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Q12923

- PTN13_HUMAN

UniProt

Q12923 - PTN13_HUMAN

Protein

Tyrosine-protein phosphatase non-receptor type 13

Gene

PTPN13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    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 intermediateCurated
    Binding sitei2452 – 24521SubstrateBy 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

    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: UniProt
    5. lamellipodium Source: UniProtKB
    6. neuron projection Source: Ensembl
    7. nucleus Source: UniProtKB
    8. plasma membrane Source: UniProtKB

    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

    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).7 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

    1
    2485
    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.
    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.
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1134 – 11352LD → FH in CAA56563. (PubMed:7929060)Curated
    Sequence conflicti1216 – 122914KDHHW…LRHIS → DLSRSHCHVYLAHL1 PublicationCuratedAdd
    BLAST
    Sequence conflicti1238 – 12392GL → A in CAA56124. 1 PublicationCurated
    Sequence conflicti1357 – 13571S → P in CAA56124. 1 PublicationCurated
    Sequence conflicti1362 – 13632KP → RS in CAA56124. 1 PublicationCurated
    Sequence conflicti1538 – 15381P → A in CAA56563. (PubMed:7929060)Curated
    Sequence conflicti1649 – 16491R → K in CAA56124. 1 PublicationCurated
    Sequence conflicti1698 – 171417KSQED…YPQKI → RVKKIPFVPCFTILRKR in CAA56124. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti1797 – 17971G → A in CAA56563. (PubMed:7929060)Curated
    Sequence conflicti1856 – 18572AA → G in CAA56124. 1 PublicationCurated
    Sequence conflicti2069 – 20691A → S in CAA56124. 1 PublicationCurated
    Sequence conflicti2206 – 22105GLLDQ → VARS in CAA56124. 1 PublicationCurated

    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.
    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:
    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

    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: October 1, 2014
    This is version 162 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