P08575 (PTPRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Receptor-type tyrosine-protein phosphatase C
EC=3.1.3.48

Alternative name(s):
Leukocyte common antigen
Short name=L-CA
T200
CD_antigen=CD45

Gene names

Name:	PTPRC
Synonyms:	CD45

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	1304 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	Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity By similarity. Ref.6 Ref.8
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Binds GANAB and PRKCSH By similarity. Interacts with SKAP1. Interacts with DPP4; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes. Ref.8 Ref.9
Subcellular location	Membrane; Single-pass type I membrane protein. Membrane raft. Note: Colocalized with DPP4 in membrane rafts. Ref.9
Domain	The first PTPase domain interacts with SKAP1.
Post-translational modification	Heavily N- and O-glycosylated.
Involvement in disease	Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID) [MIM:608971]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Multiple sclerosis (MS) [MIM:126200]: A multifactorial, inflammatory, demyelinating disease of the central nervous system. Sclerotic lesions are characterized by perivascular infiltration of monocytes and lymphocytes and appear as indurated areas in pathologic specimens (sclerosis in plaques). The pathological mechanism is regarded as an autoimmune attack of the myelin sheat, mediated by both cellular and humoral immunity. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia and bladder dysfunction. Genetic and environmental factors influence susceptibility to the disease. Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry. Ref.16
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Receptor class 1/6 subfamily. Contains 2 fibronectin type-III domains. Contains 2 tyrosine-protein phosphatase domains.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation SCID
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Hydrolase Protein phosphatase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB B cell receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB T cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB T cell receptor signaling pathway Inferred from direct assay PubMed 10358156. Source: UniProtKB axon guidance Traceable author statement. Source: Reactome bone marrow development Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB defense response to virus Inferred from sequence or structural similarity. Source: UniProtKB hematopoietic progenitor cell differentiation Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB immunoglobulin biosynthetic process Inferred from mutant phenotype PubMed 1793833. Source: UniProtKB negative regulation of T cell mediated cytotoxicity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell adhesion involved in substrate-bound cell migration Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB negative regulation of cytokine-mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein kinase activity Inferred from direct assay PubMed 9197241. Source: UniProtKB positive regulation of B cell proliferation Inferred from mutant phenotype PubMed 1793833. Source: UniProtKB positive regulation of T cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of antigen receptor-mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of hematopoietic stem cell migration Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB positive regulation of protein kinase activity Non-traceable author statement PubMed 15275963. Source: UniProtKB positive regulation of stem cell proliferation Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB regulation of S phase Inferred from mutant phenotype PubMed 1793833. Source: UniProtKB release of sequestered calcium ion into cytosol Inferred from sequence or structural similarity. Source: UniProtKB stem cell development Inferred from mutant phenotype PubMed 21911094. Source: UniProtKB
Cellular_component	external side of plasma membrane Inferred from direct assay PubMed 17213291. Source: MGI focal adhesion Inferred from sequence or structural similarity. Source: UniProtKB integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB membrane raft Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	transmembrane receptor protein tyrosine phosphatase activity Traceable author statement Ref.6. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERBB2	P04626	2	EBI-1341,EBI-641062
LCK	P06239	2	EBI-1341,EBI-1348
Lck	P06240	2	EBI-1341,EBI-1401	From a different organism.
TEK	Q02763	3	EBI-1341,EBI-2257090

Alternative products

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

Note: At least 8 isoforms are produced.

Isoform 1 (identifier: P08575-1)

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: P08575-2)

The sequence of this isoform differs from the canonical sequence as follows:
     32-192: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Chain

24 – 1304

1281

Receptor-type tyrosine-protein phosphatase C

PRO_0000025470

Regions

Topological domain

24 – 575

552

Extracellular Potential

Transmembrane

576 – 597

22

Helical; Potential

Topological domain

598 – 1304

707

Cytoplasmic Potential

Domain

390 – 478

89

Fibronectin type-III 1

Domain

482 – 570

89

Fibronectin type-III 2

Domain

651 – 910

260

Tyrosine-protein phosphatase 1

Domain

942 – 1226

285

Tyrosine-protein phosphatase 2

Region

851 – 857

7

Substrate binding By similarity

Sites

Active site

851

1

Phosphocysteine intermediate

Active site

1167

1

Phosphocysteine intermediate By similarity

Binding site

819

1

Substrate By similarity

Binding site

895

1

Substrate By similarity

Amino acid modifications

Modified residue

951

1

Phosphoserine By similarity

Modified residue

973

1

Phosphoserine Ref.10 Ref.13

Modified residue

1297

1

Phosphoserine Ref.13

Glycosylation

78

1

N-linked (GlcNAc...) Potential

Glycosylation

90

1

N-linked (GlcNAc...) Potential

Glycosylation

95

1

N-linked (GlcNAc...) Potential

Glycosylation

184

1

N-linked (GlcNAc...) Potential

Glycosylation

190

1

N-linked (GlcNAc...) Potential

Glycosylation

197

1

N-linked (GlcNAc...) Potential

Glycosylation

232

1

N-linked (GlcNAc...) Ref.11 Ref.12

Glycosylation

240

1

N-linked (GlcNAc...) Ref.12

Glycosylation

260

1

N-linked (GlcNAc...) Potential

Glycosylation

270

1

N-linked (GlcNAc...) Potential

Glycosylation

276

1

N-linked (GlcNAc...) Ref.12

Glycosylation

284

1

N-linked (GlcNAc...) Ref.12

Glycosylation

335

1

N-linked (GlcNAc...) Ref.11 Ref.12

Glycosylation

378

1

N-linked (GlcNAc...) Potential

Glycosylation

419

1

N-linked (GlcNAc...) Ref.12

Glycosylation

468

1

N-linked (GlcNAc...) Potential

Glycosylation

488

1

N-linked (GlcNAc...) Ref.12

Glycosylation

497

1

N-linked (GlcNAc...) Ref.12

Glycosylation

529

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

32 – 192

161

Missing in isoform 2.

VSP_007780

Natural variant

191

1

T → A.
Corresponds to variant rs4915154 [ dbSNP | Ensembl ].

VAR_036860

Natural variant

228

1

E → A in a breast cancer sample; somatic mutation. Ref.18

VAR_035653

Natural variant

294

1

I → L.
Corresponds to variant rs2230606 [ dbSNP | Ensembl ].

VAR_051763

Natural variant

362 – 363

2

Missing in T(-)B(+)NK(+) SCID; associated with lack of surface expression.

VAR_021205

Natural variant

421

1

T → I.
Corresponds to variant rs6696162 [ dbSNP | Ensembl ].

VAR_051764

Natural variant

568

1

H → Q.
Corresponds to variant rs12136658 [ dbSNP | Ensembl ].

VAR_051765

Natural variant

863

1

G → R in a breast cancer sample; somatic mutation. Ref.18

VAR_035654

Natural variant

1283

1

S → R.
Corresponds to variant rs2298872 [ dbSNP | Ensembl ].

VAR_020303

Experimental info

Mutagenesis

851

1

C → S: Loss of activity. Abolishes interaction with SKAP1. Ref.8

Sequence conflict

650

1

L → P in CAA68669. Ref.1

Sequence conflict

1207

1

P → L in CAA68669. Ref.1

Secondary structure

1

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1304

Helix Strand Turn

Details...

Turn

633 – 635

3

Helix

636 – 656

21

Beta strand

663 – 665

3

Turn

668 – 670

3

Helix

673 – 678

6

Turn

688 – 690

3

Beta strand

691 – 693

3

Beta strand

698 – 700

3

Turn

701 – 704

4

Beta strand

705 – 711

7

Beta strand

714 – 716

3

Beta strand

720 – 723

4

Turn

728 – 730

3

Helix

731 – 740

10

Beta strand

745 – 748

4

Beta strand

752 – 754

3

Beta strand

757 – 759

3

Turn

767 – 769

3

Beta strand

771 – 774

4

Beta strand

777 – 786

10

Beta strand

788 – 802

15

Beta strand

807 – 814

8

Helix

826 – 836

11

Beta strand

847 – 850

4

Beta strand

852 – 855

4

Helix

856 – 869

14

Helix

871 – 874

4

Beta strand

875 – 877

3

Helix

879 – 887

9

Helix

897 – 913

17

Helix

920 – 922

3

Helix

923 – 930

8

Helix

941 – 948

8

Helix

960 – 962

3

Helix

966 – 968

3

Turn

979 – 981

3

Beta strand

1018 – 1022

5

Beta strand

1029 – 1034

6

Turn

1038 – 1040

3

Helix

1041 – 1050

10

Beta strand

1055 – 1058

4

Beta strand

1062 – 1064

3

Beta strand

1067 – 1070

4

Beta strand

1088 – 1093

6

Beta strand

1095 – 1105

11

Beta strand

1113 – 1120

8

Beta strand

1125 – 1127

3

Helix

1132 – 1143

12

Beta strand

1163 – 1171

9

Helix

1174 – 1189

16

Beta strand

1190 – 1192

3

Helix

1195 – 1205

11

Turn

1207 – 1210

4

Helix

1213 – 1225

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 19, 2003. Version 2. Checksum: A08FC22D6069BAF7	FASTA	1,304	147,254
	10 20 30 40 50 60 MYLWLKLLAF GFAFLDTEVF VTGQSPTPSP TGLTTAKMPS VPLSSDPLPT HTTAFSPAST 70 80 90 100 110 120 FERENDFSET TTSLSPDNTS TQVSPDSLDN ASAFNTTGVS SVQTPHLPTH ADSQTPSAGT 130 140 150 160 170 180 DTQTFSGSAA NAKLNPTPGS NAISDVPGER STASTFPTDP VSPLTTTLSL AHHSSAALPA 190 200 210 220 230 240 RTSNTTITAN TSDAYLNASE TTTLSPSGSA VISTTTIATT PSKPTCDEKY ANITVDYLYN 250 260 270 280 290 300 KETKLFTAKL NVNENVECGN NTCTNNEVHN LTECKNASVS ISHNSCTAPD KTLILDVPPG 310 320 330 340 350 360 VEKFQLHDCT QVEKADTTIC LKWKNIETFT CDTQNITYRF QCGNMIFDNK EIKLENLEPE 370 380 390 400 410 420 HEYKCDSEIL YNNHKFTNAS KIIKTDFGSP GEPQIIFCRS EAAHQGVITW NPPQRSFHNF 430 440 450 460 470 480 TLCYIKETEK DCLNLDKNLI KYDLQNLKPY TKYVLSLHAY IIAKVQRNGS AAMCHFTTKS 490 500 510 520 530 540 APPSQVWNMT VSMTSDNSMH VKCRPPRDRN GPHERYHLEV EAGNTLVRNE SHKNCDFRVK 550 560 570 580 590 600 DLQYSTDYTF KAYFHNGDYP GEPFILHHST SYNSKALIAF LAFLIIVTSI ALLVVLYKIY 610 620 630 640 650 660 DLHKKRSCNL DEQQELVERD DEKQLMNVEP IHADILLETY KRKIADEGRL FLAEFQSIPR 670 680 690 700 710 720 VFSKFPIKEA RKPFNQNKNR YVDILPYDYN RVELSEINGD AGSNYINASY IDGFKEPRKY 730 740 750 760 770 780 IAAQGPRDET VDDFWRMIWE QKATVIVMVT RCEEGNRNKC AEYWPSMEEG TRAFGDVVVK 790 800 810 820 830 840 INQHKRCPDY IIQKLNIVNK KEKATGREVT HIQFTSWPDH GVPEDPHLLL KLRRRVNAFS 850 860 870 880 890 900 NFFSGPIVVH CSAGVGRTGT YIGIDAMLEG LEAENKVDVY GYVVKLRRQR CLMVQVEAQY 910 920 930 940 950 960 ILIHQALVEY NQFGETEVNL SELHPYLHNM KKRDPPSEPS PLEAEFQRLP SYRSWRTQHI 970 980 990 1000 1010 1020 GNQEENKSKN RNSNVIPYDY NRVPLKHELE MSKESEHDSD ESSDDDSDSE EPSKYINASF 1030 1040 1050 1060 1070 1080 IMSYWKPEVM IAAQGPLKET IGDFWQMIFQ RKVKVIVMLT ELKHGDQEIC AQYWGEGKQT 1090 1100 1110 1120 1130 1140 YGDIEVDLKD TDKSSTYTLR VFELRHSKRK DSRTVYQYQY TNWSVEQLPA EPKELISMIQ 1150 1160 1170 1180 1190 1200 VVKQKLPQKN SSEGNKHHKS TPLLIHCRDG SQQTGIFCAL LNLLESAETE EVVDIFQVVK 1210 1220 1230 1240 1250 1260 ALRKARPGMV STFEQYQFLY DVIASTYPAQ NGQVKKNNHQ EDKIEFDNEV DKVKQDANCV 1270 1280 1290 1300 NPLGAPEKLP EAKEQAEGSE PTSGTEGPEH SVNGPASPAL NQGS
	Isoform 2 [UniParc]. Checksum: DB4B4400F3602B3C	FASTA	1,143	130,898
	10 20 30 40 50 60 MYLWLKLLAF GFAFLDTEVF VTGQSPTPSP TDAYLNASET TTLSPSGSAV ISTTTIATTP 70 80 90 100 110 120 SKPTCDEKYA NITVDYLYNK ETKLFTAKLN VNENVECGNN TCTNNEVHNL TECKNASVSI 130 140 150 160 170 180 SHNSCTAPDK TLILDVPPGV EKFQLHDCTQ VEKADTTICL KWKNIETFTC DTQNITYRFQ 190 200 210 220 230 240 CGNMIFDNKE IKLENLEPEH EYKCDSEILY NNHKFTNASK IIKTDFGSPG EPQIIFCRSE 250 260 270 280 290 300 AAHQGVITWN PPQRSFHNFT LCYIKETEKD CLNLDKNLIK YDLQNLKPYT KYVLSLHAYI 310 320 330 340 350 360 IAKVQRNGSA AMCHFTTKSA PPSQVWNMTV SMTSDNSMHV KCRPPRDRNG PHERYHLEVE 370 380 390 400 410 420 AGNTLVRNES HKNCDFRVKD LQYSTDYTFK AYFHNGDYPG EPFILHHSTS YNSKALIAFL 430 440 450 460 470 480 AFLIIVTSIA LLVVLYKIYD LHKKRSCNLD EQQELVERDD EKQLMNVEPI HADILLETYK 490 500 510 520 530 540 RKIADEGRLF LAEFQSIPRV FSKFPIKEAR KPFNQNKNRY VDILPYDYNR VELSEINGDA 550 560 570 580 590 600 GSNYINASYI DGFKEPRKYI AAQGPRDETV DDFWRMIWEQ KATVIVMVTR CEEGNRNKCA 610 620 630 640 650 660 EYWPSMEEGT RAFGDVVVKI NQHKRCPDYI IQKLNIVNKK EKATGREVTH IQFTSWPDHG 670 680 690 700 710 720 VPEDPHLLLK LRRRVNAFSN FFSGPIVVHC SAGVGRTGTY IGIDAMLEGL EAENKVDVYG 730 740 750 760 770 780 YVVKLRRQRC LMVQVEAQYI LIHQALVEYN QFGETEVNLS ELHPYLHNMK KRDPPSEPSP 790 800 810 820 830 840 LEAEFQRLPS YRSWRTQHIG NQEENKSKNR NSNVIPYDYN RVPLKHELEM SKESEHDSDE 850 860 870 880 890 900 SSDDDSDSEE PSKYINASFI MSYWKPEVMI AAQGPLKETI GDFWQMIFQR KVKVIVMLTE 910 920 930 940 950 960 LKHGDQEICA QYWGEGKQTY GDIEVDLKDT DKSSTYTLRV FELRHSKRKD SRTVYQYQYT 970 980 990 1000 1010 1020 NWSVEQLPAE PKELISMIQV VKQKLPQKNS SEGNKHHKST PLLIHCRDGS QQTGIFCALL 1030 1040 1050 1060 1070 1080 NLLESAETEE VVDIFQVVKA LRKARPGMVS TFEQYQFLYD VIASTYPAQN GQVKKNNHQE 1090 1100 1110 1120 1130 1140 DKIEFDNEVD KVKQDANCVN PLGAPEKLPE AKEQAEGSEP TSGTEGPEHS VNGPASPALN QGS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential usage of three exons generates at least five different mRNAs encoding human leukocyte common antigens." Streuli M., Hall L.R., Saga Y., Schlossman S.F., Saito H. J. Exp. Med. 166:1548-1566(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING. Tissue: Lymphocyte.
[2]	"Structural variants of human T200 glycoprotein (leukocyte-common antigen)." Ralph S.J., Thomas M.L., Morton C.C., Trowbridge I.S. EMBO J. 6:1251-1257(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Synovium.
[4]	"Integrity of the exon 6 sequence is essential for tissue-specific alternative splicing of human leukocyte common antigen pre-mRNA." Tsai A.Y.M., Streuli M., Saito H. Mol. Cell. Biol. 9:4550-4555(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-192.
[5]	"Complete exon-intron organization of the human leukocyte common antigen (CD45) gene." Hall L.R., Streuli M., Schlossman S.F., Saito H. J. Immunol. 141:2781-2787(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-1304. Tissue: Placenta.
[6]	"The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase." Charbonneau H., Tonks N.K., Walsh K.A., Fischer E.H. Proc. Natl. Acad. Sci. U.S.A. 85:7182-7186(1988) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR." Streuli M., Krueger N.X., Thai T., Tang M., Saito H. EMBO J. 9:2399-2407(1990) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[8]	"SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated gene transcription." Wu L., Fu J., Shen S.-H. Mol. Cell. Biol. 22:2673-2686(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SKAP1, MUTAGENESIS OF CYS-851, FUNCTION.
[9]	"A role for interleukin-12 in the regulation of T cell plasma membrane compartmentation." Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R., Cordero O.J., Nogueira M. J. Biol. Chem. 278:24849-24857(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DPP4, SUBCELLULAR LOCATION.
[10]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973, MASS SPECTROMETRY. Tissue: T-cell.
[11]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232 AND ASN-335, MASS SPECTROMETRY. Tissue: Liver.
[12]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232; ASN-240; ASN-276; ASN-284; ASN-335; ASN-419; ASN-488 AND ASN-497, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973 AND SER-1297, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45." Nam H.J., Poy F., Saito H., Frederick C.A. J. Exp. Med. 201:441-452(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 622-1231 ALONE AND IN COMPLEX WITH PHOSPHOPEPTIDE.
[16]	"A point mutation in PTPRC is associated with the development of multiple sclerosis." Jacobsen M., Schweer D., Ziegler A., Gaber R., Schock S., Schwinzer R., Wonigeit K., Lindert R.-B., Kantarci O., Schaefer-Klein J., Schipper H.I., Oertel W.H., Heidenreich F., Weinshenker B.G., Sommer N., Hemmer B. Nat. Genet. 26:495-499(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MS SUSCEPTIBILITY.
[17]	"A deletion in the gene encoding the CD45 antigen in a patient with SCID." Tchilian E.Z., Wallace D.L., Wells R.S., Flower D.R., Morgan G., Beverley P.C.L. J. Immunol. 166:1308-1313(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT T(-)B(+)NK(+) SCID 362-GLU-TYR-363 DEL, CHARACTERIZATION OF VARIANT T(-)B(+)NK(+) SCID 362-GLU-TYR-363 DEL.
[18]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-228 AND ARG-863.
+	Additional computationally mapped references.

Web resources

PTPRCbase

PTPRC mutation db

Wikipedia

CD45 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00638 mRNA. Translation: CAA68669.1.
Y00062 mRNA. Translation: CAA68269.1.
AK292131 mRNA. Translation: BAF84820.1.
M23492 , M23496, M23466, M23467, M23468, M23469, M23470, M23471, M23472, M23473, M23474, M23475, M23476, M23477, M23478, M23479, M23480, M23481, M23482, M23483, M23484, M23485, M23486, M23487, M23488, M23489, M23490, M23491 Genomic DNA. Translation: AAD15273.2.

IPI

IPI00155168.
IPI00844079.

PIR

A46546.

RefSeq

NP_002829.3. NM_002838.4.
NP_563578.2. NM_080921.3.

UniGene

Hs.654514.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YGR	X-ray	2.90	A/B	622-1231	[»]
1YGU	X-ray	2.90	A/B	622-1231	[»]

ProteinModelPortal

P08575.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-224N.

IntAct

P08575. 34 interactions.

MINT

MINT-1130341.

STRING

9606.ENSP00000356346.

PTM databases

GlycoSuiteDB

P08575.

PhosphoSite

P08575.

Polymorphism databases

DMDM

33112650.

Proteomic databases

PaxDb

P08575.

PRIDE

P08575.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367376; ENSP00000356346; ENSG00000081237.
ENST00000573477; ENSP00000461074; ENSG00000262418.
ENST00000573679; ENSP00000458322; ENSG00000262418.
ENST00000594404; ENSP00000471843; ENSG00000081237.

GeneID

5788.

KEGG

hsa:5788.

UCSC

uc001gur.1. human.
uc001gut.1. human.

Organism-specific databases

CTD

5788.

GeneCards

GC01P198607.

HGNC

HGNC:9666. PTPRC.

HPA

CAB000052.
CAB002800.
CAB056154.
HPA000440.

MIM

126200. phenotype.
151460. gene.
608971. phenotype.

neXtProt

NX_P08575.

Orphanet

169157. Severe combined immunodeficiency T- B+ due to CD45 deficiency.

PharmGKB

PA34011.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5599.

HOGENOM

HOG000049064.

HOVERGEN

HBG000066.

InParanoid

P08575.

KO

K06478.

OrthoDB

EOG4MPHPN.

PhylomeDB

P08575.

Enzyme and pathway databases

Pathway_Interaction_DB

bcr_5pathway. BCR signaling pathway.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.

Reactome

REACT_111045. Developmental Biology.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P08575.

Bgee

P08575.

CleanEx

HS_PTPRC.

Genevestigator

P08575.

GermOnline

ENSG00000081237. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR016335. Leukocyte_common_ag.
IPR024739. PTP_recept_N.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Pfam

PF12567. CD45. 1 hit.
PF00041. fn3. 2 hits.
PF12453. PTP_N. 2 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]

PIRSF

PIRSF002004. Leukocyte_common_antigen. 1 hit.

PRINTS

PR00700. PRTYPHPHTASE.

SMART

SM00060. FN3. 2 hits.
SM00194. PTPc. 2 hits.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 2 hits.

PROSITE

PS50853. FN3. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P08575.

ChEMBL

CHEMBL3243.

ChiTaRS

PTPRC. human.

EvolutionaryTrace

P08575.

GenomeRNAi

5788.

NextBio

22518.

SOURCE

Search...

Entry information

Entry name

PTPRC_HUMAN

Accession

Primary (citable) accession number: P08575
Secondary accession number(s): A8K7W6, Q16614, Q9H0Y6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	July 19, 2003
Last modified:	May 1, 2013
This is version 159 of the entry and version 2 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.