE LLAEYVIRTF AVEKRGVHEI REIRQFHFTG WPDHGVPYHA TGLLGFVRQV 

      1090       1100       1110       1120       1130       1140 
KSKSPPSAGP LVVHCSAGAG RTGCFIVIDI MLDMAEREGV VDIYNCVREL RSRRVNMVQT 

      1150       1160       1170       1180       1190       1200 
EEQYVFIHDA ILEACLCGDT SVPASQVRSL YYDMNKLDPQ TNSSQIKEEF RTLNMVTPTL 

      1210       1220       1230       1240       1250       1260 
RVEDCSIALL PRNHEKNRCM DILPPDRCLP FLITIDGESS NYINAALMDS YKQPSAFIVT 

      1270       1280       1290       1300       1310       1320 
QHPLPNTVKD FWRLVLDYHC TSVVMLNDVD PAQLCPQYWP ENGVHRHGPI QVEFVSADLE 

      1330       1340       1350       1360       1370       1380 
EDIISRIFRI YNAARPQDGY RMVQQFQFLG WPMYRDTPVS KRSFLKLIRQ VDKWQEEYNG 

      1390       1400       1410       1420       1430       1440 
GEGRTVVHCL NGGGRSGTFC AISIVCEMLR HQRTVDVFHA VKTLRNNKPN MVDLLDQYKF 

      1450 
CYEVALEYLN SG 

« Hide

Isoform 2 [UniParc].

Checksum: B3D74735CB11E9F6
Show »

FASTA1,465165,060

References

« Hide 'large scale' references
[1]"Cloning, expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase."
Gebbink M.F.B.G., van Etten I., Hateboer G., Suijkerbuijk R., Beijersbergen R., Geurts van Kessel A., Moolenaar W.H.
FEBS Lett. 290:123-130(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"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-131.
Tissue: Plasma.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu."
Hoffmann K.M., Tonks N.K., Barford D.
J. Biol. Chem. 272:27505-27508(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 879-1156.
[8]"Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion."
Aricescu A.R., Hon W.-C., Siebold C., Lu W., van der Merwe P.A., Jones E.Y.
EMBO J. 25:701-712(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-279, FUNCTION, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58288 mRNA. Translation: CAA41226.1.
AC006566 Genomic DNA. No translation available.
AP000897 Genomic DNA. No translation available.
AP001091 Genomic DNA. No translation available.
AP001094 Genomic DNA. No translation available.
AP005118 Genomic DNA. No translation available.
AP005227 Genomic DNA. No translation available.
AP005900 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01623.1.
CH471113 Genomic DNA. Translation: EAX01624.1.
BC151842 mRNA. Translation: AAI51843.1.
CCDSCCDS11840.1. [P28827-1]
CCDS58613.1. [P28827-2]
PIRS17669.
RefSeqNP_001098714.1. NM_001105244.1. [P28827-2]
NP_002836.3. NM_002845.3. [P28827-1]
UniGeneHs.49774.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RPMX-ray2.30A/B879-1156[»]
2C9AX-ray2.70A21-279[»]
2V5YX-ray3.10A21-742[»]
ProteinModelPortalP28827.
SMRP28827. Positions 21-588, 877-1451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111761. 2 interactions.
DIPDIP-668N.
IntActP28827. 5 interactions.
MINTMINT-128128.
STRING9606.ENSP00000331418.

Chemistry

BindingDBP28827.
ChEMBLCHEMBL4661.

PTM databases

PhosphoSiteP28827.

Polymorphism databases

DMDM206729890.

Proteomic databases

MaxQBP28827.
PaxDbP28827.
PRIDEP28827.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332175; ENSP00000331418; ENSG00000173482. [P28827-1]
ENST00000580170; ENSP00000463325; ENSG00000173482. [P28827-2]
GeneID5797.
KEGGhsa:5797.
UCSCuc002knn.4. human. [P28827-1]

Organism-specific databases

CTD5797.
GeneCardsGC18P007557.
H-InvDBHIX0027374.
HGNCHGNC:9675. PTPRM.
HPACAB022442.
CAB022443.
MIM176888. gene.
neXtProtNX_P28827.
PharmGKBPA34020.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOVERGENHBG062785.
InParanoidP28827.
KOK05693.
OrthoDBEOG70KGNP.
PhylomeDBP28827.
TreeFamTF312900.

Gene expression databases

ArrayExpressP28827.
BgeeP28827.
CleanExHS_PTPRM.
GenevestigatorP28827.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
3.90.190.10. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
IPR000998. MAM_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 2 hits.
PF00047. ig. 1 hit.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 4 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 1 hit.
PS00740. MAM_1. 1 hit.
PS50060. MAM_2. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPRM. human.
EvolutionaryTraceP28827.
GeneWikiPTPRM.
GenomeRNAi5797.
NextBio22574.
PROP28827.
SOURCESearch...

Entry information

Entry namePTPRM_HUMAN
AccessionPrimary (citable) accession number: P28827
Secondary accession number(s): A7MBN1, D3DUH8, J3QL11
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 158 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 18

Human chromosome 18: entries, gene names and cross-references to MIM