Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q12923 (PTN13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 157. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase non-receptor type 13

EC=3.1.3.48
Alternative name(s):
Fas-associated protein-tyrosine phosphatase 1
Short name=FAP-1
PTP-BAS
Protein-tyrosine phosphatase 1E
Short name=PTP-E1
Short name=hPTPE1
Protein-tyrosine phosphatase PTPL1
Gene names
Name:PTPN13
Synonyms:PNP1, PTP1E, PTPL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2485 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling. Ref.18

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with TRIP6 and TNFRSF6 (Fas receptor) through its second PDZ domain. Interacts with the C-terminal SVP motif of NGFR through its third PDZ domain. Interacts with the LIM domain of PDLIM4 through its second and fourth PDZ domains. Binds PLEKHA1 and PLEKHA2 through its first PDZ domain. Interacts with BRD7 and ARHGAP29. Interacts (via PDZ 3 domain) with PKN2 (via C-terminus). Ref.7 Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Cytoplasmcytoskeleton By similarity. Nucleus. Cell projectionlamellipodium. Note: Colocalizes with PKN2 in lamellipodia-like structure, regions of large actin turnover. Ref.11

Tissue specificity

Present in most tissues with the exception of the liver and skeletal muscle. Most abundant in lung, kidney and fetal brain.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily.

Contains 1 FERM domain.

Contains 1 KIND domain.

Contains 5 PDZ (DHR) domains.

Contains 1 tyrosine-protein phosphatase domain.

Sequence caution

The sequence AAH39610.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12923-1)

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: Q12923-2)

The sequence of this isoform differs from the canonical sequence as follows:
     884-1074: Missing.
Isoform 3 (identifier: Q12923-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1056-1074: Missing.
Isoform 4 (identifier: Q12923-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1383-1383: T → TVLFDK
Note: May be due to a competing donor splice site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24852485Tyrosine-protein phosphatase non-receptor type 13
PRO_0000219435

Regions

Domain3 – 190188KIND
Domain572 – 872301FERM
Domain1093 – 117886PDZ 1
Domain1368 – 145285PDZ 2
Domain1501 – 158888PDZ 3
Domain1788 – 186881PDZ 4
Domain1882 – 196584PDZ 5
Domain2213 – 2467255Tyrosine-protein phosphatase
Region2408 – 24147Substrate
Region2408 – 24147Substrate binding By similarity
Coiled coil469 – 50436 Potential
Compositional bias56 – 594Poly-Leu
Compositional bias1742 – 17498Poly-Ser

Sites

Active site24081Phosphocysteine intermediate Probable
Binding site23781Substrate
Binding site24521Substrate By similarity

Amino acid modifications

Modified residue10291Phosphoserine Ref.15
Modified residue10331Phosphoserine Ref.15

Natural variations

Alternative sequence884 – 1074191Missing in isoform 2.
VSP_000496
Alternative sequence1056 – 107419Missing in isoform 3.
VSP_000497
Alternative sequence13831T → TVLFDK in isoform 4.
VSP_007921
Natural variant13561F → L.
Corresponds to variant rs10033029 [ dbSNP | Ensembl ].
VAR_048359
Natural variant14191L → P. Ref.19
VAR_016200
Natural variant15221I → M. Ref.19
Corresponds to variant rs2230600 [ dbSNP | Ensembl ].
VAR_016201
Natural variant16251E → K.
Corresponds to variant rs12500797 [ dbSNP | Ensembl ].
VAR_024373
Natural variant17441S → P.
Corresponds to variant rs17012064 [ dbSNP | Ensembl ].
VAR_048360
Natural variant20811Y → D.
Corresponds to variant rs989902 [ dbSNP | Ensembl ].
VAR_024374
Natural variant24581I → V No effect on substrate affinity. Ref.18
Corresponds to variant rs34226837 [ dbSNP | Ensembl ].
VAR_048361

Experimental info

Mutagenesis21541D → H: No effect on substrate affinity. Ref.18
Mutagenesis22051R → W: No effect on substrate affinity. Ref.18
Mutagenesis22211Q → M: Reduces substrate affinity 2 fold. Ref.18
Mutagenesis23071M → T: Reduces substrate affinity 7 fold. Ref.18
Mutagenesis24081C → S: Loss of catalytic activity. Ref.18
Mutagenesis24441R → E: Loss of catalytic activity. Ref.18
Mutagenesis24441R → K: Reduces substrate affinity 7 fold. Ref.18
Mutagenesis24441R → Q: Strongly decreases catalytic activity. Ref.18
Mutagenesis24481H → A: Reduces substrate affinity 2 fold. Ref.18
Mutagenesis24491G → V: Loss of catalytic activity. Ref.18
Mutagenesis24741E → D: No effect on substrate affinity. Ref.18
Sequence conflict1134 – 11352LD → FH in CAA56563. Ref.3
Sequence conflict1216 – 122914KDHHW…LRHIS → DLSRSHCHVYLAHL Ref.5
Sequence conflict1238 – 12392GL → A in CAA56124. Ref.5
Sequence conflict13571S → P in CAA56124. Ref.5
Sequence conflict1362 – 13632KP → RS in CAA56124. Ref.5
Sequence conflict15381P → A in CAA56563. Ref.3
Sequence conflict16491R → K in CAA56124. Ref.5
Sequence conflict1698 – 171417KSQED…YPQKI → RVKKIPFVPCFTILRKR in CAA56124. Ref.5
Sequence conflict17971G → A in CAA56563. Ref.3
Sequence conflict1856 – 18572AA → G in CAA56124. Ref.5
Sequence conflict20691A → S in CAA56124. Ref.5
Sequence conflict2206 – 22105GLLDQ → VARS in CAA56124. Ref.5

Secondary structure

.............................................................. 2485
Helix Strand Turn

Details...

Sequences

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

Last modified December 1, 2000. Version 2.
Checksum: 8D1B31597C66962B

FASTA2,485276,906
        10         20         30         40         50         60 
MHVSLAEALE VRGGPLQEEE IWAVLNQSAE SLQELFRKVS LADPAALGFI ISPWSLLLLP 

        70         80         90        100        110        120 
SGSVSFTDEN ISNQDLRAFT APEVLQNQSL TSLSDVEKIH IYSLGMTLYW GADYEVPQSQ 

       130        140        150        160        170        180 
PIKLGDHLNS ILLGMCEDVI YARVSVRTVL DACSAHIRNS NCAPSFSYVK HLVKLVLGNL 

       190        200        210        220        230        240 
SGTDQLSCNS EQKPDRSQAI RDRLRGKGLP TGRSSTSDVL DIQKPPLSHQ TFLNKGLSKS 

       250        260        270        280        290        300 
MGFLSIKDTQ DENYFKDILS DNSGREDSEN TFSPYQFKTS GPEKKPIPGI DVLSKKKIWA 

       310        320        330        340        350        360 
SSMDLLCTAD RDFSSGETAT YRRCHPEAVT VRTSTTPRKK EARYSDGSIA LDIFGPQKMD 

       370        380        390        400        410        420 
PIYHTRELPT SSAISSALDR IRERQKKLQV LREAMNVEEP VRRYKTYHGD VFSTSSESPS 

       430        440        450        460        470        480 
IISSESDFRQ VRRSEASKRF ESSSGLPGVD ETLSQGQSQR PSRQYETPFE GNLINQEIML 

       490        500        510        520        530        540 
KRQEEELMQL QAKMALRQSR LSLYPGDTIK ASMLDITRDP LREIALETAM TQRKLRNFFG 

       550        560        570        580        590        600 
PEFVKMTIEP FISLDLPRSI LTKKGKNEDN RRKVNIMLLN GQRLELTCDT KTICKDVFDM 

       610        620        630        640        650        660 
VVAHIGLVEH HLFALATLKD NEYFFVDPDL KLTKVAPEGW KEEPKKKTKA TVNFTLFFRI 

       670        680        690        700        710        720 
KFFMDDVSLI QHTLTCHQYY LQLRKDILEE RMHCDDETSL LLASLALQAE YGDYQPEVHG 

       730        740        750        760        770        780 
VSYFRMEHYL PARVMEKLDL SYIKEELPKL HNTYVGASEK ETELEFLKVC QRLTEYGVHF 

       790        800        810        820        830        840 
HRVHPEKKSQ TGILLGVCSK GVLVFEVHNG VRTLVLRFPW RETKKISFSK KKITLQNTSD 

       850        860        870        880        890        900 
GIKHGFQTDN SKICQYLLHL CSYQHKFQLQ MRARQSNQDA QDIERASFRS LNLQAESVRG 

       910        920        930        940        950        960 
FNMGRAISTG SLASSTLNKL AVRPLSVQAE ILKRLSCSEL SLYQPLQNSS KEKNDKASWE 

       970        980        990       1000       1010       1020 
EKPREMSKSY HDLSQASLYP HRKNVIVNME PPPQTVAELV GKPSHQMSRS DAESLAGVTK 

      1030       1040       1050       1060       1070       1080 
LNNSKSVASL NRSPERRKHE SDSSSIEDPG QAYVLGMTMH SSGNSSSQVP LKENDVLHKR 

      1090       1100       1110       1120       1130       1140 
WSIVSSPERE ITLVNLKKDA KYGLGFQIIG GEKMGRLDLG IFISSVAPGG PADLDGCLKP 

      1150       1160       1170       1180       1190       1200 
GDRLISVNSV SLEGVSHHAA IEILQNAPED VTLVISQPKE KISKVPSTPV HLTNEMKNYM 

      1210       1220       1230       1240       1250       1260 
KKSSYMQDSA IDSSSKDHHW SRGTLRHISE NSFGPSGGLR EGSLSSQDSR TESASLSQSQ 

      1270       1280       1290       1300       1310       1320 
VNGFFASHLG DQTWQESQHG SPSPSVISKA TEKETFTDSN QSKTKKPGIS DVTDYSDRGD 

      1330       1340       1350       1360       1370       1380 
SDMDEATYSS SQDHQTPKQE SSSSVNTSNK MNFKTFSSSP PKPGDIFEVE LAKNDNSLGI 

      1390       1400       1410       1420       1430       1440 
SVTGGVNTSV RHGGIYVKAV IPQGAAESDG RIHKGDRVLA VNGVSLEGAT HKQAVETLRN 

      1450       1460       1470       1480       1490       1500 
TGQVVHLLLE KGQSPTSKEH VPVTPQCTLS DQNAQGQGPE KVKKTTQVKD YSFVTEENTF 

      1510       1520       1530       1540       1550       1560 
EVKLFKNSSG LGFSFSREDN LIPEQINASI VRVKKLFPGQ PAAESGKIDV GDVILKVNGA 

      1570       1580       1590       1600       1610       1620 
SLKGLSQQEV ISALRGTAPE VFLLLCRPPP GVLPEIDTAL LTPLQSPAQV LPNSSKDSSQ 

      1630       1640       1650       1660       1670       1680 
PSCVEQSTSS DENEMSDKSK KQCKSPSRRD SYSDSSGSGE DDLVTAPANI SNSTWSSALH 

      1690       1700       1710       1720       1730       1740 
QTLSNMVSQA QSHHEAPKSQ EDTICTMFYY PQKIPNKPEF EDSNPSPLPP DMAPGQSYQP 

      1750       1760       1770       1780       1790       1800 
QSESASSSSM DKYHIHHISE PTRQENWTPL KNDLENHLED FELEVELLIT LIKSEKGSLG 

      1810       1820       1830       1840       1850       1860 
FTVTKGNQRI GCYVHDVIQD PAKSDGRLKP GDRLIKVNDT DVTNMTHTDA VNLLRAASKT 

      1870       1880       1890       1900       1910       1920 
VRLVIGRVLE LPRIPMLPHL LPDITLTCNK EELGFSLCGG HDSLYQVVYI SDINPRSVAA 

      1930       1940       1950       1960       1970       1980 
IEGNLQLLDV IHYVNGVSTQ GMTLEEVNRA LDMSLPSLVL KATRNDLPVV PSSKRSAVSA 

      1990       2000       2010       2020       2030       2040 
PKSTKGNGSY SVGSCSQPAL TPNDSFSTVA GEEINEISYP KGKCSTYQIK GSPNLTLPKE 

      2050       2060       2070       2080       2090       2100 
SYIQEDDIYD DSQEAEVIQS LLDVVDEEAQ NLLNENNAAG YSCGPGTLKM NGKLSEERTE 

      2110       2120       2130       2140       2150       2160 
DTDCDGSPLP EYFTEATKMN GCEEYCEEKV KSESLIQKPQ EKKTDDDEIT WGNDELPIER 

      2170       2180       2190       2200       2210       2220 
TNHEDSDKDH SFLTNDELAV LPVVKVLPSG KYTGANLKSV IRVLRGLLDQ GIPSKELENL 

      2230       2240       2250       2260       2270       2280 
QELKPLDQCL IGQTKENRRK NRYKNILPYD ATRVPLGDEG GYINASFIKI PVGKEEFVYI 

      2290       2300       2310       2320       2330       2340 
ACQGPLPTTV GDFWQMIWEQ KSTVIAMMTQ EVEGEKIKCQ RYWPNILGKT TMVSNRLRLA 

      2350       2360       2370       2380       2390       2400 
LVRMQQLKGF VVRAMTLEDI QTREVRHISH LNFTAWPDHD TPSQPDDLLT FISYMRHIHR 

      2410       2420       2430       2440       2450       2460 
SGPIITHCSA GIGRSGTLIC IDVVLGLISQ DLDFDISDLV RCMRLQRHGM VQTEDQYIFC 

      2470       2480 
YQVILYVLTR LQAEEEQKQQ PQLLK 

« Hide

Isoform 2 [UniParc].

Checksum: ABBFA4BCD60FF56F
Show »

FASTA2,294255,926
Isoform 3 [UniParc].

Checksum: 5BDCC226F2DEC19D
Show »

FASTA2,466274,932
Isoform 4 [UniParc].

Checksum: 8D1FE03D9738A247
Show »

FASTA2,490277,508

References

« Hide 'large scale' references
[1]"A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases."
Banville D., Ahmad S., Stocco R., Shen S.-H.
J. Biol. Chem. 269:22320-22327(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Mammary carcinoma.
[2]"Molecular cloning of a novel protein-tyrosine phosphatase containing a membrane-binding domain and GLGF repeats."
Maekawa K., Imagawa N., Nagamatsu M., Harada S.
FEBS Lett. 337:200-206(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING.
Tissue: Leukemia.
[3]"Cloning and characterization of PTPL1, a protein tyrosine phosphatase with similarities to cytoskeletal-associated proteins."
Saras J., Claesson-Welsh L., Heldin C.-H., Gonez L.J.
J. Biol. Chem. 269:24082-24089(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Fibroblast.
[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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1323-1922 (ISOFORM 1).
Tissue: Brain and Eye.
[5]Wang H.-Y.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1216-2485 (ISOFORMS 1/2/3).
Tissue: Pancreas.
[6]"FAP-1: a protein tyrosine phosphatase that associates with Fas."
Sato T., Irie S., Kitada S., Reed J.C.
Science 268:411-415(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1279-1883 (ISOFORM 4).
Tissue: Brain.
[7]"Functional interaction of Fas-associated phosphatase-1 (FAP-1) with p75(NTR) and their effect on NF-kappaB activation."
Irie S., Hachiya T., Rabizadeh S., Maruyama W., Mukai J., Li Y., Reed J.C., Bredesen D.E., Sato T.A.
FEBS Lett. 460:191-198(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1323-1821 (ISOFORMS 1/2/3), INTERACTION WITH NGFR.
[8]"Identification of novel protein-tyrosine phosphatases in a human leukemia cell line, F-36P."
Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.
Leukemia 7:742-746(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2298-2414.
Tissue: Leukemia.
[9]"A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1."
Saras J., Franzen P., Aspenstroem P., Hellman U., Gonez L.J., Heldin C.-H.
J. Biol. Chem. 272:24333-24338(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP29.
[10]"ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E."
Murthy K.K., Clark K., Fortin Y., Shen S.-H., Banville D.
J. Biol. Chem. 274:20679-20687(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIP6.
[11]"The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif."
Gross C., Heumann R., Erdmann K.S.
FEBS Lett. 496:101-104(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PKN2, SUBCELLULAR LOCATION.
[12]"Interaction of the protein tyrosine phosphatase PTPL1 with the PtdIns(3,4)P2-binding adaptor protein TAPP1."
Kimber W.A., Deak M., Prescott A.R., Alessi D.R.
Biochem. J. 376:525-535(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLEKHA1 AND PLEKHA2.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1033, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Solution structure of the PDZ2 domain from human phosphatase hPTP1E and its interactions with C-terminal peptides from the Fas receptor."
Kozlov G., Gehring K., Ekiel I.
Biochemistry 39:2572-2580(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1361-1456 UNCOMPLEXED AND IN COMPLEX WITH THE C-TERMINUS OF TNFRSF6.
[17]"Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the beta2-beta3 loop to PDZ domain-ligand interactions."
Kozlov G., Banville D., Gehring K., Ekiel I.
J. Mol. Biol. 320:813-820(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1361-1456 IN COMPLEX WITH THE C-TERMINUS OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR RA-GEF-2.
[18]"Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket."
Villa F., Deak M., Bloomberg G.B., Alessi D.R., van Aalten D.M.
J. Biol. Chem. 280:8180-8187(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2163-2477, FUNCTION, MUTAGENESIS OF ASP-2154; ARG-2205; GLN-2221; MET-2307; CYS-2408; ARG-2444; HIS-2448; GLY-2449 AND GLU-2474, CHARACTERIZATION OF VARIANT VAL-2458.
[19]"Head-to-head juxtaposition of Fas-associated phosphatase-1 (FAP-1) and c-Jun NH2-terminal kinase 3 (JNK3) genes: genomic structure and seven polymorphisms of the FAP-1 gene."
Yoshida S., Harada H., Nagai H., Fukino K., Teramoto A., Emi M.
J. Hum. Genet. 47:614-619(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PRO-1419 AND MET-1522.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12128 mRNA. Translation: AAB60339.1.
D21209 mRNA. Translation: BAA04750.1.
D21210 mRNA. Translation: BAA04751.1.
D21211 mRNA. Translation: BAA04752.1.
X80289 mRNA. Translation: CAA56563.1.
BC039610 mRNA. Translation: AAH39610.1. Sequence problems.
BC140777 mRNA. Translation: AAI40778.1.
X79676 mRNA. Translation: CAA56124.1.
L34583 mRNA. Translation: AAC41755.1.
AF233323 mRNA. Translation: AAF63474.1.
PIRA54971.
I67629.
I67630.
RefSeqNP_006255.1. NM_006264.2.
NP_542414.1. NM_080683.2.
NP_542415.1. NM_080684.2.
NP_542416.1. NM_080685.2.
UniGeneHs.436142.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D5GNMR-A1361-1456[»]
1Q7XNMR-A1358-1459[»]
1WCHX-ray1.85A2163-2477[»]
2M0ZNMR-A1361-1456[»]
2M10NMR-A1361-1456[»]
3LNXX-ray1.64A/B/C/D/E/F1361-1456[»]
3LNYX-ray1.30A1361-1456[»]
3PDZNMR-A1361-1456[»]
ProteinModelPortalQ12923.
SMRQ12923. Positions 2-174, 584-899, 1103-1174, 1361-1588, 1789-1964, 2170-2477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111747. 13 interactions.
IntActQ12923. 13 interactions.
MINTMINT-109571.

Chemistry

BindingDBQ12923.
ChEMBLCHEMBL2976.

PTM databases

PhosphoSiteQ12923.

Polymorphism databases

DMDM12643716.

Proteomic databases

PaxDbQ12923.
PRIDEQ12923.

Protocols and materials databases

DNASU5783.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316707; ENSP00000322675; ENSG00000163629. [Q12923-2]
ENST00000411767; ENSP00000407249; ENSG00000163629. [Q12923-1]
ENST00000427191; ENSP00000408368; ENSG00000163629. [Q12923-3]
ENST00000436978; ENSP00000394794; ENSG00000163629. [Q12923-4]
ENST00000511467; ENSP00000426626; ENSG00000163629. [Q12923-4]
GeneID5783.
KEGGhsa:5783.
UCSCuc003hpy.3. human. [Q12923-4]
uc003hpz.3. human. [Q12923-1]
uc003hqa.3. human. [Q12923-3]
uc003hqb.3. human. [Q12923-2]

Organism-specific databases

CTD5783.
GeneCardsGC04P087515.
HGNCHGNC:9646. PTPN13.
HPACAB002213.
MIM600267. gene.
neXtProtNX_Q12923.
PharmGKBPA33988.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOVERGENHBG053756.
InParanoidQ12923.
KOK02374.
OMAGCYVHDV.
OrthoDBEOG7K9K22.
TreeFamTF315388.

Gene expression databases

ArrayExpressQ12923.
BgeeQ12923.
GenevestigatorQ12923.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011019. KIND.
IPR001478. PDZ.
IPR011993. PH_like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR012153. Tyr_Pase_non-rcpt_typ-13.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PANTHERPTHR19134:SF197. PTHR19134:SF197. 1 hit.
PfamPF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00595. PDZ. 5 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFPIRSF000933. Tyr-Ptase_nr13. 1 hit.
PRINTSPR00935. BAND41.
PR00700. PRTYPHPHTASE.
SMARTSM00295. B41. 1 hit.
SM00750. KIND. 1 hit.
SM00228. PDZ. 5 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF50156. SSF50156. 5 hits.
PROSITEPS50057. FERM_3. 1 hit.
PS51377. KIND. 1 hit.
PS50106. PDZ. 5 hits.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN13. human.
EvolutionaryTraceQ12923.
GeneWikiPTPN13.
GenomeRNAi5783.
NextBio22492.
PROQ12923.
SOURCESearch...

Entry information

Entry namePTN13_HUMAN
AccessionPrimary (citable) accession number: Q12923
Secondary accession number(s): B2RTR0 expand/collapse secondary AC list , Q15159, Q15263, Q15264, Q15265, Q15674, Q16826, Q8IWH7, Q9NYN9, Q9UDA8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: March 19, 2014
This is version 157 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 4

Human chromosome 4: entries, gene names and cross-references to MIM