Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6DJT9 (PLAG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein PLAG1
Alternative name(s):
Pleiomorphic adenoma gene 1 protein
Gene names
Name:PLAG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor whose activation results in up-regulation of target genes, such as IGFII, leading to uncontrolled cell proliferation: when overexpressed in cultured cells, higher proliferation rate and transformation are observed. Other target genes such as CRLF1, CRABP2, CRIP2, PIGF are strongly induced in cells with PLAG1 induction. Proto-oncogene whose ectopic expression can trigger the development of pleomorphic adenomas of the salivary gland and lipoblastomas. Overexpression is associated with up-regulation of IGFII, is frequently observed in hepatoblastoma, common primary liver tumor in childhood. Cooperates with CBFB-MYH11, a fusion gene important for myeloid leukemia. Ref.11 Ref.13 Ref.15

Subunit structure

Interacts with KPNA2, which escorts protein to the nucleus via interaction with nuclear localization signal. Interacts with E3 SUMO-protein ligase PIAS1, PIAS2 and PIAS4. Ref.12 Ref.14

Subcellular location

Nucleus. Note: Strong nucleolar localization when sumoylation is inhibited. Ref.9 Ref.12 Ref.17

Tissue specificity

Expressed in fetal tissues such as lung, liver and kidney. Not detected or weak detection in normal adult tissues, but highly expressed in salivary gland with benign or malignant pleiomorphic adenomas with or without 8q12 aberrations, with preferential occurrence in benign tumors. Ref.1 Ref.6 Ref.8 Ref.13

Domain

C2H2-type zinc fingers 3 interacts with DNA-binding site G-clusterinc fingers. C2H2-type zinc fingers 6 and 7 interact with DNA-binding site core sequence.

Post-translational modification

Sumoylated with SUMO1; which inhibits transcriptional activity, but does not affect nuclear localization. Blockers of sumoylation pathway such as SENP3 and inactive UBE2I increases transcriptional capacity. Sumoylation is increased in the presence of PIAS1. Ref.14 Ref.17

Acetylated by lysine acetyltransferase EP300; which activates transcriptional capacity. Lysine residues that are sumoylated also seem to be target for acetylation. Ref.17

Involvement in disease

A chromosomal aberration involving PLAG1 is found in salivary gland pleiomorphic adenomas, the most common benign epithelial tumors of the salivary gland. Translocation t(3;8)(p21;q12) with constituvely expressed beta-catenin/CTNNB1. Fusion occurs in the 5'-regulatory regions, leading to promoter swapping between the 2 genes and activation of PLAG1 expression in adenomas. The chimeric transcript is formed by fusion of CTNNB1 exon 1 to PLAG1 exon 3. Reciprocal fusion transcript consisting of PLAG1 exon 1 and CTNNB1 exon 2-16 is also revealed in some adenomas. Translocation t(3;8)(p21;q12) with transcription elongation factor SII/TCEA1. The fusion transcript is composed of 5'-non-coding sequences as well as 63 nucleotides of the coding region of TCEA1 fused to the acceptor splice site of PLAG1 exon 3. The fusion transcript encodes a truncated TCEA1-PLAG1 protein of 90 AA as well as an apparently normal PLAG1 protein. Reciprocal fusion transcript PLAG1-TCEA1 is also present in one adenoma. Translocation t(5;8)(p13;q12) with leukemia inhibitory factor receptor LIFR. This fusion occured in the 5'-non-coding sequences of both genes, exchanging regulatory control element while preserving the coding sequences. Translocation t(6;8)(p21.3-22;q13) with Coiled-coil-helix-coiled-coil-helix domain-containing protein 7/CHCHD7. Fusion occurs in the 5' regulatory regions, leading to promoter swapping and up-regulation of PLAG1 expression. Ectopic expression of PLAG1 under the control of promoters of distinct translocation partner genes is a general pathogenetic mechanism for pleiomorphic adenomas with 8q aberrations. These fusion genes are likely to be found in adenomas with normal karyotype as this subgroup of tumors also exhibit PLAG1 activation.

A chromosomal aberration involving PLAG1 may be a cause of lipoblastomas, which are benign tumors resulting from transformation of adipocytes, usually diagnosed in children. 8q12.1 to 8q24.1 intrachromosomal rearrangement with hyaluronic acid synthase 2/HAS2 results in promoter swapping and activation of PLAG1 expression. The breakpoint of HAS2 gene is in PLAG1 intron 1, whereas its coding sequence starts at exon 2 or exon 3. Translocation t(7;8)(p22;q13) with collagen 1A2/COL1A2. Fusion transcript COL1A2-PLAG1 as well as HAS2-PLAG1 encode a full-length PLAG1 protein.

Miscellaneous

Residual nuclear import after mutation of the nuclear localization signal is assigned to zinc finger domains of PLAG1.

When cultured cells transformed by PLAG1 overexpression are injected in nude mouse, rapidly growing tumors (fibrosarcomaS) are observed at the site of inoculation.

Sequence similarities

Belongs to the krueppel C2H2-type zinc-finger protein family.

Contains 7 C2H2-type zinc fingers.

Sequence caution

The sequence BAD92368.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgland morphogenesis

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

organ growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of glial cell proliferation

Inferred from electronic annotation. Source: Ensembl

prostate gland growth

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: GOC

transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentnucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.6. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6DJT9-1)

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.
Isoform 2 (identifier: Q6DJT9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Zinc finger protein PLAG1
PRO_0000295107

Regions

Zinc finger34 – 5623C2H2-type 1
Zinc finger62 – 8625C2H2-type 2
Zinc finger92 – 11423C2H2-type 3
Zinc finger121 – 14323C2H2-type 4
Zinc finger150 – 17223C2H2-type 5
Zinc finger185 – 20723C2H2-type 6
Zinc finger213 – 23624C2H2-type 7
Region2 – 8483Interacts with KPNA2
Region41 – 242202Decreased nuclear import with localization in the nucleus but also in the cytoplasm
Region243 – 500258Activates transcription; Inhibition of nuclear import due to lack of NLS and KPNA2 interaction
Region243 – 384142Repression domain; contains 3 sumoylation motifs and massively decrease transcription activity
Region385 – 500116Massively activates transcription
Motif22 – 254Nuclear localization signal

Amino acid modifications

Cross-link244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-link263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Natural variations

Alternative sequence1 – 8282Missing in isoform 2.
VSP_045183
Natural variant4581P → T. Ref.1
Corresponds to variant rs35883156 [ dbSNP | Ensembl ].
VAR_033212

Experimental info

Mutagenesis23 – 242RK → AA: Inhibition of KPNA2 interaction when mutation occurs in the NLS; decreased nuclear import with localization in the nucleus but also in the cytoplasm; Complete inhibition of nuclear import when associated with a lack of zinc-finger domains. Ref.12
Mutagenesis31 – 322RK → AA: No inhibition of KPNA2 interaction and no change in nuclear import. Ref.12
Mutagenesis921H → A: Prevents formation of functional zinc-finger 3; induces drastic decrease of DNA affinity and complete modification of DNA binding specificity. Ref.9 Ref.12
Mutagenesis2271H → A: Prevents formation of functional zinc-finger 7 and inhibits DNA binding; No proliferation and transformation of cultured cells. Ref.9 Ref.11 Ref.12
Mutagenesis2441K → R: Abolishes single and double sumoylation; nuclear localization conserved. Increases transcriptional activity and inhibits repression domain activity; when associated with R-263 and R-353. Ref.12 Ref.14 Ref.17
Mutagenesis2631K → R: Decreases sumoylation; Abolishes double sumoylation only; Nuclear localization conserved. Increases transcriptional activity and inhibits repression domain activity; when associated with R-244 and R-353. Ref.12 Ref.14 Ref.17
Mutagenesis3391T → A: No effect on transcription activation capacity. Ref.6 Ref.12
Mutagenesis3401S → A: No effect on transcription activation capacity. Ref.6 Ref.12
Mutagenesis3531K → R: No effect on sumoylation. Increases transcriptional activity and inhibits repression domain activity; when associated with R-244 and R-263. Ref.12 Ref.14 Ref.17
Sequence conflict2761E → D in BAD92368. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: CF022A132A1BFD43

FASTA50055,909
        10         20         30         40         50         60 
MATVIPGDLS EVRDTQKVPS GKRKRGETKP RKNFPCQLCD KAFNSVEKLK VHSYSHTGER 

        70         80         90        100        110        120 
PYKCIQQDCT KAFVSKYKLQ RHMATHSPEK THKCNYCEKM FHRKDHLKNH LHTHDPNKET 

       130        140        150        160        170        180 
FKCEECGKNY NTKLGFKRHL ALHAATSGDL TCKVCLQTFE STGVLLEHLK SHAGKSSGGV 

       190        200        210        220        230        240 
KEKKHQCEHC DRRFYTRKDV RRHMVVHTGR KDFLCQYCAQ RFGRKDHLTR HMKKSHNQEL 

       250        260        270        280        290        300 
LKVKTEPVDF LDPFTCNVSV PIKDELLPVM SLPSSELLSK PFTNTLQLNL YNTPFQSMQS 

       310        320        330        340        350        360 
SGSAHQMITT LPLGMTCPID MDTVHPSHHL SFKYPFSSTS YAISIPEKEQ PLKGEIESYL 

       370        380        390        400        410        420 
MELQGGVPSS SQDSQASSSS KLGLDPQIGS LDDGAGDLSL SKSSISISDP LNTPALDFSQ 

       430        440        450        460        470        480 
LFNFIPLNGP PYNPLSVGSL GMSYSQEEAH SSVSQLPPQT QDLQDPANTI GLGSLHSLSA 

       490        500 
AFTSSLSTST TLPRFHQAFQ 

« Hide

Isoform 2 [UniParc].

Checksum: 00BA4A605A99B39C
Show »

FASTA41846,474

References

« Hide 'large scale' references
[1]"Promoter swapping between the genes for a novel zinc finger protein and beta-catenin in pleiomorphic adenomas with t(3;8)(p21;q12) translocations."
Kas K., Voz M.L., Roeijer E., Astroem A.-K., Meyen E., Stenman G., Van de Ven W.J.M.
Nat. Genet. 15:170-174(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH CTNNB1, VARIANT THR-458.
[2]"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. expand/collapse author list , 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] (ISOFORM 2).
Tissue: Tongue.
[3]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).
Tissue: Brain.
[4]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Brain.
[6]"Transcriptional activation capacity of the novel PLAG family of zinc finger proteins."
Kas K., Voz M.L., Hensen K., Meyen E., Van de Ven W.J.M.
J. Biol. Chem. 273:23026-23032(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF THR-339 AND SER-340.
[7]"The recurrent translocation t(5;8)(p13;q12) in pleomorphic adenomas results in upregulation of PLAG1 gene expression under control of the LIFR promoter."
Voz M.L., Astrom A.-K., Kas K., Mark J., Stenman G., Van de Ven W.J.M.
Oncogene 16:1409-1416(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH LIFR.
[8]"Conserved mechanism of PLAG1 activation in salivary gland tumors with and without chromosome 8q12 abnormalities: identification of SII as a new fusion partner gene."
Astroem A.-K., Voz M.L., Kas K., Roeijer E., Wedell B., Mandahl N., Van de Ven W., Mark J., Stenman G.
Cancer Res. 59:918-923(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH CTNNB1 AND TCEA1, TISSUE SPECIFICITY.
[9]"PLAG1, the main translocation target in pleomorphic adenoma of the salivary glands, is a positive regulator of IGF-II."
Voz M.L., Agten N.S., Van de Ven W.J.M., Kas K.
Cancer Res. 60:106-113(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DNA-BINDING, MUTAGENESIS OF HIS-92 AND HIS-227.
[10]"PLAG1 fusion oncogenes in lipoblastoma."
Hibbard M.K., Kozakewich H.P., Dal Cin P., Sciot R., Tan X., Xiao S., Fletcher J.A.
Cancer Res. 60:4869-4872(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL REARRANGEMENT WITH HAS2 AND COL1A2.
[11]"The tumorigenic diversity of the three PLAG family members is associated with different DNA binding capacities."
Hensen K., Van Valckenborgh I.C.C., Kas K., Van de Ven W.J.M., Voz M.L.
Cancer Res. 62:1510-1517(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF HIS-227.
[12]"Identification of a karyopherin alpha 2 recognition site in PLAG1, which functions as a nuclear localization signal."
Braem C.V., Kas K., Meyen E., Debiec-Rychter M., Van De Ven W.J.M., Voz M.L.
J. Biol. Chem. 277:19673-19678(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KPNA2, SUBCELLULAR LOCATION, MUTAGENESIS OF 23-ARG-LYS-24 AND 31-ARG-LYS-32.
[13]"Amplification and overexpression of the IGF2 regulator PLAG1 in hepatoblastoma."
Zatkova A., Rouillard J.-M., Hartmann W., Lamb B.J., Kuick R., Eckart M., von Schweinitz D., Koch A., Fonatsch C., Pietsch T., Hanash S.M., Wimmer K.
Genes Chromosomes Cancer 39:126-137(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[14]"Repression of the transactivating capacity of the oncoprotein PLAG1 by SUMOylation."
Van Dyck F., Delvaux E.L.D., Van de Ven W.J.M., Chavez M.V.
J. Biol. Chem. 279:36121-36131(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, MUTAGENESIS OF LYS-244; LYS-263 AND LYS-353, INTERACTION WITH PIAS PROTEINS.
[15]"Microarray screening for target genes of the proto-oncogene PLAG1."
Voz M.L., Mathys J., Hensen K., Pendeville H., Van Valckenborgh I., Van Huffel C., Chavez M., Van Damme B., De Moor B., Moreau Y., Van de Ven W.J.
Oncogene 23:179-191(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"PLAG1-HAS2 fusion in lipoblastoma with masked 8q intrachromosomal rearrangement."
Morerio C., Rapella A., Rosanda C., Tassano E., Gambini C., Romagnoli G., Panarello C.
Cancer Genet. Cytogenet. 156:183-184(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL REARRANGEMENT WITH HAS2.
[17]"Sumoylation and acetylation play opposite roles in the transactivation of PLAG1 and PLAGL2."
Zheng G., Yang Y.-C.
J. Biol. Chem. 280:40773-40781(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, ACETYLATION, MUTAGENESIS OF LYS-244; LYS-263 AND LYS-353, SUBCELLULAR LOCATION.
[18]"CHCHD7-PLAG1 and TCEA1-PLAG1 gene fusions resulting from cryptic, intrachromosomal 8q rearrangements in pleomorphic salivary gland adenomas."
Asp J., Persson F., Kost-Alimova M., Stenman G.
Genes Chromosomes Cancer 45:820-828(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL REARRANGEMENT WITH CHCHD7 AND TCEA1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U65002 mRNA. Translation: AAC50995.1.
AK296933 mRNA. Translation: BAG59484.1.
AB209131 mRNA. Translation: BAD92368.1. Different initiation.
AC107952 Genomic DNA. No translation available.
BC075047 mRNA. Translation: AAH75047.1.
BC075048 mRNA. Translation: AAH75048.1.
CCDSCCDS47860.1. [Q6DJT9-2]
CCDS6165.1. [Q6DJT9-1]
RefSeqNP_001108106.1. NM_001114634.1. [Q6DJT9-1]
NP_001108107.1. NM_001114635.1. [Q6DJT9-2]
NP_002646.2. NM_002655.2. [Q6DJT9-1]
XP_005251317.1. XM_005251260.1. [Q6DJT9-1]
UniGeneHs.14968.

3D structure databases

ProteinModelPortalQ6DJT9.
SMRQ6DJT9. Positions 32-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111340. 7 interactions.
IntActQ6DJT9. 3 interactions.
MINTMINT-1188755.
STRING9606.ENSP00000325546.

PTM databases

PhosphoSiteQ6DJT9.

Polymorphism databases

DMDM74757442.

Proteomic databases

MaxQBQ6DJT9.
PaxDbQ6DJT9.
PRIDEQ6DJT9.

Protocols and materials databases

DNASU5324.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316981; ENSP00000325546; ENSG00000181690. [Q6DJT9-1]
ENST00000423799; ENSP00000404067; ENSG00000181690. [Q6DJT9-2]
ENST00000429357; ENSP00000416537; ENSG00000181690. [Q6DJT9-1]
GeneID5324.
KEGGhsa:5324.
UCSCuc003xsq.4. human. [Q6DJT9-1]

Organism-specific databases

CTD5324.
GeneCardsGC08M057073.
HGNCHGNC:9045. PLAG1.
MIM181030. phenotype.
603026. gene.
neXtProtNX_Q6DJT9.
PharmGKBPA33378.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000294191.
HOVERGENHBG053608.
InParanoidQ6DJT9.
OMAIDMDAVH.
OrthoDBEOG71K62Q.
PhylomeDBQ6DJT9.
TreeFamTF332024.

Enzyme and pathway databases

SignaLinkQ6DJT9.

Gene expression databases

ArrayExpressQ6DJT9.
BgeeQ6DJT9.
CleanExHS_PLAG1.
GenevestigatorQ6DJT9.

Family and domain databases

Gene3D3.30.160.60. 5 hits.
InterProIPR027775. C2H2_Znf_fam.
IPR027765. PLAG1.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERPTHR10032. PTHR10032. 1 hit.
PTHR10032:SF124. PTHR10032:SF124. 1 hit.
PfamPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 7 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLAG1. human.
GeneWikiPLAG1.
GenomeRNAi5324.
NextBio20594.
PROQ6DJT9.
SOURCESearch...

Entry information

Entry namePLAG1_HUMAN
AccessionPrimary (citable) accession number: Q6DJT9
Secondary accession number(s): B4DLC2, Q59GH8, Q9Y4L2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM