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Q12923

- PTN13_HUMAN

UniProt

Q12923 - PTN13_HUMAN

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Protein
Tyrosine-protein phosphatase non-receptor type 13
Gene
PTPN13, PNP1, PTP1E, PTPL1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei2378 – 23781Substrate
Active sitei2408 – 24081Phosphocysteine intermediate Inferred
Binding sitei2452 – 24521Substrate By similarity

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. peptidyl-tyrosine dephosphorylation Source: GOC
  2. protein dephosphorylation Source: ProtInc
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. Cell projectionlamellipodium
Note: Colocalizes with PKN2 in lamellipodia-like structure, regions of large actin turnover.1 Publication

GO - Cellular componenti

  1. cell body Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProt
  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 13
PRO_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

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

ArrayExpressiQ12923.
BgeeiQ12923.
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 and ARHGAP29. Interacts (via PDZ 3 domain) with PKN2 (via C-terminus).5 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 2-174, 584-899, 1103-1174, 1361-1588, 1789-1964, 2170-2477.

Miscellaneous databases

EvolutionaryTraceiQ12923.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 190188KIND
Add
BLAST
Domaini572 – 872301FERM
Add
BLAST
Domaini1093 – 117886PDZ 1
Add
BLAST
Domaini1368 – 145285PDZ 2
Add
BLAST
Domaini1501 – 158888PDZ 3
Add
BLAST
Domaini1788 – 186881PDZ 4
Add
BLAST
Domaini1882 – 196584PDZ 5
Add
BLAST
Domaini2213 – 2467255Tyrosine-protein phosphatase
Add
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili469 – 50436 Reviewed prediction
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 FERM domain.
Contains 1 KIND domain.
Contains 5 PDZ (DHR) domains.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5599.
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.
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.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR012153. Tyr_Pase_non-rcpt_typ-13.
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. Align

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

MHVSLAEALE VRGGPLQEEE IWAVLNQSAE SLQELFRKVS LADPAALGFI     50
ISPWSLLLLP SGSVSFTDEN ISNQDLRAFT APEVLQNQSL TSLSDVEKIH 100
IYSLGMTLYW GADYEVPQSQ PIKLGDHLNS ILLGMCEDVI YARVSVRTVL 150
DACSAHIRNS NCAPSFSYVK HLVKLVLGNL SGTDQLSCNS EQKPDRSQAI 200
RDRLRGKGLP TGRSSTSDVL DIQKPPLSHQ TFLNKGLSKS MGFLSIKDTQ 250
DENYFKDILS DNSGREDSEN TFSPYQFKTS GPEKKPIPGI DVLSKKKIWA 300
SSMDLLCTAD RDFSSGETAT YRRCHPEAVT VRTSTTPRKK EARYSDGSIA 350
LDIFGPQKMD PIYHTRELPT SSAISSALDR IRERQKKLQV LREAMNVEEP 400
VRRYKTYHGD VFSTSSESPS IISSESDFRQ VRRSEASKRF ESSSGLPGVD 450
ETLSQGQSQR PSRQYETPFE GNLINQEIML KRQEEELMQL QAKMALRQSR 500
LSLYPGDTIK ASMLDITRDP LREIALETAM TQRKLRNFFG PEFVKMTIEP 550
FISLDLPRSI LTKKGKNEDN RRKVNIMLLN GQRLELTCDT KTICKDVFDM 600
VVAHIGLVEH HLFALATLKD NEYFFVDPDL KLTKVAPEGW KEEPKKKTKA 650
TVNFTLFFRI KFFMDDVSLI QHTLTCHQYY LQLRKDILEE RMHCDDETSL 700
LLASLALQAE YGDYQPEVHG VSYFRMEHYL PARVMEKLDL SYIKEELPKL 750
HNTYVGASEK ETELEFLKVC QRLTEYGVHF HRVHPEKKSQ TGILLGVCSK 800
GVLVFEVHNG VRTLVLRFPW RETKKISFSK KKITLQNTSD GIKHGFQTDN 850
SKICQYLLHL CSYQHKFQLQ MRARQSNQDA QDIERASFRS LNLQAESVRG 900
FNMGRAISTG SLASSTLNKL AVRPLSVQAE ILKRLSCSEL SLYQPLQNSS 950
KEKNDKASWE EKPREMSKSY HDLSQASLYP HRKNVIVNME PPPQTVAELV 1000
GKPSHQMSRS DAESLAGVTK LNNSKSVASL NRSPERRKHE SDSSSIEDPG 1050
QAYVLGMTMH SSGNSSSQVP LKENDVLHKR WSIVSSPERE ITLVNLKKDA 1100
KYGLGFQIIG GEKMGRLDLG IFISSVAPGG PADLDGCLKP GDRLISVNSV 1150
SLEGVSHHAA IEILQNAPED VTLVISQPKE KISKVPSTPV HLTNEMKNYM 1200
KKSSYMQDSA IDSSSKDHHW SRGTLRHISE NSFGPSGGLR EGSLSSQDSR 1250
TESASLSQSQ VNGFFASHLG DQTWQESQHG SPSPSVISKA TEKETFTDSN 1300
QSKTKKPGIS DVTDYSDRGD SDMDEATYSS SQDHQTPKQE SSSSVNTSNK 1350
MNFKTFSSSP PKPGDIFEVE LAKNDNSLGI SVTGGVNTSV RHGGIYVKAV 1400
IPQGAAESDG RIHKGDRVLA VNGVSLEGAT HKQAVETLRN TGQVVHLLLE 1450
KGQSPTSKEH VPVTPQCTLS DQNAQGQGPE KVKKTTQVKD YSFVTEENTF 1500
EVKLFKNSSG LGFSFSREDN LIPEQINASI VRVKKLFPGQ PAAESGKIDV 1550
GDVILKVNGA SLKGLSQQEV ISALRGTAPE VFLLLCRPPP GVLPEIDTAL 1600
LTPLQSPAQV LPNSSKDSSQ PSCVEQSTSS DENEMSDKSK KQCKSPSRRD 1650
SYSDSSGSGE DDLVTAPANI SNSTWSSALH QTLSNMVSQA QSHHEAPKSQ 1700
EDTICTMFYY PQKIPNKPEF EDSNPSPLPP DMAPGQSYQP QSESASSSSM 1750
DKYHIHHISE PTRQENWTPL KNDLENHLED FELEVELLIT LIKSEKGSLG 1800
FTVTKGNQRI GCYVHDVIQD PAKSDGRLKP GDRLIKVNDT DVTNMTHTDA 1850
VNLLRAASKT VRLVIGRVLE LPRIPMLPHL LPDITLTCNK EELGFSLCGG 1900
HDSLYQVVYI SDINPRSVAA IEGNLQLLDV IHYVNGVSTQ GMTLEEVNRA 1950
LDMSLPSLVL KATRNDLPVV PSSKRSAVSA PKSTKGNGSY SVGSCSQPAL 2000
TPNDSFSTVA GEEINEISYP KGKCSTYQIK GSPNLTLPKE SYIQEDDIYD 2050
DSQEAEVIQS LLDVVDEEAQ NLLNENNAAG YSCGPGTLKM NGKLSEERTE 2100
DTDCDGSPLP EYFTEATKMN GCEEYCEEKV KSESLIQKPQ EKKTDDDEIT 2150
WGNDELPIER TNHEDSDKDH SFLTNDELAV LPVVKVLPSG KYTGANLKSV 2200
IRVLRGLLDQ GIPSKELENL QELKPLDQCL IGQTKENRRK NRYKNILPYD 2250
ATRVPLGDEG GYINASFIKI PVGKEEFVYI ACQGPLPTTV GDFWQMIWEQ 2300
KSTVIAMMTQ EVEGEKIKCQ RYWPNILGKT TMVSNRLRLA LVRMQQLKGF 2350
VVRAMTLEDI QTREVRHISH LNFTAWPDHD TPSQPDDLLT FISYMRHIHR 2400
SGPIITHCSA GIGRSGTLIC IDVVLGLISQ DLDFDISDLV RCMRLQRHGM 2450
VQTEDQYIFC YQVILYVLTR LQAEEEQKQQ PQLLK 2485
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. Reason: Contaminating sequence. Potential poly-A sequence.

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.
VSP_000496Add
BLAST
Alternative sequencei1056 – 107419Missing in isoform 3.
VSP_000497Add
BLAST
Alternative sequencei1383 – 13831T → TVLFDK in isoform 4.
VSP_007921

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1134 – 11352LD → FH in CAA56563. 1 Publication
Sequence conflicti1216 – 122914KDHHW…LRHIS → DLSRSHCHVYLAHL1 Publication
Add
BLAST
Sequence conflicti1238 – 12392GL → A in CAA56124. 1 Publication
Sequence conflicti1357 – 13571S → P in CAA56124. 1 Publication
Sequence conflicti1362 – 13632KP → RS in CAA56124. 1 Publication
Sequence conflicti1538 – 15381P → A in CAA56563. 1 Publication
Sequence conflicti1649 – 16491R → K in CAA56124. 1 Publication
Sequence conflicti1698 – 171417KSQED…YPQKI → RVKKIPFVPCFTILRKR in CAA56124. 1 Publication
Add
BLAST
Sequence conflicti1797 – 17971G → A in CAA56563. 1 Publication
Sequence conflicti1856 – 18572AA → G in CAA56124. 1 Publication
Sequence conflicti2069 – 20691A → S in CAA56124. 1 Publication
Sequence conflicti2206 – 22105GLLDQ → VARS in CAA56124. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS47093.1. [Q12923-4 ]
CCDS47094.1. [Q12923-1 ]
CCDS47095.1. [Q12923-3 ]
CCDS47096.1. [Q12923-2 ]
PIRi A54971.
I67629.
I67630.
RefSeqi NP_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 ]
UniGenei Hs.436142.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D5G NMR - A 1361-1456 [» ]
1Q7X NMR - A 1358-1459 [» ]
1WCH X-ray 1.85 A 2163-2477 [» ]
2M0Z NMR - A 1361-1456 [» ]
2M10 NMR - A 1361-1456 [» ]
3LNX X-ray 1.64 A/B/C/D/E/F 1361-1456 [» ]
3LNY X-ray 1.30 A 1361-1456 [» ]
3PDZ NMR - A 1361-1456 [» ]
ProteinModelPortali Q12923.
SMRi Q12923. Positions 2-174, 584-899, 1103-1174, 1361-1588, 1789-1964, 2170-2477.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111747. 13 interactions.
DIPi DIP-40449N.
IntActi Q12923. 13 interactions.
MINTi MINT-109571.

Chemistry

BindingDBi Q12923.
ChEMBLi CHEMBL2976.

PTM databases

PhosphoSitei Q12923.

Polymorphism databases

DMDMi 12643716.

Proteomic databases

MaxQBi Q12923.
PaxDbi Q12923.
PRIDEi Q12923.

Protocols and materials databases

DNASUi 5783.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316707 ; ENSP00000322675 ; ENSG00000163629 . [Q12923-2 ]
ENST00000411767 ; ENSP00000407249 ; ENSG00000163629 . [Q12923-1 ]
ENST00000427191 ; ENSP00000408368 ; ENSG00000163629 . [Q12923-3 ]
ENST00000436978 ; ENSP00000394794 ; ENSG00000163629 . [Q12923-4 ]
ENST00000511467 ; ENSP00000426626 ; ENSG00000163629 . [Q12923-4 ]
GeneIDi 5783.
KEGGi hsa:5783.
UCSCi uc003hpy.3. human. [Q12923-4 ]
uc003hpz.3. human. [Q12923-1 ]
uc003hqa.3. human. [Q12923-3 ]
uc003hqb.3. human. [Q12923-2 ]

Organism-specific databases

CTDi 5783.
GeneCardsi GC04P087515.
HGNCi HGNC:9646. PTPN13.
HPAi CAB002213.
MIMi 600267. gene.
neXtProti NX_Q12923.
PharmGKBi PA33988.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
HOVERGENi HBG053756.
InParanoidi Q12923.
KOi K02374.
OMAi GCYVHDV.
OrthoDBi EOG7K9K22.
PhylomeDBi Q12923.
TreeFami TF315388.

Miscellaneous databases

ChiTaRSi PTPN13. human.
EvolutionaryTracei Q12923.
GeneWikii PTPN13.
GenomeRNAii 5783.
NextBioi 22492.
PROi Q12923.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q12923.
Bgeei Q12923.
Genevestigatori Q12923.

Family and domain databases

Gene3Di 1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 5 hits.
3.90.190.10. 1 hit.
InterProi IPR019749. 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.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR012153. Tyr_Pase_non-rcpt_typ-13.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
PANTHERi PTHR19134:SF197. PTHR19134:SF197. 1 hit.
Pfami PF09380. 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 ]
PIRSFi PIRSF000933. Tyr-Ptase_nr13. 1 hit.
PRINTSi PR00935. BAND41.
PR00700. PRTYPHPHTASE.
SMARTi SM00295. B41. 1 hit.
SM00750. KIND. 1 hit.
SM00228. PDZ. 5 hits.
SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF47031. SSF47031. 1 hit.
SSF50156. SSF50156. 5 hits.
SSF52799. SSF52799. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS50057. 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 ]
ProtoNeti Search...

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. "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.

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: July 9, 2014
This is version 161 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

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