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P43243 (MATR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrin-3
Gene names
Name:MATR3
Synonyms:KIAA0723
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length847 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Ref.9

Subunit structure

Part of complex consisting of SFPQ, NONO and MATR3. Interacts with AGO1 and AGO2. Part of a complex composed at least of ASCL2, C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Ref.9 Ref.11 Ref.18

Subcellular location

Nucleus matrix.

Involvement in disease

Myopathy, distal, 2 (MPD2) [MIM:606070]: A muscular disorder characterized by distal weakness, with onset in hands and feet, associated with vocal cord and pharyngeal weakness causing a nasal voice and swallowing disorders.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25

Sequence similarities

Contains 1 matrin-type zinc finger.

Contains 2 RRM (RNA recognition motif) domains.

Sequence caution

The sequence AAF17217.1 differs from that shown. Reason: Frameshift at several positions.

The sequence BAA34443.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NR4A1P227362EBI-352602,EBI-721550

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P43243-1)

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: P43243-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-304: MSKSFQQSSL...ICDLPVHSNK → MLGAQWRRNQPSRAAE
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 847846Matrin-3
PRO_0000081622

Regions

Domain398 – 47376RRM 1
Domain496 – 57176RRM 2
Zinc finger801 – 83232Matrin-type
Motif710 – 7189Nuclear localization signal Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.7 Ref.20 Ref.24
Modified residue31N6-acetyllysine Ref.20
Modified residue41Phosphoserine Ref.21 Ref.23
Modified residue91Phosphoserine Ref.23
Modified residue141Phosphoserine Ref.21
Modified residue221Phosphoserine Ref.19
Modified residue411Phosphoserine Ref.21
Modified residue1181Phosphoserine Ref.19
Modified residue1881Phosphoserine Ref.10 Ref.12 Ref.13 Ref.16 Ref.17 Ref.21 Ref.23
Modified residue1951Phosphoserine Ref.16 Ref.21 Ref.23
Modified residue2061Phosphoserine Ref.13 Ref.21 Ref.23
Modified residue2081Phosphoserine Ref.16 Ref.21 Ref.23
Modified residue2191Phosphotyrosine Ref.23
Modified residue5221N6-acetyllysine Ref.20
Modified residue5331Phosphoserine Ref.16 Ref.21 Ref.23
Modified residue5711N6-acetyllysine Ref.20
Modified residue5961Phosphoserine Ref.16 Ref.23
Modified residue5981Phosphoserine Ref.16 Ref.21 Ref.23
Modified residue6041Phosphoserine Ref.16 Ref.21 Ref.23
Modified residue6061Phosphoserine Ref.21
Modified residue7411Phosphothreonine Ref.23
Modified residue7471Phosphoserine Ref.23
Modified residue7661Phosphoserine Ref.21 Ref.23
Modified residue8361N6-acetyllysine Ref.20

Natural variations

Alternative sequence1 – 304304MSKSF…VHSNK → MLGAQWRRNQPSRAAE in isoform 2.
VSP_042624
Natural variant851S → C in MPD2. Ref.25
Corresponds to variant rs121434591 [ dbSNP | Ensembl ].
VAR_063421

Experimental info

Sequence conflict2571P → S in AAF17217. Ref.2
Sequence conflict2741P → S in AAF17217. Ref.2
Sequence conflict5721Y → C in AAF17217. Ref.2
Sequence conflict5721Y → C in M63483. Ref.8
Sequence conflict6911G → P in M63483. Ref.8
Sequence conflict7031D → H in M63483. Ref.8

Sequences

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

Last modified January 24, 2001. Version 2.
Checksum: 530AA49214BC1611

FASTA84794,623
        10         20         30         40         50         60 
MSKSFQQSSL SRDSQGHGRD LSAAGIGLLA AATQSLSMPA SLGRMNQGTA RLASLMNLGM 

        70         80         90        100        110        120 
SSSLNQQGAH SALSSASTSS HNLQSIFNIG SRGPLPLSSQ HRGDADQASN ILASFGLSAR 

       130        140        150        160        170        180 
DLDELSRYPE DKITPENLPQ ILLQLKRRRT EEGPTLSYGR DGRSATREPP YRVPRDDWEE 

       190        200        210        220        230        240 
KRHFRRDSFD DRGPSLNPVL DYDHGSRSQE SGYYDRMDYE DDRLRDGERC RDDSFFGETS 

       250        260        270        280        290        300 
HNYHKFDSEY ERMGRGPGPL QERSLFEKKR GAPPSSNIED FHGLLPKGYP HLCSICDLPV 

       310        320        330        340        350        360 
HSNKEWSQHI NGASHSRRCQ LLLEIYPEWN PDNDTGHTMG DPFMLQQSTN PAPGILGPPP 

       370        380        390        400        410        420 
PSFHLGGPAV GPRGNLGAGN GNLQGPRHMQ KGRVETSRVV HIMDFQRGKN LRYQLLQLVE 

       430        440        450        460        470        480 
PFGVISNHLI LNKINEAFIE MATTEDAQAA VDYYTTTPAL VFGKPVRVHL SQKYKRIKKP 

       490        500        510        520        530        540 
EGKPDQKFDQ KQELGRVIHL SNLPHSGYSD SAVLKLAEPY GKIKNYILMR MKSQAFIEME 

       550        560        570        580        590        600 
TREDAMAMVD HCLKKALWFQ GRCVKVDLSE KYKKLVLRIP NRGIDLLKKD KSRKRSYSPD 

       610        620        630        640        650        660 
GKESPSDKKS KTDGSQKTES STEGKEQEEK SGEDGEKDTK DDQTEQEPNM LLESEDELLV 

       670        680        690        700        710        720 
DEEEAAALLE SGSSVGDETD LANLGDVASD GKKEPSDKAV KKDGSASAAA KKKLKKVDKI 

       730        740        750        760        770        780 
EELDQENEAA LENGIKNEEN TEPGAESSEN ADDPNKDTSE NADGQSDENK DDYTIPDEYR 

       790        800        810        820        830        840 
IGPYQPNVPV GIDYVIPKTG FYCKLCSLFY TNEEVAKNTH CSSLPHYQKL KKFLNKLAEE 


RRQKKET 

« Hide

Isoform 2 [UniParc].

Checksum: 7E7772B22A7AF741
Show »

FASTA55962,576

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hypothalamus.
[3]"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: Testis.
[4]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Skin.
[7]Bienvenut W.V., Matallanas D., Kolch W.
Submitted (JUL-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12; 150-160; 187-207 AND 374-387, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Mammary carcinoma.
[8]"Molecular cloning of matrin 3. A 125-kilodalton protein of the nuclear matrix contains an extensive acidic domain."
Belgrader P., Dey R., Berezney R.
J. Biol. Chem. 266:9893-9899(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 432-847 (ISOFORM 1).
[9]"The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs."
Zhang Z., Carmichael G.G.
Cell 106:465-475(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, IDENTIFICATION IN A COMPLEX WITH SFPQ AND NONO.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGO1 AND AGO2.
[12]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-188 AND SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[15]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-195; SER-208; SER-533; SER-596; SER-598 AND SER-604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[18]"Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation."
Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.
J. Biol. Chem. 284:7542-7552(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH ZNF335; MKI67; C11ORF30; ZNF335; HSPA8; TUBB2A; CCAR2; ASCL2; RBBP5 AND WDR5.
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-3; LYS-522; LYS-571 AND LYS-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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-4; SER-14; SER-41; SER-188; SER-195; SER-206; SER-208; SER-533; SER-598; SER-604; SER-606 AND SER-766, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"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-4; SER-9; SER-188; SER-195; SER-206; SER-208; TYR-219; SER-533; SER-596; SER-598; SER-604; THR-741; SER-747 AND SER-766, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Autosomal-dominant distal myopathy associated with a recurrent missense mutation in the gene encoding the nuclear matrix protein, matrin 3."
Senderek J., Garvey S.M., Krieger M., Guergueltcheva V., Urtizberea A., Roos A., Elbracht M., Stendel C., Tournev I., Mihailova V., Feit H., Tramonte J., Hedera P., Crooks K., Bergmann C., Rudnik-Schoeneborn S., Zerres K., Lochmueller H. expand/collapse author list , Seboun E., Weis J., Beckmann J.S., Hauser M.A., Jackson C.E.
Am. J. Hum. Genet. 84:511-518(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPD2 CYS-85.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB018266 mRNA. Translation: BAA34443.2. Different initiation.
AF117236 mRNA. Translation: AAF17217.1. Frameshift.
AK316420 mRNA. Translation: BAH14791.1.
AC011404 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62114.1.
CH471062 Genomic DNA. Translation: EAW62115.1.
CH471062 Genomic DNA. Translation: EAW62116.1.
CH471062 Genomic DNA. Translation: EAW62117.1.
BC015031 mRNA. Translation: AAH15031.1.
M63483 mRNA. No translation available.
RefSeqNP_001181883.1. NM_001194954.1.
NP_001181884.1. NM_001194955.1.
NP_001181885.1. NM_001194956.1.
NP_001269207.1. NM_001282278.1.
NP_061322.2. NM_018834.5.
NP_954659.1. NM_199189.2.
UniGeneHs.268939.
Hs.595110.

3D structure databases

ProteinModelPortalP43243.
SMRP43243. Positions 390-576.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115126. 59 interactions.
IntActP43243. 50 interactions.
MINTMINT-4999417.
STRING9606.ENSP00000354346.

PTM databases

PhosphoSiteP43243.

Polymorphism databases

DMDM12643409.

Proteomic databases

PaxDbP43243.
PRIDEP43243.

Protocols and materials databases

DNASU9782.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361059; ENSP00000354346; ENSG00000015479. [P43243-1]
ENST00000394805; ENSP00000378284; ENSG00000015479. [P43243-1]
ENST00000503811; ENSP00000423587; ENSG00000015479. [P43243-2]
ENST00000509990; ENSP00000423533; ENSG00000015479. [P43243-1]
GeneID9782.
KEGGhsa:9782.
UCSCuc003ldt.3. human. [P43243-1]
uc011czb.2. human. [P43243-2]

Organism-specific databases

CTD9782.
GeneCardsGC05P138609.
HGNCHGNC:6912. MATR3.
HPACAB033552.
HPA036564.
HPA036565.
MIM164015. gene.
606070. phenotype.
neXtProtNX_P43243.
Orphanet600. Distal myopathy with vocal cord weakness.
PharmGKBPA30655.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80010.
HOGENOMHOG000015369.
HOVERGENHBG057347.
KOK13213.
OrthoDBEOG7GJ6C8.
PhylomeDBP43243.
TreeFamTF333921.

Gene expression databases

ArrayExpressP43243.
BgeeP43243.
CleanExHS_MATR3.
GenevestigatorP43243.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR015880. Znf_C2H2-like.
IPR000690. Znf_C2H2_matrin.
IPR003604. Znf_U1.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
SM00355. ZnF_C2H2. 1 hit.
SM00451. ZnF_U1. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
PS50171. ZF_MATRIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMATR3. human.
GeneWikiMATR3.
GenomeRNAi9782.
NextBio36832.
PMAP-CutDBP43243.
PROP43243.
SOURCESearch...

Entry information

Entry nameMATR3_HUMAN
AccessionPrimary (citable) accession number: P43243
Secondary accession number(s): B7ZAV5 expand/collapse secondary AC list , D3DQC3, Q9UHW0, Q9UQ27
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 24, 2001
Last modified: April 16, 2014
This is version 153 of the entry and version 2 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 5

Human chromosome 5: entries, gene names and cross-references to MIM