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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei2378 – 23781Substrate
Active sitei2408 – 24081Phosphocysteine intermediateCurated
Binding sitei2452 – 24521SubstrateBy similarity

GO - Molecular functioni

  1. phosphatidylinositol 3-kinase regulatory subunit binding Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

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
ProteomesiUP000005640: 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

  1. cell body Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProtKB
  5. lamellipodium Source: UniProtKB
  6. neuron projection Source: Ensembl
  7. nucleus Source: UniProtKB
  8. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2154 – 21541D → H: No effect on substrate affinity. 1 Publication
Mutagenesisi2205 – 22051R → W: No effect on substrate affinity. 1 Publication
Mutagenesisi2221 – 22211Q → M: Reduces substrate affinity 2 fold. 1 Publication
Mutagenesisi2307 – 23071M → T: Reduces substrate affinity 7 fold. 1 Publication
Mutagenesisi2408 – 24081C → S: Loss of catalytic activity. 1 Publication
Mutagenesisi2444 – 24441R → E: Loss of catalytic activity. 1 Publication
Mutagenesisi2444 – 24441R → K: Reduces substrate affinity 7 fold. 1 Publication
Mutagenesisi2444 – 24441R → Q: Strongly decreases catalytic activity. 1 Publication
Mutagenesisi2448 – 24481H → A: Reduces substrate affinity 2 fold. 1 Publication
Mutagenesisi2449 – 24491G → V: Loss of catalytic activity. 1 Publication
Mutagenesisi2474 – 24741E → D: No effect on substrate affinity. 1 Publication

Organism-specific databases

PharmGKBiPA33988.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24852485Tyrosine-protein phosphatase non-receptor type 13PRO_0000219435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1029 – 10291Phosphoserine1 Publication
Modified residuei1033 – 10331Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12923.
PaxDbiQ12923.
PRIDEiQ12923.

PTM databases

DEPODiQ12923.
PhosphoSiteiQ12923.

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

BgeeiQ12923.
ExpressionAtlasiQ12923. baseline and differential.
GenevestigatoriQ12923.

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

Protein-protein interaction databases

BioGridi111747. 14 interactions.
DIPiDIP-40449N.
IntActiQ12923. 13 interactions.
MINTiMINT-109571.

Structurei

Secondary structure

1
2485
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1366 – 13727Combined sources
Beta strandi1374 – 13774Combined sources
Beta strandi1379 – 13846Combined sources
Beta strandi1385 – 13873Combined sources
Beta strandi1388 – 13903Combined sources
Helixi1391 – 13933Combined sources
Beta strandi1395 – 14006Combined sources
Helixi1405 – 14095Combined sources
Beta strandi1417 – 14215Combined sources
Helixi1431 – 14399Combined sources
Beta strandi1443 – 14508Combined sources
Helixi2175 – 21795Combined sources
Beta strandi2188 – 21903Combined sources
Helixi2194 – 220916Combined sources
Helixi2212 – 22209Combined sources
Helixi2231 – 22333Combined sources
Helixi2235 – 22384Combined sources
Turni2257 – 22604Combined sources
Beta strandi2264 – 22729Combined sources
Beta strandi2275 – 22828Combined sources
Helixi2287 – 22893Combined sources
Helixi2290 – 229910Combined sources
Beta strandi2304 – 23074Combined sources
Beta strandi2311 – 23133Combined sources
Beta strandi2331 – 234616Combined sources
Beta strandi2348 – 235912Combined sources
Turni2360 – 23634Combined sources
Beta strandi2364 – 237310Combined sources
Helixi2385 – 239814Combined sources
Beta strandi2404 – 24074Combined sources
Beta strandi2409 – 24124Combined sources
Helixi2413 – 242917Combined sources
Helixi2436 – 24449Combined sources
Helixi2454 – 247522Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1361-1454, 2170-2477.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12923.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 190188KINDPROSITE-ProRule annotationAdd
BLAST
Domaini572 – 872301FERMPROSITE-ProRule annotationAdd
BLAST
Domaini1093 – 117886PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini1368 – 145285PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini1501 – 158888PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini1788 – 186881PDZ 4PROSITE-ProRule annotationAdd
BLAST
Domaini1882 – 196584PDZ 5PROSITE-ProRule annotationAdd
BLAST
Domaini2213 – 2467255Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2408 – 24147Substrate
Regioni2408 – 24147Substrate bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili469 – 50436Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi56 – 594Poly-Leu
Compositional biasi1742 – 17498Poly-Ser

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

eggNOGiCOG5599.
GeneTreeiENSGT00780000121879.
HOVERGENiHBG053756.
InParanoidiQ12923.
KOiK02374.
OMAiGCYVHDV.
OrthoDBiEOG7K9K22.
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.
IPR001478. PDZ.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR012153. PTPN13.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR19134:SF197. PTHR19134:SF197. 1 hit.
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.
SM00750. KIND. 1 hit.
SM00228. PDZ. 5 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50156. SSF50156. 5 hits.
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 AAH39610.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1134 – 11352LD → FH in CAA56563 (PubMed:7929060).Curated
Sequence conflicti1216 – 122914KDHHW…LRHIS → DLSRSHCHVYLAHL (Ref. 5) CuratedAdd
BLAST
Sequence conflicti1238 – 12392GL → A in CAA56124 (Ref. 5) Curated
Sequence conflicti1357 – 13571S → P in CAA56124 (Ref. 5) Curated
Sequence conflicti1362 – 13632KP → RS in CAA56124 (Ref. 5) Curated
Sequence conflicti1538 – 15381P → A in CAA56563 (PubMed:7929060).Curated
Sequence conflicti1649 – 16491R → K in CAA56124 (Ref. 5) Curated
Sequence conflicti1698 – 171417KSQED…YPQKI → RVKKIPFVPCFTILRKR in CAA56124 (Ref. 5) CuratedAdd
BLAST
Sequence conflicti1797 – 17971G → A in CAA56563 (PubMed:7929060).Curated
Sequence conflicti1856 – 18572AA → G in CAA56124 (Ref. 5) Curated
Sequence conflicti2069 – 20691A → S in CAA56124 (Ref. 5) Curated
Sequence conflicti2206 – 22105GLLDQ → VARS in CAA56124 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1356 – 13561F → L.
Corresponds to variant rs10033029 [ dbSNP | Ensembl ].
VAR_048359
Natural varianti1419 – 14191L → P.1 Publication
VAR_016200
Natural varianti1522 – 15221I → M.1 Publication
Corresponds to variant rs2230600 [ dbSNP | Ensembl ].
VAR_016201
Natural varianti1625 – 16251E → K.
Corresponds to variant rs12500797 [ dbSNP | Ensembl ].
VAR_024373
Natural varianti1744 – 17441S → P.
Corresponds to variant rs17012064 [ dbSNP | Ensembl ].
VAR_048360
Natural varianti2081 – 20811Y → D.
Corresponds to variant rs989902 [ dbSNP | Ensembl ].
VAR_024374
Natural varianti2458 – 24581I → V No effect on substrate affinity. 1 Publication
Corresponds to variant rs34226837 [ dbSNP | Ensembl ].
VAR_048361

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei884 – 1074191Missing in isoform 2. 1 PublicationVSP_000496Add
BLAST
Alternative sequencei1056 – 107419Missing in isoform 3. 3 PublicationsVSP_000497Add
BLAST
Alternative sequencei1383 – 13831T → TVLFDK in isoform 4. 2 PublicationsVSP_007921

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.3. human. [Q12923-4]
uc003hpz.3. human. [Q12923-1]
uc003hqa.3. human. [Q12923-3]
uc003hqb.3. human. [Q12923-2]

Polymorphism databases

DMDMi12643716.

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
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. Positions 1361-1454, 2170-2477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111747. 14 interactions.
DIPiDIP-40449N.
IntActiQ12923. 13 interactions.
MINTiMINT-109571.

Chemistry

BindingDBiQ12923.
ChEMBLiCHEMBL2976.

PTM databases

DEPODiQ12923.
PhosphoSiteiQ12923.

Polymorphism databases

DMDMi12643716.

Proteomic databases

MaxQBiQ12923.
PaxDbiQ12923.
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.3. human. [Q12923-4]
uc003hpz.3. human. [Q12923-1]
uc003hqa.3. human. [Q12923-3]
uc003hqb.3. human. [Q12923-2]

Organism-specific databases

CTDi5783.
GeneCardsiGC04P087515.
HGNCiHGNC:9646. PTPN13.
HPAiCAB002213.
MIMi600267. gene.
neXtProtiNX_Q12923.
PharmGKBiPA33988.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00780000121879.
HOVERGENiHBG053756.
InParanoidiQ12923.
KOiK02374.
OMAiGCYVHDV.
OrthoDBiEOG7K9K22.
PhylomeDBiQ12923.
TreeFamiTF315388.

Miscellaneous databases

ChiTaRSiPTPN13. human.
EvolutionaryTraceiQ12923.
GeneWikiiPTPN13.
GenomeRNAii5783.
NextBioi22492.
PROiQ12923.
SOURCEiSearch...

Gene expression databases

BgeeiQ12923.
ExpressionAtlasiQ12923. baseline and differential.
GenevestigatoriQ12923.

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.
IPR001478. PDZ.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR012153. PTPN13.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR19134:SF197. PTHR19134:SF197. 1 hit.
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.
SM00750. KIND. 1 hit.
SM00228. PDZ. 5 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50156. SSF50156. 5 hits.
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...

Publicationsi

« Hide 'large scale' publications
  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. 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. "FBXL2- and PTPL1-mediated degradation of p110-free p85beta regulatory subunit controls the PI(3)K signalling cascade."
    Kuchay S., Duan S., Schenkein E., Peschiaroli A., Saraf A., Florens L., Washburn M.P., Pagano M.
    Nat. Cell Biol. 15:472-480(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FBXL2 AND PIK3R2.
  17. "The serologically defined colon cancer antigen-3 interacts with the protein tyrosine phosphatase PTPN13 and is involved in the regulation of cytokinesis."
    Hagemann N., Ackermann N., Christmann J., Brier S., Yu F., Erdmann K.S.
    Oncogene 32:4602-4613(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SDCCAG3.
  18. "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.
  19. "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.
  20. "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.
  21. "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.

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: February 4, 2015
This is version 166 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

External Data

Dasty 3

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 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.