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Q16825

- PTN21_HUMAN

UniProt

Q16825 - PTN21_HUMAN

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Protein

Tyrosine-protein phosphatase non-receptor type 21

Gene
PTPN21, PTPD1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1067 – 10671Substrate Reviewed prediction
Active sitei1108 – 11081Phosphocysteine intermediate By similarity
Binding sitei1152 – 11521Substrate By similarity

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein tyrosine phosphatase activity Source: ProtInc

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 21 (EC:3.1.3.48)
Alternative name(s):
Protein-tyrosine phosphatase D1
Gene namesi
Name:PTPN21
Synonyms:PTPD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:9651. PTPN21.

Subcellular locationi

Cytoplasmcytoskeleton By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33994.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11741174Tyrosine-protein phosphatase non-receptor type 21PRO_0000219439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei577 – 5771Phosphoserine By similarity
Modified residuei637 – 6371Phosphoserine1 Publication
Modified residuei804 – 8041Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ16825.
PaxDbiQ16825.
PRIDEiQ16825.

PTM databases

PhosphoSiteiQ16825.

Expressioni

Gene expression databases

ArrayExpressiQ16825.
BgeeiQ16825.
CleanExiHS_PTPN21.
GenevestigatoriQ16825.

Organism-specific databases

HPAiCAB011468.
HPA049110.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Akap1O08715-52EBI-2860264,EBI-9117988From a different organism.
SRCP129312EBI-2860264,EBI-621482

Protein-protein interaction databases

BioGridi116280. 3 interactions.
IntActiQ16825. 4 interactions.
STRINGi9606.ENSP00000330276.

Structurei

3D structure databases

ProteinModelPortaliQ16825.
SMRiQ16825. Positions 36-306, 882-1171.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 308286FERMAdd
BLAST
Domaini896 – 1167272Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1108 – 11147Substrate binding By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi340 – 3434Poly-Pro
Compositional biasi565 – 57410Poly-Pro
Compositional biasi712 – 7176Poly-Glu

Sequence similaritiesi

Contains 1 FERM domain.

Phylogenomic databases

eggNOGiCOG5599.
HOGENOMiHOG000115775.
HOVERGENiHBG053757.
InParanoidiQ16825.
KOiK18025.
OMAiAPNIMRT.
OrthoDBiEOG7PK8XS.
PhylomeDBiQ16825.
TreeFamiTF315900.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
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.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR014392. Tyr_Pase_non-rcpt_typ-14/21.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000934. Tyr-Ptase_nr14. 1 hit.
PRINTSiPR00935. BAND41.
PR00700. PRTYPHPHTASE.
SMARTiSM00295. B41. 1 hit.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q16825-1 [UniParc]FASTAAdd to Basket

« Hide

MPLPFGLKLK RTRRYTVSSK SCLVARIQLL NNEFVEFTLS VESTGQESLE     50
AVAQRLELRE VTYFSLWYYN KQNQRRWVDL EKPLKKQLDK YALEPTVYFG 100
VVFYVPSVSQ LQQEITRYQY YLQLKKDILE GSIPCTLEQA IQLAGLAVQA 150
DFGDFDQYES QDFLQKFALF PVGWLQDEKV LEEATQKVAL LHQKYRGLTA 200
PDAEMLYMQE VERMDGYGEE SYPAKDSQGS DISIGACLEG IFVKHKNGRH 250
PVVFRWHDIA NMSHNKSFFA LELANKEETI QFQTEDMETA KYIWRLCVAR 300
HKFYRLNQCN LQTQTVTVNP IRRRSSSRMS LPKPQPYVMP PPPQLHYNGH 350
YTEPYASSQD NLFVPNQNGY YCHSQTSLDR AQIDLNGRIR NGSVYSAHST 400
NSLNNPQPYL QPSPMSSNPS ITGSDVMRPD YLPSHRHSAV IPPSYRPTPD 450
YETVMKQLNR GLVHAERQSH SLRNLNIGSS YAYSRPAALV YSQPEIREHA 500
QLPSPAAAHC PFSLSYSFHS PSPYPYPAER RPVVGAVSVP ELTNAQLQAQ 550
DYPSPNIMRT QVYRPPPPYP PPRPANSTPD LSRHLYISSS NPDLITRRVH 600
HSVQTFQEDS LPVAHSLQEV SEPLTAARHA QLHKRNSIEV AGLSHGLEGL 650
RLKERTLSAS AAEVAPRAVS VGSQPSVFTE RTQREGPEEA EGLRYGHKKS 700
LSDATMLIHS SEEEEDEDFE EESGARAPPA RAREPRPGLA QDPPGCPRVL 750
LAGPLHILEP KAHVPDAEKR MMDSSPVRTT AEAQRPWRDG LLMPSMSESD 800
LTTSGRYRAR RDSLKKRPVS DLLSGKKNIV EGLPPLGGMK KTRVDAKKIG 850
PLKLAALNGL SLSRVPLPDE GKEVATRATN DERCKILEQR LEQGMVFTEY 900
ERILKKRLVD GECSTARLPE NAERNRFQDV LPYDDVRVEL VPTKENNTGY 950
INASHIKVSV SGIEWDYIAT QGPLQNTCQD FWQMVWEQGI AIIAMVTAEE 1000
EGGREKSFRY WPRLGSRHNT VTYGRFKITT RFRTDSGCYA TTGLKMKHLL 1050
TGQERTVWHL QYTDWPEHGC PEDLKGFLSY LEEIQSVRRH TNSTSDPQSP 1100
NPPLLVHCSA GVGRTGVVIL SEIMIACLEH NEVLDIPRVL DMLRQQRMML 1150
VQTLCQYTFV YRVLIQFLKS SRLI 1174
Length:1,174
Mass (Da):133,281
Last modified:March 2, 2010 - v2
Checksum:i5B746C824578F117
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti385 – 3851L → F.1 Publication
Corresponds to variant rs2401751 [ dbSNP | Ensembl ].
VAR_060341
Natural varianti906 – 9061K → N.
Corresponds to variant rs12879993 [ dbSNP | Ensembl ].
VAR_055539
Natural varianti936 – 9361V → A.1 Publication
Corresponds to variant rs2274736 [ dbSNP | Ensembl ].
VAR_060342

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X79510 mRNA. Translation: CAA56042.1.
AL162171 Genomic DNA. No translation available.
CCDSiCCDS9884.1.
PIRiI38140.
RefSeqiNP_008970.2. NM_007039.3.
XP_005267344.1. XM_005267287.1.
UniGeneiHs.437040.

Genome annotation databases

EnsembliENST00000328736; ENSP00000330276; ENSG00000070778.
ENST00000556564; ENSP00000452414; ENSG00000070778.
GeneIDi11099.
KEGGihsa:11099.
UCSCiuc001xwv.4. human.

Polymorphism databases

DMDMi290457654.

Keywords - Coding sequence diversityi

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
X79510 mRNA. Translation: CAA56042.1 .
AL162171 Genomic DNA. No translation available.
CCDSi CCDS9884.1.
PIRi I38140.
RefSeqi NP_008970.2. NM_007039.3.
XP_005267344.1. XM_005267287.1.
UniGenei Hs.437040.

3D structure databases

ProteinModelPortali Q16825.
SMRi Q16825. Positions 36-306, 882-1171.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116280. 3 interactions.
IntActi Q16825. 4 interactions.
STRINGi 9606.ENSP00000330276.

PTM databases

PhosphoSitei Q16825.

Polymorphism databases

DMDMi 290457654.

Proteomic databases

MaxQBi Q16825.
PaxDbi Q16825.
PRIDEi Q16825.

Protocols and materials databases

DNASUi 11099.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000328736 ; ENSP00000330276 ; ENSG00000070778 .
ENST00000556564 ; ENSP00000452414 ; ENSG00000070778 .
GeneIDi 11099.
KEGGi hsa:11099.
UCSCi uc001xwv.4. human.

Organism-specific databases

CTDi 11099.
GeneCardsi GC14M088932.
H-InvDB HIX0037798.
HGNCi HGNC:9651. PTPN21.
HPAi CAB011468.
HPA049110.
MIMi 603271. gene.
neXtProti NX_Q16825.
PharmGKBi PA33994.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
HOGENOMi HOG000115775.
HOVERGENi HBG053757.
InParanoidi Q16825.
KOi K18025.
OMAi APNIMRT.
OrthoDBi EOG7PK8XS.
PhylomeDBi Q16825.
TreeFami TF315900.

Miscellaneous databases

GeneWikii PTPN21.
GenomeRNAii 11099.
NextBioi 42194.
PROi Q16825.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16825.
Bgeei Q16825.
CleanExi HS_PTPN21.
Genevestigatori Q16825.

Family and domain databases

Gene3Di 1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
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.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR014392. Tyr_Pase_non-rcpt_typ-14/21.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000934. Tyr-Ptase_nr14. 1 hit.
PRINTSi PR00935. BAND41.
PR00700. PRTYPHPHTASE.
SMARTi SM00295. B41. 1 hit.
SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF47031. SSF47031. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
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. "Src kinase associates with a member of a distinct subfamily of protein-tyrosine phosphatases containing an ezrin-like domain."
    Moeller N.P.H., Moeller K.B., Lammers R., Kharitonenkov A., Sures I., Ullrich A.
    Proc. Natl. Acad. Sci. U.S.A. 91:7477-7481(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PHE-385 AND ALA-936.
    Tissue: Skeletal muscle.
  2. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPTN21_HUMAN
AccessioniPrimary (citable) accession number: Q16825
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 2, 2010
Last modified: July 9, 2014
This is version 123 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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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