P43243 (MATR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Matrin-3

Gene names

Name:	MATR3
Synonyms:	KIAA0723

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	847 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 EIF2C1 and EIF2C2. Ref.9 Ref.11
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.23
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.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Domain	Repeat Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	nuclear inner membrane Traceable author statement Ref.8. Source: ProtInc nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro structural molecule activity Traceable author statement Ref.8. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NR4A1	P22736	2	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 847	846	Matrin-3		PRO_0000081622
Regions
	Domain	398 – 473	76	RRM 1
	Domain	496 – 571	76	RRM 2
	Zinc finger	801 – 832	32	Matrin-type
	Motif	710 – 718	9	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.7 Ref.19
	Modified residue	3	1	N6-acetyllysine Ref.19
	Modified residue	4	1	Phosphoserine Ref.20 Ref.22
	Modified residue	9	1	Phosphoserine Ref.22
	Modified residue	14	1	Phosphoserine Ref.20
	Modified residue	22	1	Phosphoserine Ref.18
	Modified residue	41	1	Phosphoserine Ref.20
	Modified residue	118	1	Phosphoserine Ref.18
	Modified residue	188	1	Phosphoserine Ref.10 Ref.12 Ref.13 Ref.16 Ref.17 Ref.20 Ref.22
	Modified residue	195	1	Phosphoserine Ref.16 Ref.20 Ref.22
	Modified residue	206	1	Phosphoserine Ref.13 Ref.20 Ref.22
	Modified residue	208	1	Phosphoserine Ref.16 Ref.20 Ref.22
	Modified residue	219	1	Phosphotyrosine Ref.22
	Modified residue	522	1	N6-acetyllysine Ref.19
	Modified residue	533	1	Phosphoserine Ref.16 Ref.20 Ref.22
	Modified residue	571	1	N6-acetyllysine Ref.19
	Modified residue	596	1	Phosphoserine Ref.16 Ref.22
	Modified residue	598	1	Phosphoserine Ref.16 Ref.20 Ref.22
	Modified residue	604	1	Phosphoserine Ref.16 Ref.20 Ref.22
	Modified residue	606	1	Phosphoserine Ref.20
	Modified residue	741	1	Phosphothreonine Ref.22
	Modified residue	747	1	Phosphoserine Ref.22
	Modified residue	766	1	Phosphoserine Ref.20 Ref.22
	Modified residue	836	1	N6-acetyllysine Ref.19
Natural variations
	Alternative sequence	1 – 304	304	MSKSF…VHSNK → MLGAQWRRNQPSRAAE in isoform 2.		VSP_042624
	Natural variant	85	1	S → C in MPD2. Ref.23 Corresponds to variant rs121434591 [ dbSNP | Ensembl ].		VAR_063421
Experimental info
	Sequence conflict	257	1	P → S in AAF17217. Ref.2
	Sequence conflict	274	1	P → S in AAF17217. Ref.2
	Sequence conflict	572	1	Y → C in AAF17217. Ref.2
	Sequence conflict	572	1	Y → C in M63483. Ref.8
	Sequence conflict	691	1	G → P in M63483. Ref.8
	Sequence conflict	703	1	D → H in M63483. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 24, 2001. Version 2. Checksum: 530AA49214BC1611	FASTA	847	94,623
	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
	Isoform 2 [UniParc]. Checksum: 7E7772B22A7AF741	FASTA	559	62,576
	10 20 30 40 50 60 MLGAQWRRNQ PSRAAEEWSQ HINGASHSRR CQLLLEIYPE WNPDNDTGHT MGDPFMLQQS 70 80 90 100 110 120 TNPAPGILGP PPPSFHLGGP AVGPRGNLGA GNGNLQGPRH MQKGRVETSR VVHIMDFQRG 130 140 150 160 170 180 KNLRYQLLQL VEPFGVISNH LILNKINEAF IEMATTEDAQ AAVDYYTTTP ALVFGKPVRV 190 200 210 220 230 240 HLSQKYKRIK KPEGKPDQKF DQKQELGRVI HLSNLPHSGY SDSAVLKLAE PYGKIKNYIL 250 260 270 280 290 300 MRMKSQAFIE METREDAMAM VDHCLKKALW FQGRCVKVDL SEKYKKLVLR IPNRGIDLLK 310 320 330 340 350 360 KDKSRKRSYS PDGKESPSDK KSKTDGSQKT ESSTEGKEQE EKSGEDGEKD TKDDQTEQEP 370 380 390 400 410 420 NMLLESEDEL LVDEEEAAAL LESGSSVGDE TDLANLGDVA SDGKKEPSDK AVKKDGSASA 430 440 450 460 470 480 AAKKKLKKVD KIEELDQENE AALENGIKNE ENTEPGAESS ENADDPNKDT SENADGQSDE 490 500 510 520 530 540 NKDDYTIPDE YRIGPYQPNV PVGIDYVIPK TGFYCKLCSL FYTNEEVAKN THCSSLPHYQ 550 KLKKFLNKLA EERRQKKET

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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, 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, MASS SPECTROMETRY. 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 EIF2C1 AND EIF2C2.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[18]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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, MASS SPECTROMETRY.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"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, MASS SPECTROMETRY.
[23]	"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. , 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.
IPI	IPI00017297. IPI00965324.
RefSeq	NP_001181883.1. NM_001194954.1. NP_001181884.1. NM_001194955.1. NP_001181885.1. NM_001194956.1. NP_061322.2. NM_018834.5. NP_954659.1. NM_199189.2.
UniGene	Hs.268939. Hs.595110.
3D structure databases
ProteinModelPortal	P43243.
ModBase	Search...
Protein-protein interaction databases
IntAct	P43243. 37 interactions.
MINT	MINT-4999417.
STRING	9606.ENSP00000354346.
PTM databases
PhosphoSite	P43243.
Polymorphism databases
DMDM	12643409.
Proteomic databases
PaxDb	P43243.
PRIDE	P43243.
Protocols and materials databases
DNASU	9782.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361059; ENSP00000354346; ENSG00000015479. ENST00000394805; ENSP00000378284; ENSG00000015479. ENST00000503811; ENSP00000423587; ENSG00000015479. ENST00000509990; ENSP00000423533; ENSG00000015479.
GeneID	9782.
KEGG	hsa:9782.
UCSC	uc003ldt.3. human. uc011czb.2. human.
Organism-specific databases
CTD	9782.
GeneCards	GC05P138609.
HGNC	HGNC:6912. MATR3.
HPA	CAB033552. HPA036564. HPA036565.
MIM	164015. gene. 606070. phenotype.
neXtProt	NX_P43243.
Orphanet	600. Distal myopathy with vocal cord weakness.
PharmGKB	PA30655.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG80010.
HOGENOM	HOG000015369.
HOVERGEN	HBG057347.
KO	K13213.
PhylomeDB	P43243.
Gene expression databases
ArrayExpress	P43243.
Bgee	P43243.
CleanEx	HS_MATR3.
Genevestigator	P43243.
GermOnline	ENSG00000015479. Homo sapiens.
Family and domain databases
Gene3D	3.30.70.330. 2 hits.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. IPR015880. Znf_C2H2-like. IPR000690. Znf_C2H2_matrin. IPR003604. Znf_U1. [Graphical view]
SMART	SM00360. RRM. 2 hits. SM00355. ZnF_C2H2. 1 hit. SM00451. ZnF_U1. 2 hits. [Graphical view]
PROSITE	PS50102. RRM. 2 hits. PS50171. ZF_MATRIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MATR3. human.
GenomeRNAi	9782.
NextBio	36832.
PMAP-CutDB	P43243.
SOURCE	Search...

Entry information

Entry name

MATR3_HUMAN

Accession

Primary (citable) accession number: P43243
Secondary accession number(s): B7ZAV5 , D3DQC3, Q9UHW0, Q9UQ27

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 24, 2001
Last modified:	May 29, 2013
This is version 144 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.