Reviewed, UniProtKB/Swiss-Prot P28827 (PTPRM_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.6
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 process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane
Molecular function	Hydrolase Protein phosphatase Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	homophilic cell adhesion Inferred from direct assay. Source: UniProtKB negative regulation of angiogenesis Inferred from mutant phenotype. Source: UniProtKB negative regulation of endothelial cell migration Inferred from mutant phenotype. Source: UniProtKB negative regulation of endothelial cell proliferation Inferred from mutant phenotype. Source: UniProtKB protein amino acid dephosphorylation Inferred from direct assay. Source: UniProtKB response to drug Inferred from direct assay. Source: UniProtKB retina layer formation Inferred from mutant phenotype. Source: UniProtKB retinal ganglion cell axon guidance Inferred from direct assay. Source: UniProtKB signal transduction Inferred from direct assay. Source: UniProtKB
Cellular component	cell-cell adherens junction Inferred from direct assay. Source: UniProtKB integral to plasma membrane Ref.1 Non-traceable author statement. Source: UniProtKB lamellipodium Inferred from direct assay. Source: MGI perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	cadherin binding Inferred from direct assay. Source: UniProtKB transmembrane receptor protein tyrosine phosphatase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LCK	P06239	1	EBI-2257317,EBI-1348

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 1452

1432

Receptor-type tyrosine-protein phosphatase mu

PRO_0000025448

Regions

Topological domain

21 – 742

722

Extracellular Potential

Transmembrane

743 – 764

22

Potential

Topological domain

765 – 1452

688

Cytoplasmic Potential

Domain

22 – 184

163

MAM

Domain

186 – 277

92

Ig-like C2-type

Domain

281 – 371

91

Fibronectin type-III 1

Domain

379 – 477

99

Fibronectin type-III 2

Domain

482 – 581

100

Fibronectin type-III 3

Domain

589 – 671

83

Fibronectin type-III 4

Domain

900 – 1154

255

Tyrosine-protein phosphatase 1

Domain

1186 – 1448

263

Tyrosine-protein phosphatase 2

Sites

Active site

1095

1

Phosphocysteine intermediate By similarity

Active site

1389

1

Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue

821

1

Phosphoserine Ref.4

Modified residue

824

1

Phosphoserine Ref.4

Glycosylation

72

1

N-linked (GlcNAc...) Potential

Glycosylation

92

1

N-linked (GlcNAc...) Potential

Glycosylation

131

1

N-linked (GlcNAc...) Ref.3

Glycosylation

249

1

N-linked (GlcNAc...) Potential

Glycosylation

406

1

N-linked (GlcNAc...) Potential

Glycosylation

414

1

N-linked (GlcNAc...) Potential

Glycosylation

454

1

N-linked (GlcNAc...) Potential

Glycosylation

534

1

N-linked (GlcNAc...) Potential

Glycosylation

544

1

N-linked (GlcNAc...) Potential

Glycosylation

598

1

N-linked (GlcNAc...) Potential

Glycosylation

651

1

N-linked (GlcNAc...) Potential

Glycosylation

681

1

N-linked (GlcNAc...) Potential

Disulfide bond

27 ↔ 36

Ref.6

Disulfide bond

96 ↔ 182

Ref.6

Disulfide bond

206 ↔ 260

Ref.6

Natural variations

Natural variant

39

1

S → R: dbSNP rs35224276.

VAR_046634

Experimental info

Sequence conflict

3

1

G → T in CAA41226. Ref.1

Sequence conflict

68

1

F → L in CAA41226. Ref.1

Sequence conflict

1384

1

R → P in CAA41226. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1452

Helix Strand Turn

Details...

Beta strand

29 – 31

3

Helix

33 – 36

4

Beta strand

42 – 45

4

Beta strand

49 – 52

4

Turn

53 – 55

3

Beta strand

66 – 72

7

Beta strand

81 – 85

5

Beta strand

96 – 104

9

Beta strand

106 – 109

4

Beta strand

111 – 120

10

Beta strand

129 – 132

4

Beta strand

140 – 147

8

Beta strand

155 – 163

9

Beta strand

169 – 180

12

Beta strand

183 – 185

3

Beta strand

194 – 196

3

Beta strand

198 – 200

3

Beta strand

202 – 210

9

Beta strand

217 – 222

6

Beta strand

230 – 237

8

Beta strand

240 – 247

8

Helix

252 – 254

3

Beta strand

256 – 264

9

Beta strand

267 – 278

12

Turn

882 – 884

3

Helix

885 – 905

21

Turn

916 – 919

4

Helix

921 – 926

6

Helix

936 – 938

3

Beta strand

939 – 941

3

Turn

949 – 952

4

Beta strand

953 – 961

9

Beta strand

964 – 971

8

Helix

976 – 978

3

Helix

979 – 988

10

Beta strand

993 – 996

4

Beta strand

1000 – 1002

3

Beta strand

1014 – 1019

6

Beta strand

1022 – 1032

11

Beta strand

1035 – 1044

10

Beta strand

1051 – 1058

8

Beta strand

1063 – 1065

3

Helix

1071 – 1083

13

Beta strand

1091 – 1099

9

Helix

1100 – 1118

19

Beta strand

1119 – 1121

3

Helix

1123 – 1133

11

Helix

1141 – 1155

15

Sequences

	Sequence		Length	Mass (Da)
	P28827-1 [UniParc]. Last modified September 23, 2008. Version 2. Checksum: 8319E3D3A583E992	FASTA	1,452	163,682
	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

References

	« Hide 'large scale' referencesShow '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: 1655529] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. , 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: 16177791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-131, MASS SPECTROMETRY. Tissue: Plasma.
[4]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821 AND SER-824, MASS SPECTROMETRY.
[5]	"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: 9346878] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 879-1156.
[6]	"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: 16456543] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-279, FUNCTION, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00293849.

PIR

S17669.

RefSeq

NP_002836.3.

UniGene

Hs.49774

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RPM	X-ray	2.30	A/B	879-1156	[»]
2C9A	X-ray	2.70	A	21-279	[»]
2V5Y	X-ray	3.10	A	21-742	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:668N.

IntAct

P28827. 1 interaction.

PTM databases

PhosphoSite

P28827.

Proteomic databases

PRIDE

P28827.

Genome annotation databases

Ensembl

ENSG00000173482. Homo sapiens. [Contig view]

GeneID

5797.

Organism-specific databases

GeneCards

GC18P007557.

H-InvDB

HIX0027374.

HGNC

HGNC:9675. PTPRM.

MIM

176888. gene.

PharmGKB

PA34020.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P28827.

HOVERGEN

P28827.

OMA

P28827. ASIIMVT.

Enzyme and pathway databases

BRENDA

3.1.3.48. 247.

Gene expression databases

ArrayExpress

P28827.

Bgee

P28827.

CleanEx

HS_PTPRM.

GermOnline

ENSG00000173482. Homo sapiens.

Family and domain databases

InterPro

IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR000998. MAM.
IPR000387. Tyr_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Gene3D

G3DSA:2.60.40.30. FN_III-like. 2 hits.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

Pfam

PF00041. fn3. 3 hits.
PF00047. ig. 1 hit.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]

PRINTS

PR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.

SMART

SM00060. FN3. 4 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]

PROSITE

PS50853. 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]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

PTPRM_HUMAN

Accession

Primary (citable) accession number: P28827

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	September 23, 2008
Last modified:	June 16, 2009
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)