ZMAT2_MOUSE
ID ZMAT2_MOUSE Reviewed; 199 AA.
AC Q9CPW7; Q5EBK0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Zinc finger matrin-type protein 2;
GN Name=Zmat2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the
CC spliceosome. {ECO:0000250|UniProtKB:Q96NC0}.
CC -!- SUBUNIT: Component of the spliceosome B complex.
CC {ECO:0000250|UniProtKB:Q96NC0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96NC0}.
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DR EMBL; AK008717; BAB25852.1; -; mRNA.
DR EMBL; AK012091; BAB28023.1; -; mRNA.
DR EMBL; BC024881; AAH24881.1; -; mRNA.
DR EMBL; BC089501; AAH89501.1; -; mRNA.
DR CCDS; CCDS37773.1; -.
DR RefSeq; NP_079870.1; NM_025594.3.
DR AlphaFoldDB; Q9CPW7; -.
DR SMR; Q9CPW7; -.
DR BioGRID; 211513; 7.
DR STRING; 10090.ENSMUSP00000001419; -.
DR PhosphoSitePlus; Q9CPW7; -.
DR EPD; Q9CPW7; -.
DR MaxQB; Q9CPW7; -.
DR PaxDb; Q9CPW7; -.
DR PeptideAtlas; Q9CPW7; -.
DR PRIDE; Q9CPW7; -.
DR ProteomicsDB; 302063; -.
DR Antibodypedia; 27104; 170 antibodies from 24 providers.
DR DNASU; 66492; -.
DR Ensembl; ENSMUST00000001419; ENSMUSP00000001419; ENSMUSG00000001383.
DR GeneID; 66492; -.
DR KEGG; mmu:66492; -.
DR UCSC; uc008eos.1; mouse.
DR CTD; 153527; -.
DR MGI; MGI:1913742; Zmat2.
DR VEuPathDB; HostDB:ENSMUSG00000001383; -.
DR eggNOG; KOG4727; Eukaryota.
DR GeneTree; ENSGT00390000010712; -.
DR HOGENOM; CLU_067237_1_1_1; -.
DR InParanoid; Q9CPW7; -.
DR OMA; FKDNLQW; -.
DR OrthoDB; 1626636at2759; -.
DR PhylomeDB; Q9CPW7; -.
DR TreeFam; TF314475; -.
DR BioGRID-ORCS; 66492; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Zmat2; mouse.
DR PRO; PR:Q9CPW7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9CPW7; protein.
DR Bgee; ENSMUSG00000001383; Expressed in motor neuron and 257 other tissues.
DR Genevisible; Q9CPW7; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR040107; Snu23.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR45986; PTHR45986; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
PE 2: Evidence at transcript level;
KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Spliceosome; Ubl conjugation;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
FT CHAIN 2..199
FT /note="Zinc finger matrin-type protein 2"
FT /id="PRO_0000047328"
FT ZN_FING 80..104
FT /note="Matrin-type"
FT REGION 27..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
FT CROSSLNK 45
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
FT CROSSLNK 55
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96NC0"
SQ SEQUENCE 199 AA; 23612 MW; EF419358B7977E36 CRC64;
MASGSGTKNL DFRRKWDKDE YEKLAEKRLT EEREKKDGKP VQPVKRELLR HRDYKVDLES
KLGKTIVITK TTPQSEMGGY YCNVCDCVVK DSINFLDHIN GKKHQRNLGM SMRVERSTLD
QVKKRFEVNK KKMEEKQKDY DFEERMKELR EEEEKAKAYK KEKQKEKKRR AEEDLTFEED
DEMAAVMGFS GFGSTKKSY
