O14522 (PTPRT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Receptor-type tyrosine-protein phosphatase T
Short name=R-PTP-T
EC=3.1.3.48

Alternative name(s):
Receptor-type tyrosine-protein phosphatase rho
Short name=RPTP-rho

Gene names

Name:	PTPRT
Synonyms:	KIAA0283

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1441 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	May be involved in both signal transduction and cellular adhesion in the CNS.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed in colon, lung, heart and testis, as well as in fetal and adult brain. Not detected in muscle and peripheral blood leukocytes. Ref.8
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.
Sequence caution	The sequence BAA22952.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAH72555.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI19251.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI19867.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI19879.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI19983.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI20439.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI22491.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI22911.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI23312.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Hydrolase Protein phosphatase Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	homophilic cell adhesion Inferred from direct assay PubMed 18644975. Source: UniProtKB transmembrane receptor protein tyrosine kinase signaling pathway Inferred from mutant phenotype PubMed 16973135. Source: UniProtKB
Cellular_component	cell surface Inferred from direct assay PubMed 18644975. Source: UniProtKB integral to membrane Non-traceable author statement Ref.1. Source: UniProtKB plasma membrane Inferred from direct assay PubMed 18644975. Source: UniProtKB
Molecular_function	alpha-catenin binding Inferred from direct assay PubMed 16973135. Source: UniProtKB gamma-catenin binding Inferred from direct assay PubMed 16973135. Source: UniProtKB protein tyrosine phosphatase activity Inferred from mutant phenotype PubMed 16973135PubMed 17360477. Source: UniProtKB thiolester hydrolase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTPRN	Q16849	3	EBI-728180,EBI-728153

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: O14522-3)

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 1 (identifier: O14522-1)

The sequence of this isoform differs from the canonical sequence as follows:
     725-725: K → KAPMGSAQVTPGTPLCLLTT
     781-781: L → LSQR

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Chain

26 – 1441

1416

Receptor-type tyrosine-protein phosphatase T

PRO_0000025463

Regions

Topological domain

26 – 747

722

Extracellular Potential

Transmembrane

748 – 768

21

Helical; Potential

Topological domain

769 – 1441

673

Cytoplasmic Potential

Domain

30 – 191

162

MAM

Domain

193 – 284

92

Ig-like C2-type

Domain

288 – 379

92

Fibronectin type-III 1

Domain

386 – 480

95

Fibronectin type-III 2

Domain

481 – 584

104

Fibronectin type-III 3

Domain

589 – 726

138

Fibronectin type-III 4

Domain

889 – 1143

255

Tyrosine-protein phosphatase 1

Domain

1175 – 1437

263

Tyrosine-protein phosphatase 2

Region

1084 – 1090

7

Substrate binding By similarity

Sites

Active site

1084

1

Phosphocysteine intermediate By similarity

Active site

1378

1

Phosphocysteine intermediate By similarity

Binding site

1052

1

Substrate By similarity

Binding site

1128

1

Substrate By similarity

Amino acid modifications

Glycosylation

78

1

N-linked (GlcNAc...) Potential

Glycosylation

98

1

N-linked (GlcNAc...) Potential

Glycosylation

137

1

N-linked (GlcNAc...) Potential

Glycosylation

208

1

N-linked (GlcNAc...) Potential

Glycosylation

421

1

N-linked (GlcNAc...) Potential

Glycosylation

510

1

N-linked (GlcNAc...) Potential

Glycosylation

547

1

N-linked (GlcNAc...) Potential

Glycosylation

601

1

N-linked (GlcNAc...) Potential

Glycosylation

654

1

N-linked (GlcNAc...) Potential

Glycosylation

684

1

N-linked (GlcNAc...) Potential

Disulfide bond

213 ↔ 267

By similarity

Natural variations

Alternative sequence

725

1

K → KAPMGSAQVTPGTPLCLLTT in isoform 1.

VSP_040385

Alternative sequence

781

1

L → LSQR in isoform 1.

VSP_040386

Natural variant

29

1

A → P. Ref.1 Ref.2 Ref.4
Corresponds to variant rs2867655 [ dbSNP | Ensembl ].

VAR_028795

Natural variant

74

1

F → S in a colorectal cancer. Ref.8

VAR_020746

Natural variant

76

1

M → V.
Corresponds to variant rs17811401 [ dbSNP | Ensembl ].

VAR_028796

Natural variant

209

1

A → T in some colorectal cancers. Ref.8

VAR_020747

Natural variant

218

1

K → T in a gastric cancer. Ref.8

VAR_020748

Natural variant

248

1

F → S in a colorectal cancer. Ref.8

VAR_020749

Natural variant

280

1

Y → H in a colorectal cancer. Ref.8

VAR_020750

Natural variant

395

1

I → V in a colorectal cancer. Ref.8

VAR_020751

Natural variant

412

1

Y → F in a colorectal cancer. Ref.8

VAR_020752

Natural variant

453

1

R → C in a gastric cancer. Ref.8

VAR_020753

Natural variant

510

1

N → K in a colorectal cancer. Ref.8

VAR_020754

Natural variant

605

1

T → M in a colorectal cancer. Ref.8

VAR_020755

Natural variant

648

1

V → G in a colorectal cancer. Ref.8

VAR_020756

Natural variant

707

1

A → T in a colorectal cancer. Ref.8

VAR_020757

Natural variant

707

1

A → V in a colorectal cancer. Ref.8

VAR_020758

Natural variant

708

1

L → P in a colorectal cancer. Ref.8

VAR_020759

Natural variant

771

1

R → I in a lung cancer. Ref.8

VAR_020760

Natural variant

905

1

D → G in a colorectal cancer. Ref.8

VAR_020761

Natural variant

965

1

Q → K in a colorectal cancer; reduced phosphatase activity. Ref.8

VAR_020762

Natural variant

1096

1

A → P in a colorectal cancer. Ref.8

VAR_020763

Natural variant

1106

1

N → I in a colorectal cancer; reduced phosphatase activity. Ref.8

VAR_020764

Natural variant

1190

1

R → W in a colorectal cancer; reduced phosphatase activity. Ref.8

VAR_020765

Natural variant

1213

1

P → L in an acute myeloid leukemia sample; somatic mutation. Ref.9

VAR_054144

Natural variant

1237

1

M → L in a colorectal cancer. Ref.8

VAR_020766

Natural variant

1247

1

V → M in a colorectal cancer. Ref.8

VAR_020767

Natural variant

1324

1

R → L in a lung cancer; reduced phosphatase activity. Ref.8

VAR_020768

Natural variant

1329

1

Y → F in a colorectal cancer. Ref.8

VAR_020769

Natural variant

1346

1

T → M in some colorectal cancers; reduced phosphatase activity. Ref.8

VAR_020770

Experimental info

Sequence conflict

60

1

W → T in AAD09421. Ref.1

Sequence conflict

375

1

P → A in AAD09421. Ref.1

Sequence conflict

867

1

P → L in AAD09421. Ref.1

Secondary structure

1

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1441

Helix Strand Turn

Details...

Helix

871 – 873

3

Helix

874 – 882

9

Helix

889 – 895

7

Turn

905 – 908

4

Helix

910 – 915

6

Helix

925 – 927

3

Helix

938 – 941

4

Beta strand

944 – 948

5

Beta strand

951 – 953

3

Beta strand

957 – 960

4

Turn

965 – 967

3

Helix

968 – 978

11

Beta strand

982 – 985

4

Beta strand

989 – 991

3

Beta strand

1003 – 1009

7

Beta strand

1011 – 1020

10

Beta strand

1022 – 1033

12

Beta strand

1040 – 1047

8

Helix

1060 – 1072

13

Beta strand

1080 – 1083

4

Beta strand

1085 – 1088

4

Helix

1089 – 1107

19

Beta strand

1108 – 1110

3

Helix

1112 – 1122

11

Helix

1130 – 1145

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 [UniParc]. Last modified January 11, 2011. Version 6. Checksum: BE60F3DB2CE13539	FASTA	1,441	162,134
	10 20 30 40 50 60 MASLAALALS LLLRLQLPPL PGARAQSAAG GCSFDEHYSN CGYSVALGTN GFTWEQINTW 70 80 90 100 110 120 EKPMLDQAVP TGSFMMVNSS GRASGQKAHL LLPTLKENDT HCIDFHYYFS SRDRSSPGAL 130 140 150 160 170 180 NVYVKVNGGP QGNPVWNVSG VVTEGWVKAE LAISTFWPHF YQVIFESVSL KGHPGYIAVD 190 200 210 220 230 240 EVRVLAHPCR KAPHFLRLQN VEVNVGQNAT FQCIAGGKWS QHDKLWLQQW NGRDTALMVT 250 260 270 280 290 300 RVVNHRRFSA TVSVADTAQR SVSKYRCVIR SDGGSGVSNY AELIVKEPPT PIAPPELLAV 310 320 330 340 350 360 GATYLWIKPN ANSIIGDGPI ILKEVEYRTT TGTWAETHIV DSPNYKLWHL DPDVEYEIRV 370 380 390 400 410 420 LLTRPGEGGT GPPGPPLTTR TKCADPVHGP QNVEIVDIRA RQLTLQWEPF GYAVTRCHSY 430 440 450 460 470 480 NLTVQYQYVF NQQQYEAEEV IQTSSHYTLR GLRPFMTIRL RLLLSNPEGR MESEELVVQT 490 500 510 520 530 540 EEDVPGAVPL ESIQGGPFEE KIYIQWKPPN ETNGVITLYE INYKAVGSLD PSADLSSQRG 550 560 570 580 590 600 KVFKLRNETH HLFVGLYPGT TYSFTIKAST AKGFGPPVTT RIATKISAPS MPEYDTDTPL 610 620 630 640 650 660 NETDTTITVM LKPAQSRGAP VSVYQLVVKE ERLQKSRRAA DIIECFSVPV SYRNASSLDS 670 680 690 700 710 720 LHYFAAELKP ANLPVTQPFT VGDNKTYNGY WNPPLSPLKS YSIYFQALSK ANGETKINCV 730 740 750 760 770 780 RLATKGASTQ NSNTVEPEKQ VDNTVKMAGV IAGLLMFIII LLGVMLTIKR RRNAYSYSYY 790 800 810 820 830 840 LKLAKKQKET QSGAQREMGP VASADKPTTK LSASRNDEGF SSSSQDVNGF TDGSRGELSQ 850 860 870 880 890 900 PTLTIQTHPY RTCDPVEMSY PRDQFQPAIR VADLLQHITQ MKRGQGYGFK EEYEALPEGQ 910 920 930 940 950 960 TASWDTAKED ENRNKNRYGN IISYDHSRVR LLVLDGDPHS DYINANYIDG YHRPRHYIAT 970 980 990 1000 1010 1020 QGPMQETVKD FWRMIWQENS ASIVMVTNLV EVGRVKCVRY WPDDTEVYGD IKVTLIETEP 1030 1040 1050 1060 1070 1080 LAEYVIRTFT VQKKGYHEIR ELRLFHFTSW PDHGVPCYAT GLLGFVRQVK FLNPPEAGPI 1090 1100 1110 1120 1130 1140 VVHCSAGAGR TGCFIAIDTM LDMAENEGVV DIFNCVRELR AQRVNLVQTE EQYVFVHDAI 1150 1160 1170 1180 1190 1200 LEACLCGNTA IPVCEFRSLY YNISRLDPQT NSSQIKDEFQ TLNIVTPRVR PEDCSIGLLP 1210 1220 1230 1240 1250 1260 RNHDKNRSMD VLPLDRCLPF LISVDGESSN YINAALMDSH KQPAAFVVTQ HPLPNTVADF 1270 1280 1290 1300 1310 1320 WRLVFDYNCS SVVMLNEMDT AQFCMQYWPE KTSGCYGPIQ VEFVSADIDE DIIHRIFRIC 1330 1340 1350 1360 1370 1380 NMARPQDGYR IVQHLQYIGW PAYRDTPPSK RSLLKVVRRL EKWQEQYDGR EGRTVVHCLN 1390 1400 1410 1420 1430 1440 GGGRSGTFCA ICSVCEMIQQ QNIIDVFHIV KTLRNNKSNM VETLEQYKFV YEVALEYLSS F
	Isoform 1 [UniParc]. Checksum: 531E33DF9040F4B5	FASTA	1,463	164,346
	10 20 30 40 50 60 MASLAALALS LLLRLQLPPL PGARAQSAAG GCSFDEHYSN CGYSVALGTN GFTWEQINTW 70 80 90 100 110 120 EKPMLDQAVP TGSFMMVNSS GRASGQKAHL LLPTLKENDT HCIDFHYYFS SRDRSSPGAL 130 140 150 160 170 180 NVYVKVNGGP QGNPVWNVSG VVTEGWVKAE LAISTFWPHF YQVIFESVSL KGHPGYIAVD 190 200 210 220 230 240 EVRVLAHPCR KAPHFLRLQN VEVNVGQNAT FQCIAGGKWS QHDKLWLQQW NGRDTALMVT 250 260 270 280 290 300 RVVNHRRFSA TVSVADTAQR SVSKYRCVIR SDGGSGVSNY AELIVKEPPT PIAPPELLAV 310 320 330 340 350 360 GATYLWIKPN ANSIIGDGPI ILKEVEYRTT TGTWAETHIV DSPNYKLWHL DPDVEYEIRV 370 380 390 400 410 420 LLTRPGEGGT GPPGPPLTTR TKCADPVHGP QNVEIVDIRA RQLTLQWEPF GYAVTRCHSY 430 440 450 460 470 480 NLTVQYQYVF NQQQYEAEEV IQTSSHYTLR GLRPFMTIRL RLLLSNPEGR MESEELVVQT 490 500 510 520 530 540 EEDVPGAVPL ESIQGGPFEE KIYIQWKPPN ETNGVITLYE INYKAVGSLD PSADLSSQRG 550 560 570 580 590 600 KVFKLRNETH HLFVGLYPGT TYSFTIKAST AKGFGPPVTT RIATKISAPS MPEYDTDTPL 610 620 630 640 650 660 NETDTTITVM LKPAQSRGAP VSVYQLVVKE ERLQKSRRAA DIIECFSVPV SYRNASSLDS 670 680 690 700 710 720 LHYFAAELKP ANLPVTQPFT VGDNKTYNGY WNPPLSPLKS YSIYFQALSK ANGETKINCV 730 740 750 760 770 780 RLATKAPMGS AQVTPGTPLC LLTTGASTQN SNTVEPEKQV DNTVKMAGVI AGLLMFIIIL 790 800 810 820 830 840 LGVMLTIKRR RNAYSYSYYL SQRKLAKKQK ETQSGAQREM GPVASADKPT TKLSASRNDE 850 860 870 880 890 900 GFSSSSQDVN GFTDGSRGEL SQPTLTIQTH PYRTCDPVEM SYPRDQFQPA IRVADLLQHI 910 920 930 940 950 960 TQMKRGQGYG FKEEYEALPE GQTASWDTAK EDENRNKNRY GNIISYDHSR VRLLVLDGDP 970 980 990 1000 1010 1020 HSDYINANYI DGYHRPRHYI ATQGPMQETV KDFWRMIWQE NSASIVMVTN LVEVGRVKCV 1030 1040 1050 1060 1070 1080 RYWPDDTEVY GDIKVTLIET EPLAEYVIRT FTVQKKGYHE IRELRLFHFT SWPDHGVPCY 1090 1100 1110 1120 1130 1140 ATGLLGFVRQ VKFLNPPEAG PIVVHCSAGA GRTGCFIAID TMLDMAENEG VVDIFNCVRE 1150 1160 1170 1180 1190 1200 LRAQRVNLVQ TEEQYVFVHD AILEACLCGN TAIPVCEFRS LYYNISRLDP QTNSSQIKDE 1210 1220 1230 1240 1250 1260 FQTLNIVTPR VRPEDCSIGL LPRNHDKNRS MDVLPLDRCL PFLISVDGES SNYINAALMD 1270 1280 1290 1300 1310 1320 SHKQPAAFVV TQHPLPNTVA DFWRLVFDYN CSSVVMLNEM DTAQFCMQYW PEKTSGCYGP 1330 1340 1350 1360 1370 1380 IQVEFVSADI DEDIIHRIFR ICNMARPQDG YRIVQHLQYI GWPAYRDTPP SKRSLLKVVR 1390 1400 1410 1420 1430 1440 RLEKWQEQYD GREGRTVVHC LNGGGRSGTF CAICSVCEMI QQQNIIDVFH IVKTLRNNKS 1450 1460 NMVETLEQYK FVYEVALEYL SSF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of RPTP rho, a novel RPTP mu/kappa-like receptor protein tyrosine phosphatase whose expression is restricted to the central nervous system." McAndrew P.E., Frostholm A., White R.A., Rotter A., Burghes A.H.M. Brain Res. Mol. Brain Res. 56:9-21(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, VARIANT PRO-29.
[2]	"Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins." Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N. DNA Res. 4:53-59(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT PRO-29. Tissue: Brain.
[3]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] 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 3), VARIANT PRO-29.
[5]	"Genomic organization and alternative splicing of the human and mouse RPTPrho genes." Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A. BMC Genomics 2:1-1(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING.
[6]	Erratum Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A. BMC Genomics 2:5-5(2001) [PubMed] [Europe PMC] [Abstract]
[7]	"Large-scale structural analysis of the classical human protein tyrosine phosphatome." Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S. Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 868-1151.
[8]	"Mutational analysis of the tyrosine phosphatome in colorectal cancers." Wang Z., Shen D., Parsons D.W., Bardelli A., Sager J., Szabo S., Ptak J., Silliman N., Peters B.A., van der Heijden M.S., Parmigiani G., Yan H., Wang T.-L., Riggins G., Powell S.M., Willson J.K.V., Markowitz S., Kinzler K.W., Vogelstein B., Velculescu V.E. Science 304:1164-1166(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SER-74; THR-209; THR-218; SER-248; HIS-280; VAL-395; PHE-412; CYS-453; LYS-510; MET-605; GLY-648; THR-707; VAL-707; PRO-708; ILE-771; GLY-905; LYS-965; PRO-1096; ILE-1106; TRP-1190; LEU-1237; MET-1247; LEU-1324; PHE-1329 AND MET-1346, TISSUE SPECIFICITY.
[9]	"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome." Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K. Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-1213.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF043644 mRNA. Translation: AAD09421.2.
AB006621 mRNA. Translation: BAA22952.2. Different initiation.
AL021395 , AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19981.1.
AL021395 , AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19983.1. Sequence problems.
AL022239 , AL021395, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI20437.1.
AL022239 , AL021395, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI20439.1. Sequence problems.
AL024473 , AL021395, AL022239, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI22489.1.
AL024473 , AL021395, AL022239, AL031656, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI22491.1. Sequence problems.
AL031656 , AL021395, AL022239, AL024473, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19877.1.
AL031656 , AL021395, AL022239, AL024473, AL035459, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19879.1. Sequence problems.
AL035459 , AL021395, AL022239, AL024473, AL031656, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI22909.1.
AL035459 , AL021395, AL022239, AL024473, AL031656, AL049812, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI22911.1. Sequence problems.
AL049812 , AL021395, AL022239, AL024473, AL031656, AL035459, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19251.1. Sequence problems.
AL049812 , AL022239, AL031656, AL021395, AL024473, AL035459, AL121763, AL136461, Z93942 Genomic DNA. Translation: CAI19253.1.
AL121763 , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL136461, Z93942 Genomic DNA. Translation: CAI23310.1.
AL121763 , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL136461, Z93942 Genomic DNA. Translation: CAI23312.1. Sequence problems.
AL136461 , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, Z93942 Genomic DNA. Translation: CAH72553.1.
AL136461 , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, Z93942 Genomic DNA. Translation: CAH72555.1. Sequence problems.
Z93942 , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461 Genomic DNA. Translation: CAI19865.1.
Z93942 , AL021395, AL022239, AL024473, AL031656, AL035459, AL049812, AL121763, AL136461 Genomic DNA. Translation: CAI19867.1. Sequence problems.
AL031676 Genomic DNA. No translation available.
AL035666 Genomic DNA. No translation available.
AL109826 Genomic DNA. No translation available.
AL117374 Genomic DNA. No translation available.
AL359695 Genomic DNA. No translation available.
BC153300 mRNA. Translation: AAI53301.1.

IPI

IPI00013096.
IPI00655582.

RefSeq

NP_008981.4. NM_007050.5.
NP_573400.3. NM_133170.3.

UniGene

Hs.526879.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OOQ	X-ray	1.80	A/B	868-1151	[»]

ProteinModelPortal

O14522.

SMR

O14522. Positions 29-591, 866-1441.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33967N.

IntAct

O14522. 1 interaction.

MINT

MINT-1350261.

PTM databases

PhosphoSite

O14522.

Proteomic databases

PaxDb

O14522.

PRIDE

O14522.

Protocols and materials databases

DNASU

11122.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373187; ENSP00000362283; ENSG00000196090.
ENST00000373193; ENSP00000362289; ENSG00000196090.
ENST00000373198; ENSP00000362294; ENSG00000196090.

GeneID

11122.

KEGG

hsa:11122.

UCSC

uc002xkg.3. human.
uc010ggj.3. human.

Organism-specific databases

CTD

11122.

GeneCards

GC20M040701.

HGNC

HGNC:9682. PTPRT.

HPA

HPA017336.

MIM

608712. gene.

neXtProt

NX_O14522.

PharmGKB

PA34027.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5599.

HOVERGEN

HBG062785.

InParanoid

O14522.

KO

K13297.

OMA

QTHPYRT.

Gene expression databases

ArrayExpress

O14522.

Bgee

O14522.

Genevestigator

O14522.

GermOnline

ENSG00000196090. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 4 hits.

InterPro

IPR008985. ConA-like_lec_gl_sf.
IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR000998. MAM_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Pfam

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

PRINTS

PR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.

SMART

SM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.
SSF49265. FN_III-like. 3 hits.

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

EvolutionaryTrace

O14522.

GenomeRNAi

11122.

NextBio

42270.

SOURCE

Search...

Entry information

Entry name

PTPRT_HUMAN

Accession

Primary (citable) accession number: O14522
Secondary accession number(s): A8E4R6 , O43655, O75664, Q5W0X9, Q5W0Y1, Q9BR24, Q9BR28, Q9H0Y8, Q9NTL1, Q9NU72, Q9UBD2, Q9UJL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2003
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 121 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.