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Q05209

- PTN12_HUMAN

UniProt

Q05209 - PTN12_HUMAN

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Protein
Tyrosine-protein phosphatase non-receptor type 12
Gene
PTPN12
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei199 – 1991Substrate By similarity
Active sitei231 – 2311Phosphocysteine intermediate By similarity
Binding sitei278 – 2781Substrate By similarity

GO - Molecular functioni

  1. SH3 domain binding Source: UniProtKB
  2. non-membrane spanning protein tyrosine phosphatase activity Source: ProtInc
  3. protein binding Source: UniProtKB
Complete GO annotation...

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 12 (EC:3.1.3.48)
Alternative name(s):
PTP-PEST
Protein-tyrosine phosphatase G1
Short name:
PTPG1
Gene namesi
Name:PTPN12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:9645. PTPN12.

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: HPA
  4. cytosol Source: Ensembl
  5. plasma membrane Source: HPA
  6. podosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm

Pathology & Biotechi

Keywords - Diseasei

Disease mutation

Organism-specific databases

PharmGKBiPA33987.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 780780Tyrosine-protein phosphatase non-receptor type 12
PRO_0000094771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei19 – 191Phosphoserine1 Publication
Modified residuei332 – 3321Phosphoserine2 Publications
Modified residuei435 – 4351Phosphoserine2 Publications
Modified residuei449 – 4491Phosphoserine2 Publications
Modified residuei468 – 4681Phosphoserine1 Publication
Modified residuei519 – 5191Phosphothreonine1 Publication
Modified residuei567 – 5671Phosphoserine1 Publication
Modified residuei569 – 5691Phosphothreonine1 Publication
Modified residuei571 – 5711Phosphoserine1 Publication
Modified residuei596 – 5961Phosphoserine By similarity
Modified residuei598 – 5981Phosphothreonine By similarity
Modified residuei603 – 6031Phosphoserine3 Publications
Modified residuei606 – 6061Phosphoserine2 Publications
Modified residuei608 – 6081Phosphoserine1 Publication
Modified residuei613 – 6131Phosphoserine1 Publication
Modified residuei673 – 6731Phosphoserine4 Publications
Modified residuei689 – 6891Phosphoserine2 Publications
Modified residuei693 – 6931Phosphothreonine2 Publications

Post-translational modificationi

Phosphorylated by STK24/MST3 and this results in inhibition of its activity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ05209.
PaxDbiQ05209.
PRIDEiQ05209.

PTM databases

PhosphoSiteiQ05209.

Expressioni

Gene expression databases

ArrayExpressiQ05209.
BgeeiQ05209.
CleanExiHS_PTPN12.
GenevestigatoriQ05209.

Organism-specific databases

HPAiHPA007097.

Interactioni

Subunit structurei

Interacts with TGFB1I1 By similarity. Interacts with PSTPIP1. Interacts with PTK2B/PYK2. Interacts with LPXN By similarity.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAR1P569454EBI-2266035,EBI-702093
ERBB2P046264EBI-2266035,EBI-641062
PDGFRBP096193EBI-2266035,EBI-641237
TEKQ027632EBI-2266035,EBI-2257090

Protein-protein interaction databases

BioGridi111746. 41 interactions.
IntActiQ05209. 37 interactions.
MINTiMINT-243699.
STRINGi9606.ENSP00000248594.

Structurei

3D structure databases

ProteinModelPortaliQ05209.
SMRiQ05209. Positions 3-298.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 293266Tyrosine-protein phosphatase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni231 – 2377Substrate binding By similarity
Regioni345 – 43894Interaction with TGFB1I1 By similarity
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5599.
HOGENOMiHOG000252955.
HOVERGENiHBG007666.
InParanoidiQ05209.
KOiK18024.
OMAiTWSFHGP.
OrthoDBiEOG744T8Z.
PhylomeDBiQ05209.
TreeFamiTF351977.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR012266. Ptpn_12.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000932. Tyr-Ptase_nr12. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q05209-1) [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

MEQVEILRKF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT    50
ATGEKEENVK KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP 100
KAYVATQGPL ANTVIDFWRM IWEYNVVIIV MACREFEMGR KKCERYWPLY 150
GEDPITFAPF KISCEDEQAR TDYFIRTLLL EFQNESRRLY QFHYVNWPDH 200
DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA ICAIDYTWNL 250
LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL 300
YEIHGAQKIA DGVNEINTEN MVSSIEPEKQ DSPPPKPPRT RSCLVEGDAK 350
EEILQPPEPH PVPPILTPSP PSAFPTVTTV WQDNDRYHPK PVLHMVSSEQ 400
HSADLNRNYS KSTELPGKNE STIEQIDKKL ERNLSFEIKK VPLQEGPKSF 450
DGNTLLNRGH AIKIKSASPC IADKISKPQE LSSDLNVGDT SQNSCVDCSV 500
TQSNKVSVTP PEESQNSDTP PRPDRLPLDE KGHVTWSFHG PENAIPIPDL 550
SEGNSSDINY QTRKTVSLTP SPTTQVETPD LVDHDNTSPL FRTPLSFTNP 600
LHSDDSDSDE RNSDGAVTQN KTNISTASAT VSAATSTESI STRKVLPMSI 650
ARHNIAGTTH SGAEKDVDVS EDSPPPLPER TPESFVLASE HNTPVRSEWS 700
ELQSQERSEQ KKSEGLITSE NEKCDHPAGG IHYEMCIECP PTFSDKREQI 750
SENPTEATDI GFGNRCGKPK GPRDPPSEWT 780
Length:780
Mass (Da):88,106
Last modified:January 11, 2011 - v3
Checksum:i663DB3E5176FD7FD
GO
Isoform 2 (identifier: Q05209-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-130: Missing.

Note: No experimental confirmation available.

Show »
Length:650
Mass (Da):72,778
Checksum:i217EF3041B7E5EDB
GO
Isoform 3 (identifier: Q05209-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:661
Mass (Da):74,138
Checksum:i74E2947477636633
GO

Sequence cautioni

The sequence BAD92761.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611K → R in colon cancer. 1 Publication
VAR_006385
Natural varianti322 – 3221V → I.4 Publications
Corresponds to variant rs9640663 [ dbSNP | Ensembl ].
VAR_019512
Natural varianti573 – 5731T → A.1 Publication
Corresponds to variant rs3750050 [ dbSNP | Ensembl ].
VAR_020297
Natural varianti706 – 7061E → K.
Corresponds to variant rs2230602 [ dbSNP | Ensembl ].
VAR_057129

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 130130Missing in isoform 2.
VSP_046274Add
BLAST
Alternative sequencei1 – 119119Missing in isoform 3.
VSP_054168Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211I → V in BAA02648. 1 Publication
Sequence conflicti121 – 1211I → V in AAB30047. 1 Publication
Sequence conflicti612 – 6121N → D in BAG59344. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13380 mRNA. Translation: BAA02648.1.
M93425 mRNA. Translation: AAA36529.1.
AK289573 mRNA. Translation: BAF82262.1.
AK296764 mRNA. Translation: BAG59344.1.
AB209524 mRNA. Translation: BAD92761.1. Different initiation.
AC006451 Genomic DNA. Translation: AAQ96881.1.
CH236949 Genomic DNA. Translation: EAL24198.1.
CH471091 Genomic DNA. Translation: EAW77036.1.
CH471091 Genomic DNA. Translation: EAW77037.1.
BC050008 mRNA. Translation: AAH50008.2.
S69184 mRNA. Translation: AAB30047.2.
CCDSiCCDS47619.1. [Q05209-3]
CCDS47620.1. [Q05209-2]
CCDS5592.1. [Q05209-1]
PIRiJC1368.
RefSeqiNP_001124480.1. NM_001131008.1. [Q05209-3]
NP_001124481.1. NM_001131009.1. [Q05209-2]
NP_002826.3. NM_002835.3. [Q05209-1]
UniGeneiHs.61812.

Genome annotation databases

EnsembliENST00000248594; ENSP00000248594; ENSG00000127947. [Q05209-1]
ENST00000415482; ENSP00000392429; ENSG00000127947.
ENST00000435495; ENSP00000397991; ENSG00000127947. [Q05209-2]
GeneIDi5782.
KEGGihsa:5782.
UCSCiuc003ugh.2. human. [Q05209-1]

Polymorphism databases

DMDMi317373522.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13380 mRNA. Translation: BAA02648.1 .
M93425 mRNA. Translation: AAA36529.1 .
AK289573 mRNA. Translation: BAF82262.1 .
AK296764 mRNA. Translation: BAG59344.1 .
AB209524 mRNA. Translation: BAD92761.1 . Different initiation.
AC006451 Genomic DNA. Translation: AAQ96881.1 .
CH236949 Genomic DNA. Translation: EAL24198.1 .
CH471091 Genomic DNA. Translation: EAW77036.1 .
CH471091 Genomic DNA. Translation: EAW77037.1 .
BC050008 mRNA. Translation: AAH50008.2 .
S69184 mRNA. Translation: AAB30047.2 .
CCDSi CCDS47619.1. [Q05209-3 ]
CCDS47620.1. [Q05209-2 ]
CCDS5592.1. [Q05209-1 ]
PIRi JC1368.
RefSeqi NP_001124480.1. NM_001131008.1. [Q05209-3 ]
NP_001124481.1. NM_001131009.1. [Q05209-2 ]
NP_002826.3. NM_002835.3. [Q05209-1 ]
UniGenei Hs.61812.

3D structure databases

ProteinModelPortali Q05209.
SMRi Q05209. Positions 3-298.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111746. 41 interactions.
IntActi Q05209. 37 interactions.
MINTi MINT-243699.
STRINGi 9606.ENSP00000248594.

Chemistry

BindingDBi Q05209.
ChEMBLi CHEMBL3236.

PTM databases

PhosphoSitei Q05209.

Polymorphism databases

DMDMi 317373522.

Proteomic databases

MaxQBi Q05209.
PaxDbi Q05209.
PRIDEi Q05209.

Protocols and materials databases

DNASUi 5782.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000248594 ; ENSP00000248594 ; ENSG00000127947 . [Q05209-1 ]
ENST00000415482 ; ENSP00000392429 ; ENSG00000127947 .
ENST00000435495 ; ENSP00000397991 ; ENSG00000127947 . [Q05209-2 ]
GeneIDi 5782.
KEGGi hsa:5782.
UCSCi uc003ugh.2. human. [Q05209-1 ]

Organism-specific databases

CTDi 5782.
GeneCardsi GC07P077166.
H-InvDBi HIX0033626.
HGNCi HGNC:9645. PTPN12.
HPAi HPA007097.
MIMi 600079. gene.
neXtProti NX_Q05209.
PharmGKBi PA33987.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
HOGENOMi HOG000252955.
HOVERGENi HBG007666.
InParanoidi Q05209.
KOi K18024.
OMAi TWSFHGP.
OrthoDBi EOG744T8Z.
PhylomeDBi Q05209.
TreeFami TF351977.

Miscellaneous databases

ChiTaRSi PTPN12. human.
GeneWikii PTPN12.
GenomeRNAii 5782.
NextBioi 22488.
PROi Q05209.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q05209.
Bgeei Q05209.
CleanExi HS_PTPN12.
Genevestigatori Q05209.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR029021. Prot-tyrosine_phosphatase-like.
IPR012266. Ptpn_12.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000932. Tyr-Ptase_nr12. 1 hit.
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a human cDNA encoding a novel putative cytoplasmic protein-tyrosine-phosphatase."
    Takekawa M., Itoh F., Hinoda Y., Arimura Y., Toyota M., Sekiya M., Adachi M., Imai K., Yachi A.
    Biochem. Biophys. Res. Commun. 189:1223-1230(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-322.
    Tissue: Colon.
  2. "Cloning and expression of PTP-PEST. A novel, human, nontransmembrane protein tyrosine phosphatase."
    Yang Q., Co D., Sommercorn J., Tonks N.K.
    J. Biol. Chem. 268:6622-6628(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Erratum
    Yang Q., Co D., Sommercorn J., Tonks N.K.
    J. Biol. Chem. 268:17650-17650(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 495-517 AND 526-780.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS ILE-322 AND ALA-573.
    Tissue: Cerebellum and Tongue.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-322.
    Tissue: Brain.
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 1).
    Tissue: Testis.
  9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-8, ACETYLATION AT MET-1.
    Tissue: Platelet.
  10. "Chromosomal localization of the protein tyrosine phosphatase G1 gene and characterization of the aberrant transcripts in human colon cancer cells."
    Takekawa M., Itoh F., Hinoda Y., Adachi M., Ariyama T., Inazawa J., Imai K., Yachi A.
    FEBS Lett. 339:222-228(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-136 (ISOFORM 1), VARIANT COLON CANCER ARG-61.
  11. "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion."
    Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R., Sunder-Plassmann R., Reinherz E.L.
    EMBO J. 17:7320-7336(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSTPIP1.
  12. "Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST."
    Lu T.J., Lai W.Y., Huang C.Y., Hsieh W.J., Yu J.S., Hsieh Y.J., Chang W.T., Leu T.H., Chang W.C., Chuang W.J., Tang M.J., Chen T.Y., Lu T.L., Lai M.D.
    J. Biol. Chem. 281:38405-38417(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY STK24.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells."
    Sahu S.N., Nunez S., Bai G., Gupta A.
    Am. J. Physiol. 292:C2288-C2296(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTK2B/PYK2, FUNCTION.
  15. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689 AND THR-693, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-468; THR-519; SER-567; THR-569; SER-571; SER-603; SER-606; SER-608; SER-613; SER-689 AND THR-693, VARIANT [LARGE SCALE ANALYSIS] ILE-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-435; SER-449 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-332; SER-435; SER-449; SER-603; SER-606 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPTN12_HUMAN
AccessioniPrimary (citable) accession number: Q05209
Secondary accession number(s): A4D1C5
, B4DKY2, E9PBR5, E9PEH9, Q16130, Q59FD6, Q75MN8, Q86XU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 143 of the entry and version 3 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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