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P28827

- PTPRM_HUMAN

UniProt

P28827 - PTPRM_HUMAN

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Protein

Receptor-type tyrosine-protein phosphatase mu

Gene

PTPRM

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

Functioni

Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1063 – 10631SubstrateBy similarity
Active sitei1095 – 10951Phosphocysteine intermediateBy similarity
Binding sitei1139 – 11391SubstrateBy similarity
Active sitei1389 – 13891Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. cadherin binding Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. protein tyrosine phosphatase activity Source: UniProtKB
  4. transmembrane receptor protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. homophilic cell adhesion via plasma membrane adhesion molecules Source: UniProtKB
  2. negative regulation of angiogenesis Source: UniProtKB
  3. negative regulation of endothelial cell migration Source: UniProtKB
  4. negative regulation of endothelial cell proliferation Source: UniProtKB
  5. neuron projection development Source: UniProtKB
  6. peptidyl-tyrosine dephosphorylation Source: GOC
  7. positive regulation of vasodilation Source: Ensembl
  8. protein dephosphorylation Source: UniProtKB
  9. response to drug Source: UniProtKB
  10. retina layer formation Source: UniProtKB
  11. retinal ganglion cell axon guidance Source: UniProtKB
  12. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase, Receptor

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase mu (EC:3.1.3.48)
Short name:
Protein-tyrosine phosphatase mu
Short name:
R-PTP-mu
Gene namesi
Name:PTPRM
Synonyms:PTPRL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:9675. PTPRM.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 742722ExtracellularSequence AnalysisAdd
BLAST
Transmembranei743 – 76422HelicalSequence AnalysisAdd
BLAST
Topological domaini765 – 1452688CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell-cell adherens junction Source: UniProtKB
  2. cell-cell junction Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. integral component of plasma membrane Source: UniProtKB
  5. lamellipodium Source: MGI
  6. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 14521432Receptor-type tyrosine-protein phosphatase muPRO_0000025448Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 361 PublicationPROSITE-ProRule annotation
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi96 ↔ 1821 PublicationPROSITE-ProRule annotation
Glycosylationi131 – 1311N-linked (GlcNAc...)1 Publication
Disulfide bondi206 ↔ 2601 PublicationPROSITE-ProRule annotation
Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi534 – 5341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi544 – 5441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi651 – 6511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi681 – 6811N-linked (GlcNAc...)Sequence Analysis
Modified residuei821 – 8211Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP28827.
PaxDbiP28827.
PRIDEiP28827.

PTM databases

PhosphoSiteiP28827.

Expressioni

Gene expression databases

BgeeiP28827.
CleanExiHS_PTPRM.
ExpressionAtlasiP28827. baseline and differential.
GenevestigatoriP28827.

Organism-specific databases

HPAiCAB022442.
CAB022443.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2257317,EBI-2257317
Cdh1P098033EBI-2257317,EBI-984420From a different organism.

Protein-protein interaction databases

BioGridi111761. 2 interactions.
DIPiDIP-668N.
IntActiP28827. 5 interactions.
MINTiMINT-128128.
STRINGi9606.ENSP00000331418.

Structurei

Secondary structure

1
1452
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 313Combined sources
Helixi33 – 364Combined sources
Beta strandi42 – 454Combined sources
Beta strandi49 – 524Combined sources
Turni53 – 553Combined sources
Beta strandi66 – 727Combined sources
Beta strandi81 – 855Combined sources
Beta strandi96 – 1049Combined sources
Beta strandi106 – 1094Combined sources
Beta strandi111 – 12010Combined sources
Beta strandi129 – 1324Combined sources
Beta strandi140 – 1478Combined sources
Beta strandi155 – 1639Combined sources
Beta strandi169 – 18012Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi202 – 2109Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi230 – 2378Combined sources
Beta strandi240 – 2478Combined sources
Helixi252 – 2543Combined sources
Beta strandi256 – 2649Combined sources
Beta strandi267 – 27812Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi289 – 2935Combined sources
Beta strandi298 – 3014Combined sources
Beta strandi305 – 3095Combined sources
Beta strandi315 – 32612Combined sources
Beta strandi328 – 3325Combined sources
Beta strandi335 – 3406Combined sources
Beta strandi348 – 3569Combined sources
Beta strandi370 – 3734Combined sources
Beta strandi384 – 3918Combined sources
Beta strandi396 – 4016Combined sources
Helixi405 – 4084Combined sources
Beta strandi410 – 4123Combined sources
Beta strandi414 – 43421Combined sources
Beta strandi443 – 4464Combined sources
Beta strandi454 – 4629Combined sources
Beta strandi467 – 4693Combined sources
Beta strandi473 – 4764Combined sources
Turni487 – 4893Combined sources
Beta strandi491 – 4955Combined sources
Beta strandi498 – 5025Combined sources
Beta strandi515 – 52511Combined sources
Beta strandi536 – 5427Combined sources
Beta strandi547 – 5504Combined sources
Beta strandi557 – 56711Combined sources
Beta strandi570 – 58011Combined sources
Turni882 – 8843Combined sources
Helixi885 – 90521Combined sources
Turni916 – 9194Combined sources
Helixi921 – 9266Combined sources
Helixi936 – 9383Combined sources
Beta strandi939 – 9413Combined sources
Turni949 – 9524Combined sources
Beta strandi953 – 9619Combined sources
Beta strandi964 – 9718Combined sources
Helixi976 – 9783Combined sources
Helixi979 – 98810Combined sources
Beta strandi993 – 9964Combined sources
Beta strandi1000 – 10023Combined sources
Beta strandi1014 – 10196Combined sources
Beta strandi1022 – 103211Combined sources
Beta strandi1035 – 104410Combined sources
Beta strandi1051 – 10588Combined sources
Beta strandi1063 – 10653Combined sources
Helixi1071 – 108313Combined sources
Beta strandi1091 – 10999Combined sources
Helixi1100 – 111819Combined sources
Beta strandi1119 – 11213Combined sources
Helixi1123 – 113311Combined sources
Helixi1141 – 115515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RPMX-ray2.30A/B879-1156[»]
2C9AX-ray2.70A21-279[»]
2V5YX-ray3.10A21-742[»]
ProteinModelPortaliP28827.
SMRiP28827. Positions 21-588, 877-1451.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28827.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 184163MAMPROSITE-ProRule annotationAdd
BLAST
Domaini186 – 27792Ig-like C2-typeAdd
BLAST
Domaini284 – 37996Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini382 – 48099Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini482 – 587106Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini589 – 67183Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini900 – 1154255Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
BLAST
Domaini1186 – 1448263Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1095 – 11017Substrate bindingBy similarity

Sequence similaritiesi

Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 MAM domain.PROSITE-ProRule annotation
Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118900.
HOVERGENiHBG062785.
InParanoidiP28827.
KOiK05693.
OrthoDBiEOG70KGNP.
PhylomeDBiP28827.
TreeFamiTF312900.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.90.190.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
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]
PfamiPF00041. fn3. 2 hits.
PF00047. ig. 1 hit.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 4 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEiPS50853. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P28827-1) [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
MRGLGTCLAT LAGLLLTAAG ETFSGGCLFD EPYSTCGYSQ SEGDDFNWEQ
60 70 80 90 100
VNTLTKPTSD PWMPSGSFML VNASGRPEGQ RAHLLLPQLK ENDTHCIDFH
110 120 130 140 150
YFVSSKSNSP PGLLNVYVKV NNGPLGNPIW NISGDPTRTW NRAELAISTF
160 170 180 190 200
WPNFYQVIFE VITSGHQGYL AIDEVKVLGH PCTRTPHFLR IQNVEVNAGQ
210 220 230 240 250
FATFQCSAIG RTVAGDRLWL QGIDVRDAPL KEIKVTSSRR FIASFNVVNT
260 270 280 290 300
TKRDAGKYRC MIRTEGGVGI SNYAELVVKE PPVPIAPPQL ASVGATYLWI
310 320 330 340 350
QLNANSINGD GPIVAREVEY CTASGSWNDR QPVDSTSYKI GHLDPDTEYE
360 370 380 390 400
ISVLLTRPGE GGTGSPGPAL RTRTKCADPM RGPRKLEVVE VKSRQITIRW
410 420 430 440 450
EPFGYNVTRC HSYNLTVHYC YQVGGQEQVR EEVSWDTENS HPQHTITNLS
460 470 480 490 500
PYTNVSVKLI LMNPEGRKES QELIVQTDED LPGAVPTESI QGSTFEEKIF
510 520 530 540 550
LQWREPTQTY GVITLYEITY KAVSSFDPEI DLSNQSGRVS KLGNETHFLF
560 570 580 590 600
FGLYPGTTYS FTIRASTAKG FGPPATNQFT TKISAPSMPA YELETPLNQT
610 620 630 640 650
DNTVTVMLKP AHSRGAPVSV YQIVVEEERP RRTKKTTEIL KCYPVPIHFQ
660 670 680 690 700
NASLLNSQYY FAAEFPADSL QAAQPFTIGD NKTYNGYWNT PLLPYKSYRI
710 720 730 740 750
YFQAASRANG ETKIDCVQVA TKGAATPKPV PEPEKQTDHT VKIAGVIAGI
760 770 780 790 800
LLFVIIFLGV VLVMKKRKLA KKRKETMSST RQEMTVMVNS MDKSYAEQGT
810 820 830 840 850
NCDEAFSFMD THNLNGRSVS SPSSFTMKTN TLSTSVPNSY YPDETHTMAS
860 870 880 890 900
DTSSLVQSHT YKKREPADVP YQTGQLHPAI RVADLLQHIT QMKCAEGYGF
910 920 930 940 950
KEEYESFFEG QSAPWDSAKK DENRMKNRYG NIIAYDHSRV RLQTIEGDTN
960 970 980 990 1000
SDYINGNYID GYHRPNHYIA TQGPMQETIY DFWRMVWHEN TASIIMVTNL
1010 1020 1030 1040 1050
VEVGRVKCCK YWPDDTEIYK DIKVTLIETE LLAEYVIRTF AVEKRGVHEI
1060 1070 1080 1090 1100
REIRQFHFTG WPDHGVPYHA TGLLGFVRQV KSKSPPSAGP LVVHCSAGAG
1110 1120 1130 1140 1150
RTGCFIVIDI MLDMAEREGV VDIYNCVREL RSRRVNMVQT EEQYVFIHDA
1160 1170 1180 1190 1200
ILEACLCGDT SVPASQVRSL YYDMNKLDPQ TNSSQIKEEF RTLNMVTPTL
1210 1220 1230 1240 1250
RVEDCSIALL PRNHEKNRCM DILPPDRCLP FLITIDGESS NYINAALMDS
1260 1270 1280 1290 1300
YKQPSAFIVT QHPLPNTVKD FWRLVLDYHC TSVVMLNDVD PAQLCPQYWP
1310 1320 1330 1340 1350
ENGVHRHGPI QVEFVSADLE EDIISRIFRI YNAARPQDGY RMVQQFQFLG
1360 1370 1380 1390 1400
WPMYRDTPVS KRSFLKLIRQ VDKWQEEYNG GEGRTVVHCL NGGGRSGTFC
1410 1420 1430 1440 1450
AISIVCEMLR HQRTVDVFHA VKTLRNNKPN MVDLLDQYKF CYEVALEYLN

SG
Length:1,452
Mass (Da):163,682
Last modified:September 23, 2008 - v2
Checksum:i8319E3D3A583E992
GO
Isoform 2 (identifier: P28827-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,465
Mass (Da):165,060
Checksum:iB3D74735CB11E9F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31G → T in CAA41226. (PubMed:1655529)Curated
Sequence conflicti68 – 681F → L in CAA41226. (PubMed:1655529)Curated
Sequence conflicti1300 – 13001P → L in AAI51843. (PubMed:15489334)Curated
Sequence conflicti1384 – 13841R → P in CAA41226. (PubMed:1655529)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391S → R.
Corresponds to variant rs35224276 [ dbSNP | Ensembl ].
VAR_046634

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei842 – 8421P → PDPFVPTAILVPIN in isoform 2. 1 PublicationVSP_046677

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11840.1. [P28827-1]
CCDS58613.1. [P28827-2]
PIRiS17669.
RefSeqiNP_001098714.1. NM_001105244.1. [P28827-2]
NP_002836.3. NM_002845.3. [P28827-1]
UniGeneiHs.49774.

Genome annotation databases

EnsembliENST00000332175; ENSP00000331418; ENSG00000173482. [P28827-1]
ENST00000580170; ENSP00000463325; ENSG00000173482. [P28827-2]
GeneIDi5797.
KEGGihsa:5797.
UCSCiuc002knn.4. human. [P28827-1]

Polymorphism databases

DMDMi206729890.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS11840.1. [P28827-1 ]
CCDS58613.1. [P28827-2 ]
PIRi S17669.
RefSeqi NP_001098714.1. NM_001105244.1. [P28827-2 ]
NP_002836.3. NM_002845.3. [P28827-1 ]
UniGenei Hs.49774.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P28827.
SMRi P28827. Positions 21-588, 877-1451.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111761. 2 interactions.
DIPi DIP-668N.
IntActi P28827. 5 interactions.
MINTi MINT-128128.
STRINGi 9606.ENSP00000331418.

Chemistry

BindingDBi P28827.
ChEMBLi CHEMBL4661.

PTM databases

PhosphoSitei P28827.

Polymorphism databases

DMDMi 206729890.

Proteomic databases

MaxQBi P28827.
PaxDbi P28827.
PRIDEi P28827.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000332175 ; ENSP00000331418 ; ENSG00000173482 . [P28827-1 ]
ENST00000580170 ; ENSP00000463325 ; ENSG00000173482 . [P28827-2 ]
GeneIDi 5797.
KEGGi hsa:5797.
UCSCi uc002knn.4. human. [P28827-1 ]

Organism-specific databases

CTDi 5797.
GeneCardsi GC18P007557.
H-InvDB HIX0027374.
HGNCi HGNC:9675. PTPRM.
HPAi CAB022442.
CAB022443.
MIMi 176888. gene.
neXtProti NX_P28827.
PharmGKBi PA34020.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118900.
HOVERGENi HBG062785.
InParanoidi P28827.
KOi K05693.
OrthoDBi EOG70KGNP.
PhylomeDBi P28827.
TreeFami TF312900.

Miscellaneous databases

ChiTaRSi PTPRM. human.
EvolutionaryTracei P28827.
GeneWikii PTPRM.
GenomeRNAii 5797.
NextBioi 22574.
PROi P28827.
SOURCEi Search...

Gene expression databases

Bgeei P28827.
CleanExi HS_PTPRM.
ExpressionAtlasi P28827. baseline and differential.
Genevestigatori P28827.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
3.90.190.10. 2 hits.
InterProi IPR013320. ConA-like_dom.
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 ]
Pfami PF00041. fn3. 2 hits.
PF00047. ig. 1 hit.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view ]
PRINTSi PR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.
SMARTi SM00060. FN3. 4 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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. 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.

Entry informationi

Entry nameiPTPRM_HUMAN
AccessioniPrimary (citable) accession number: P28827
Secondary accession number(s): A7MBN1, D3DUH8, J3QL11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: September 23, 2008
Last modified: November 26, 2014
This is version 161 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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

Dasty 3