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Protein

Tyrosine-protein phosphatase non-receptor type 13

Gene

PTPN13

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

Functioni

Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling (PubMed:15611135). May regulate phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of PIK3R2 (PubMed:23604317).2 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei2378Substrate1
Active sitei2408Phosphocysteine intermediateCurated1
Binding sitei2452SubstrateBy similarity1

GO - Molecular functioni

  • phosphatidylinositol 3-kinase regulatory subunit binding Source: UniProtKB
  • protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  • peptidyl-tyrosine dephosphorylation Source: UniProtKB
  • protein dephosphorylation Source: UniProtKB
  • regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciZFISH:HS08898-MONOMER.
BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-1660499. Synthesis of PIPs at the plasma membrane.
SIGNORiQ12923.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PTPN13
Synonyms:PNP1, PTP1E, PTPL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:9646. PTPN13.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Nucleus 1 Publication
  • Cell projectionlamellipodium 1 Publication

  • Note: Colocalizes with PKN2 in lamellipodia-like structure, regions of large actin turnover.

GO - Cellular componenti

  • cell body Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • neuron projection Source: Ensembl
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2154D → H: No effect on substrate affinity. 1 Publication1
Mutagenesisi2205R → W: No effect on substrate affinity. 1 Publication1
Mutagenesisi2221Q → M: Reduces substrate affinity 2 fold. 1 Publication1
Mutagenesisi2307M → T: Reduces substrate affinity 7 fold. 1 Publication1
Mutagenesisi2408C → S: Loss of catalytic activity. 1 Publication1
Mutagenesisi2444R → E: Loss of catalytic activity. 1 Publication1
Mutagenesisi2444R → K: Reduces substrate affinity 7 fold. 1 Publication1
Mutagenesisi2444R → Q: Strongly decreases catalytic activity. 1 Publication1
Mutagenesisi2448H → A: Reduces substrate affinity 2 fold. 1 Publication1
Mutagenesisi2449G → V: Loss of catalytic activity. 1 Publication1
Mutagenesisi2474E → D: No effect on substrate affinity. 1 Publication1

Organism-specific databases

DisGeNETi5783.
OpenTargetsiENSG00000163629.
PharmGKBiPA33988.

Chemistry databases

ChEMBLiCHEMBL2976.

Polymorphism and mutation databases

BioMutaiPTPN13.
DMDMi12643716.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194351 – 2485Tyrosine-protein phosphatase non-receptor type 13Add BLAST2485

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei240PhosphoserineCombined sources1
Modified residuei301PhosphoserineBy similarity1
Modified residuei302PhosphoserineBy similarity1
Modified residuei890PhosphoserineCombined sources1
Modified residuei897PhosphoserineBy similarity1
Modified residuei908PhosphoserineCombined sources1
Modified residuei911PhosphoserineBy similarity1
Modified residuei914PhosphoserineBy similarity1
Modified residuei1029PhosphoserineCombined sources1
Modified residuei1033PhosphoserineCombined sources1
Modified residuei1085PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ12923.
MaxQBiQ12923.
PaxDbiQ12923.
PeptideAtlasiQ12923.
PRIDEiQ12923.

PTM databases

DEPODiQ12923.
iPTMnetiQ12923.
PhosphoSitePlusiQ12923.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000163629.
ExpressionAtlasiQ12923. baseline and differential.
GenevisibleiQ12923. HS.

Organism-specific databases

HPAiCAB002213.

Interactioni

Subunit structurei

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. Interacts with ARHGAP29. Interacts (via PDZ 3 domain) with PKN2 (via C-terminus). Interacts with PIK3R2; dephosphorylates PIK3R2 (PubMed:23604317). Interacts with FBXL2 (PubMed:23604317). Interacts with SDCCAG3 (PubMed:23108400).9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FASP254453EBI-355227,EBI-494743
PDCD10Q9BUL83EBI-355227,EBI-740195
RAPGEF6Q8TEU74EBI-355227,EBI-2693017

GO - Molecular functioni

  • phosphatidylinositol 3-kinase regulatory subunit binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111747. 22 interactors.
DIPiDIP-40449N.
IntActiQ12923. 20 interactors.
MINTiMINT-109571.
STRINGi9606.ENSP00000394794.

Chemistry databases

BindingDBiQ12923.

Structurei

Secondary structure

12485
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1366 – 1372Combined sources7
Beta strandi1374 – 1377Combined sources4
Beta strandi1379 – 1384Combined sources6
Beta strandi1385 – 1387Combined sources3
Beta strandi1388 – 1390Combined sources3
Helixi1391 – 1393Combined sources3
Beta strandi1395 – 1400Combined sources6
Helixi1405 – 1409Combined sources5
Beta strandi1417 – 1421Combined sources5
Helixi1431 – 1439Combined sources9
Beta strandi1443 – 1450Combined sources8
Helixi2175 – 2179Combined sources5
Beta strandi2188 – 2190Combined sources3
Helixi2194 – 2209Combined sources16
Helixi2212 – 2220Combined sources9
Helixi2231 – 2233Combined sources3
Helixi2235 – 2238Combined sources4
Turni2257 – 2260Combined sources4
Beta strandi2264 – 2272Combined sources9
Beta strandi2275 – 2282Combined sources8
Helixi2287 – 2289Combined sources3
Helixi2290 – 2299Combined sources10
Beta strandi2304 – 2307Combined sources4
Beta strandi2311 – 2313Combined sources3
Beta strandi2331 – 2346Combined sources16
Beta strandi2348 – 2359Combined sources12
Turni2360 – 2363Combined sources4
Beta strandi2364 – 2373Combined sources10
Helixi2385 – 2398Combined sources14
Beta strandi2404 – 2407Combined sources4
Beta strandi2409 – 2412Combined sources4
Helixi2413 – 2429Combined sources17
Helixi2436 – 2444Combined sources9
Helixi2454 – 2475Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ12923.
SMRiQ12923.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12923.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 190KINDPROSITE-ProRule annotationAdd BLAST188
Domaini572 – 872FERMPROSITE-ProRule annotationAdd BLAST301
Domaini1093 – 1178PDZ 1PROSITE-ProRule annotationAdd BLAST86
Domaini1368 – 1452PDZ 2PROSITE-ProRule annotationAdd BLAST85
Domaini1501 – 1588PDZ 3PROSITE-ProRule annotationAdd BLAST88
Domaini1788 – 1868PDZ 4PROSITE-ProRule annotationAdd BLAST81
Domaini1882 – 1965PDZ 5PROSITE-ProRule annotationAdd BLAST84
Domaini2213 – 2467Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST255

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2408 – 2414Substrate7
Regioni2408 – 2414Substrate bindingBy similarity7

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili469 – 504Sequence analysisAdd BLAST36

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi56 – 59Poly-Leu4
Compositional biasi1742 – 1749Poly-Ser8

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation
Contains 1 KIND domain.PROSITE-ProRule annotation
Contains 5 PDZ (DHR) domains.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0792. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00830000128259.
HOVERGENiHBG053756.
InParanoidiQ12923.
KOiK02374.
OMAiGCYVHDV.
OrthoDBiEOG091G0BZR.
PhylomeDBiQ12923.
TreeFamiTF315388.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 5 hits.
3.90.190.10. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011019. KIND_dom.
IPR001478. PDZ.
IPR011993. PH_dom-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR012153. PTPN13.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR19134:SF197. PTHR19134:SF197. 2 hits.
PfamiPF09380. 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]
PIRSFiPIRSF000933. Tyr-Ptase_nr13. 1 hit.
PRINTSiPR00935. BAND41.
PR00700. PRTYPHPHTASE.
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
SM00750. KIND. 1 hit.
SM00228. PDZ. 5 hits.
SM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50156. SSF50156. 5 hits.
SSF50729. SSF50729. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50057. 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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q12923-1) [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
MHVSLAEALE VRGGPLQEEE IWAVLNQSAE SLQELFRKVS LADPAALGFI
60 70 80 90 100
ISPWSLLLLP SGSVSFTDEN ISNQDLRAFT APEVLQNQSL TSLSDVEKIH
110 120 130 140 150
IYSLGMTLYW GADYEVPQSQ PIKLGDHLNS ILLGMCEDVI YARVSVRTVL
160 170 180 190 200
DACSAHIRNS NCAPSFSYVK HLVKLVLGNL SGTDQLSCNS EQKPDRSQAI
210 220 230 240 250
RDRLRGKGLP TGRSSTSDVL DIQKPPLSHQ TFLNKGLSKS MGFLSIKDTQ
260 270 280 290 300
DENYFKDILS DNSGREDSEN TFSPYQFKTS GPEKKPIPGI DVLSKKKIWA
310 320 330 340 350
SSMDLLCTAD RDFSSGETAT YRRCHPEAVT VRTSTTPRKK EARYSDGSIA
360 370 380 390 400
LDIFGPQKMD PIYHTRELPT SSAISSALDR IRERQKKLQV LREAMNVEEP
410 420 430 440 450
VRRYKTYHGD VFSTSSESPS IISSESDFRQ VRRSEASKRF ESSSGLPGVD
460 470 480 490 500
ETLSQGQSQR PSRQYETPFE GNLINQEIML KRQEEELMQL QAKMALRQSR
510 520 530 540 550
LSLYPGDTIK ASMLDITRDP LREIALETAM TQRKLRNFFG PEFVKMTIEP
560 570 580 590 600
FISLDLPRSI LTKKGKNEDN RRKVNIMLLN GQRLELTCDT KTICKDVFDM
610 620 630 640 650
VVAHIGLVEH HLFALATLKD NEYFFVDPDL KLTKVAPEGW KEEPKKKTKA
660 670 680 690 700
TVNFTLFFRI KFFMDDVSLI QHTLTCHQYY LQLRKDILEE RMHCDDETSL
710 720 730 740 750
LLASLALQAE YGDYQPEVHG VSYFRMEHYL PARVMEKLDL SYIKEELPKL
760 770 780 790 800
HNTYVGASEK ETELEFLKVC QRLTEYGVHF HRVHPEKKSQ TGILLGVCSK
810 820 830 840 850
GVLVFEVHNG VRTLVLRFPW RETKKISFSK KKITLQNTSD GIKHGFQTDN
860 870 880 890 900
SKICQYLLHL CSYQHKFQLQ MRARQSNQDA QDIERASFRS LNLQAESVRG
910 920 930 940 950
FNMGRAISTG SLASSTLNKL AVRPLSVQAE ILKRLSCSEL SLYQPLQNSS
960 970 980 990 1000
KEKNDKASWE EKPREMSKSY HDLSQASLYP HRKNVIVNME PPPQTVAELV
1010 1020 1030 1040 1050
GKPSHQMSRS DAESLAGVTK LNNSKSVASL NRSPERRKHE SDSSSIEDPG
1060 1070 1080 1090 1100
QAYVLGMTMH SSGNSSSQVP LKENDVLHKR WSIVSSPERE ITLVNLKKDA
1110 1120 1130 1140 1150
KYGLGFQIIG GEKMGRLDLG IFISSVAPGG PADLDGCLKP GDRLISVNSV
1160 1170 1180 1190 1200
SLEGVSHHAA IEILQNAPED VTLVISQPKE KISKVPSTPV HLTNEMKNYM
1210 1220 1230 1240 1250
KKSSYMQDSA IDSSSKDHHW SRGTLRHISE NSFGPSGGLR EGSLSSQDSR
1260 1270 1280 1290 1300
TESASLSQSQ VNGFFASHLG DQTWQESQHG SPSPSVISKA TEKETFTDSN
1310 1320 1330 1340 1350
QSKTKKPGIS DVTDYSDRGD SDMDEATYSS SQDHQTPKQE SSSSVNTSNK
1360 1370 1380 1390 1400
MNFKTFSSSP PKPGDIFEVE LAKNDNSLGI SVTGGVNTSV RHGGIYVKAV
1410 1420 1430 1440 1450
IPQGAAESDG RIHKGDRVLA VNGVSLEGAT HKQAVETLRN TGQVVHLLLE
1460 1470 1480 1490 1500
KGQSPTSKEH VPVTPQCTLS DQNAQGQGPE KVKKTTQVKD YSFVTEENTF
1510 1520 1530 1540 1550
EVKLFKNSSG LGFSFSREDN LIPEQINASI VRVKKLFPGQ PAAESGKIDV
1560 1570 1580 1590 1600
GDVILKVNGA SLKGLSQQEV ISALRGTAPE VFLLLCRPPP GVLPEIDTAL
1610 1620 1630 1640 1650
LTPLQSPAQV LPNSSKDSSQ PSCVEQSTSS DENEMSDKSK KQCKSPSRRD
1660 1670 1680 1690 1700
SYSDSSGSGE DDLVTAPANI SNSTWSSALH QTLSNMVSQA QSHHEAPKSQ
1710 1720 1730 1740 1750
EDTICTMFYY PQKIPNKPEF EDSNPSPLPP DMAPGQSYQP QSESASSSSM
1760 1770 1780 1790 1800
DKYHIHHISE PTRQENWTPL KNDLENHLED FELEVELLIT LIKSEKGSLG
1810 1820 1830 1840 1850
FTVTKGNQRI GCYVHDVIQD PAKSDGRLKP GDRLIKVNDT DVTNMTHTDA
1860 1870 1880 1890 1900
VNLLRAASKT VRLVIGRVLE LPRIPMLPHL LPDITLTCNK EELGFSLCGG
1910 1920 1930 1940 1950
HDSLYQVVYI SDINPRSVAA IEGNLQLLDV IHYVNGVSTQ GMTLEEVNRA
1960 1970 1980 1990 2000
LDMSLPSLVL KATRNDLPVV PSSKRSAVSA PKSTKGNGSY SVGSCSQPAL
2010 2020 2030 2040 2050
TPNDSFSTVA GEEINEISYP KGKCSTYQIK GSPNLTLPKE SYIQEDDIYD
2060 2070 2080 2090 2100
DSQEAEVIQS LLDVVDEEAQ NLLNENNAAG YSCGPGTLKM NGKLSEERTE
2110 2120 2130 2140 2150
DTDCDGSPLP EYFTEATKMN GCEEYCEEKV KSESLIQKPQ EKKTDDDEIT
2160 2170 2180 2190 2200
WGNDELPIER TNHEDSDKDH SFLTNDELAV LPVVKVLPSG KYTGANLKSV
2210 2220 2230 2240 2250
IRVLRGLLDQ GIPSKELENL QELKPLDQCL IGQTKENRRK NRYKNILPYD
2260 2270 2280 2290 2300
ATRVPLGDEG GYINASFIKI PVGKEEFVYI ACQGPLPTTV GDFWQMIWEQ
2310 2320 2330 2340 2350
KSTVIAMMTQ EVEGEKIKCQ RYWPNILGKT TMVSNRLRLA LVRMQQLKGF
2360 2370 2380 2390 2400
VVRAMTLEDI QTREVRHISH LNFTAWPDHD TPSQPDDLLT FISYMRHIHR
2410 2420 2430 2440 2450
SGPIITHCSA GIGRSGTLIC IDVVLGLISQ DLDFDISDLV RCMRLQRHGM
2460 2470 2480
VQTEDQYIFC YQVILYVLTR LQAEEEQKQQ PQLLK
Length:2,485
Mass (Da):276,906
Last modified:December 1, 2000 - v2
Checksum:i8D1B31597C66962B
GO
Isoform 2 (identifier: Q12923-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     884-1074: Missing.

Show »
Length:2,294
Mass (Da):255,926
Checksum:iABBFA4BCD60FF56F
GO
Isoform 3 (identifier: Q12923-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1056-1074: Missing.

Show »
Length:2,466
Mass (Da):274,932
Checksum:i5BDCC226F2DEC19D
GO
Isoform 4 (identifier: Q12923-4) [UniParc]FASTAAdd to basket

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.
Show »
Length:2,490
Mass (Da):277,508
Checksum:i8D1FE03D9738A247
GO

Sequence cautioni

The sequence AAH39610 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1134 – 1135LD → FH in CAA56563 (PubMed:7929060).Curated2
Sequence conflicti1216 – 1229KDHHW…LRHIS → DLSRSHCHVYLAHL (Ref. 5) CuratedAdd BLAST14
Sequence conflicti1238 – 1239GL → A in CAA56124 (Ref. 5) Curated2
Sequence conflicti1357S → P in CAA56124 (Ref. 5) Curated1
Sequence conflicti1362 – 1363KP → RS in CAA56124 (Ref. 5) Curated2
Sequence conflicti1538P → A in CAA56563 (PubMed:7929060).Curated1
Sequence conflicti1649R → K in CAA56124 (Ref. 5) Curated1
Sequence conflicti1698 – 1714KSQED…YPQKI → RVKKIPFVPCFTILRKR in CAA56124 (Ref. 5) CuratedAdd BLAST17
Sequence conflicti1797G → A in CAA56563 (PubMed:7929060).Curated1
Sequence conflicti1856 – 1857AA → G in CAA56124 (Ref. 5) Curated2
Sequence conflicti2069A → S in CAA56124 (Ref. 5) Curated1
Sequence conflicti2206 – 2210GLLDQ → VARS in CAA56124 (Ref. 5) Curated5

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0483591356F → L.Corresponds to variant rs10033029dbSNPEnsembl.1
Natural variantiVAR_0162001419L → P.1 PublicationCorresponds to variant rs749353184dbSNPEnsembl.1
Natural variantiVAR_0162011522I → M.1 PublicationCorresponds to variant rs2230600dbSNPEnsembl.1
Natural variantiVAR_0243731625E → K.Corresponds to variant rs12500797dbSNPEnsembl.1
Natural variantiVAR_0483601744S → P.Corresponds to variant rs17012064dbSNPEnsembl.1
Natural variantiVAR_0243742081Y → D.Corresponds to variant rs989902dbSNPEnsembl.1
Natural variantiVAR_0483612458I → V No effect on substrate affinity. 1 PublicationCorresponds to variant rs34226837dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000496884 – 1074Missing in isoform 2. 1 PublicationAdd BLAST191
Alternative sequenceiVSP_0004971056 – 1074Missing in isoform 3. 3 PublicationsAdd BLAST19
Alternative sequenceiVSP_0079211383T → TVLFDK in isoform 4. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47093.1. [Q12923-4]
CCDS47094.1. [Q12923-1]
CCDS47095.1. [Q12923-3]
CCDS47096.1. [Q12923-2]
PIRiA54971.
I67629.
I67630.
RefSeqiNP_006255.1. NM_006264.2. [Q12923-3]
NP_542414.1. NM_080683.2. [Q12923-1]
NP_542415.1. NM_080684.2. [Q12923-2]
NP_542416.1. NM_080685.2. [Q12923-4]
UniGeneiHs.436142.

Genome annotation databases

EnsembliENST00000316707; ENSP00000322675; ENSG00000163629. [Q12923-2]
ENST00000411767; ENSP00000407249; ENSG00000163629. [Q12923-1]
ENST00000427191; ENSP00000408368; ENSG00000163629. [Q12923-3]
ENST00000436978; ENSP00000394794; ENSG00000163629. [Q12923-4]
ENST00000511467; ENSP00000426626; ENSG00000163629. [Q12923-4]
GeneIDi5783.
KEGGihsa:5783.
UCSCiuc003hpy.4. human. [Q12923-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47093.1. [Q12923-4]
CCDS47094.1. [Q12923-1]
CCDS47095.1. [Q12923-3]
CCDS47096.1. [Q12923-2]
PIRiA54971.
I67629.
I67630.
RefSeqiNP_006255.1. NM_006264.2. [Q12923-3]
NP_542414.1. NM_080683.2. [Q12923-1]
NP_542415.1. NM_080684.2. [Q12923-2]
NP_542416.1. NM_080685.2. [Q12923-4]
UniGeneiHs.436142.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ12923.
SMRiQ12923.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111747. 22 interactors.
DIPiDIP-40449N.
IntActiQ12923. 20 interactors.
MINTiMINT-109571.
STRINGi9606.ENSP00000394794.

Chemistry databases

BindingDBiQ12923.
ChEMBLiCHEMBL2976.

PTM databases

DEPODiQ12923.
iPTMnetiQ12923.
PhosphoSitePlusiQ12923.

Polymorphism and mutation databases

BioMutaiPTPN13.
DMDMi12643716.

Proteomic databases

EPDiQ12923.
MaxQBiQ12923.
PaxDbiQ12923.
PeptideAtlasiQ12923.
PRIDEiQ12923.

Protocols and materials databases

DNASUi5783.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316707; ENSP00000322675; ENSG00000163629. [Q12923-2]
ENST00000411767; ENSP00000407249; ENSG00000163629. [Q12923-1]
ENST00000427191; ENSP00000408368; ENSG00000163629. [Q12923-3]
ENST00000436978; ENSP00000394794; ENSG00000163629. [Q12923-4]
ENST00000511467; ENSP00000426626; ENSG00000163629. [Q12923-4]
GeneIDi5783.
KEGGihsa:5783.
UCSCiuc003hpy.4. human. [Q12923-1]

Organism-specific databases

CTDi5783.
DisGeNETi5783.
GeneCardsiPTPN13.
HGNCiHGNC:9646. PTPN13.
HPAiCAB002213.
MIMi600267. gene.
neXtProtiNX_Q12923.
OpenTargetsiENSG00000163629.
PharmGKBiPA33988.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0792. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00830000128259.
HOVERGENiHBG053756.
InParanoidiQ12923.
KOiK02374.
OMAiGCYVHDV.
OrthoDBiEOG091G0BZR.
PhylomeDBiQ12923.
TreeFamiTF315388.

Enzyme and pathway databases

BioCyciZFISH:HS08898-MONOMER.
BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-1660499. Synthesis of PIPs at the plasma membrane.
SIGNORiQ12923.

Miscellaneous databases

ChiTaRSiPTPN13. human.
EvolutionaryTraceiQ12923.
GeneWikiiPTPN13.
GenomeRNAii5783.
PROiQ12923.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163629.
ExpressionAtlasiQ12923. baseline and differential.
GenevisibleiQ12923. HS.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 5 hits.
3.90.190.10. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011019. KIND_dom.
IPR001478. PDZ.
IPR011993. PH_dom-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR012153. PTPN13.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR19134:SF197. PTHR19134:SF197. 2 hits.
PfamiPF09380. 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]
PIRSFiPIRSF000933. Tyr-Ptase_nr13. 1 hit.
PRINTSiPR00935. BAND41.
PR00700. PRTYPHPHTASE.
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
SM00750. KIND. 1 hit.
SM00228. PDZ. 5 hits.
SM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50156. SSF50156. 5 hits.
SSF50729. SSF50729. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50057. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPTN13_HUMAN
AccessioniPrimary (citable) accession number: Q12923
Secondary accession number(s): B2RTR0
, Q15159, Q15263, Q15264, Q15265, Q15674, Q16826, Q8IWH7, Q9NYN9, Q9UDA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: November 30, 2016
This is version 186 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 4
    Human chromosome 4: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.