ZMAT2_HUMAN
ID ZMAT2_HUMAN Reviewed; 199 AA.
AC Q96NC0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Zinc finger matrin-type protein 2;
GN Name=ZMAT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-45 AND LYS-64, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-36; LYS-39; LYS-45;
RP LYS-55; LYS-61; LYS-64; LYS-70; LYS-102 AND LYS-123, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [8] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the
CC spliceosome. {ECO:0000269|PubMed:28781166}.
CC -!- SUBUNIT: Component of the spliceosome B complex.
CC {ECO:0000269|PubMed:28781166}.
CC -!- INTERACTION:
CC Q96NC0; Q96MA6: AK8; NbExp=3; IntAct=EBI-2682299, EBI-8466265;
CC Q96NC0; Q92870-2: APBB2; NbExp=3; IntAct=EBI-2682299, EBI-21535880;
CC Q96NC0; P54253: ATXN1; NbExp=6; IntAct=EBI-2682299, EBI-930964;
CC Q96NC0; P54252: ATXN3; NbExp=3; IntAct=EBI-2682299, EBI-946046;
CC Q96NC0; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-2682299, EBI-11975051;
CC Q96NC0; Q9P1Z2: CALCOCO1; NbExp=3; IntAct=EBI-2682299, EBI-749920;
CC Q96NC0; Q8NA61: CBY2; NbExp=3; IntAct=EBI-2682299, EBI-741724;
CC Q96NC0; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-2682299, EBI-2808286;
CC Q96NC0; Q01850: CDR2; NbExp=3; IntAct=EBI-2682299, EBI-1181367;
CC Q96NC0; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-2682299, EBI-742887;
CC Q96NC0; A1L4K1: FSD2; NbExp=3; IntAct=EBI-2682299, EBI-5661036;
CC Q96NC0; P51114-2: FXR1; NbExp=3; IntAct=EBI-2682299, EBI-11022345;
CC Q96NC0; P51116: FXR2; NbExp=6; IntAct=EBI-2682299, EBI-740459;
CC Q96NC0; Q08379: GOLGA2; NbExp=6; IntAct=EBI-2682299, EBI-618309;
CC Q96NC0; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2682299, EBI-5916454;
CC Q96NC0; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-2682299, EBI-717919;
CC Q96NC0; P54257: HAP1; NbExp=3; IntAct=EBI-2682299, EBI-712814;
CC Q96NC0; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-2682299, EBI-2549423;
CC Q96NC0; P42858: HTT; NbExp=20; IntAct=EBI-2682299, EBI-466029;
CC Q96NC0; Q13422: IKZF1; NbExp=3; IntAct=EBI-2682299, EBI-745305;
CC Q96NC0; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-2682299, EBI-2556193;
CC Q96NC0; Q6A162: KRT40; NbExp=3; IntAct=EBI-2682299, EBI-10171697;
CC Q96NC0; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2682299, EBI-741037;
CC Q96NC0; P50222: MEOX2; NbExp=3; IntAct=EBI-2682299, EBI-748397;
CC Q96NC0; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-2682299, EBI-742948;
CC Q96NC0; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2682299, EBI-11522433;
CC Q96NC0; Q15742: NAB2; NbExp=3; IntAct=EBI-2682299, EBI-8641936;
CC Q96NC0; Q92597: NDRG1; NbExp=3; IntAct=EBI-2682299, EBI-716486;
CC Q96NC0; P61970: NUTF2; NbExp=3; IntAct=EBI-2682299, EBI-591778;
CC Q96NC0; Q96CV9: OPTN; NbExp=4; IntAct=EBI-2682299, EBI-748974;
CC Q96NC0; Q7Z412: PEX26; NbExp=3; IntAct=EBI-2682299, EBI-752057;
CC Q96NC0; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-2682299, EBI-713786;
CC Q96NC0; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2682299, EBI-79165;
CC Q96NC0; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2682299, EBI-25882629;
CC Q96NC0; P41219: PRPH; NbExp=3; IntAct=EBI-2682299, EBI-752074;
CC Q96NC0; P49768-2: PSEN1; NbExp=6; IntAct=EBI-2682299, EBI-11047108;
CC Q96NC0; P49810: PSEN2; NbExp=3; IntAct=EBI-2682299, EBI-2010251;
CC Q96NC0; P37840: SNCA; NbExp=3; IntAct=EBI-2682299, EBI-985879;
CC Q96NC0; P00441: SOD1; NbExp=3; IntAct=EBI-2682299, EBI-990792;
CC Q96NC0; Q96R06: SPAG5; NbExp=3; IntAct=EBI-2682299, EBI-413317;
CC Q96NC0; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-2682299, EBI-2212028;
CC Q96NC0; Q9UBB9: TFIP11; NbExp=4; IntAct=EBI-2682299, EBI-1105213;
CC Q96NC0; Q15025: TNIP1; NbExp=3; IntAct=EBI-2682299, EBI-357849;
CC Q96NC0; Q12933: TRAF2; NbExp=6; IntAct=EBI-2682299, EBI-355744;
CC Q96NC0; Q9NQ86: TRIM36; NbExp=3; IntAct=EBI-2682299, EBI-2341518;
CC Q96NC0; O94972: TRIM37; NbExp=3; IntAct=EBI-2682299, EBI-741602;
CC Q96NC0; Q8WW01: TSEN15; NbExp=5; IntAct=EBI-2682299, EBI-372432;
CC Q96NC0; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-2682299, EBI-2799833;
CC Q96NC0; O43829: ZBTB14; NbExp=3; IntAct=EBI-2682299, EBI-10176632;
CC Q96NC0; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-2682299, EBI-742740;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28781166}.
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DR EMBL; AK055683; BAB70983.1; -; mRNA.
DR EMBL; BC056668; AAH56668.1; -; mRNA.
DR CCDS; CCDS4239.1; -.
DR RefSeq; NP_653324.1; NM_144723.2.
DR PDB; 5O9Z; EM; 4.50 A; N=1-199.
DR PDB; 6AHD; EM; 3.80 A; 8=1-199.
DR PDB; 7AAV; EM; 4.20 A; N=1-199.
DR PDB; 7ABF; EM; 3.90 A; N=1-199.
DR PDB; 7ABG; EM; 7.80 A; N=1-199.
DR PDB; 7ABI; EM; 8.00 A; N=1-199.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 7AAV; -.
DR PDBsum; 7ABF; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABI; -.
DR AlphaFoldDB; Q96NC0; -.
DR SMR; Q96NC0; -.
DR BioGRID; 127499; 113.
DR IntAct; Q96NC0; 63.
DR MINT; Q96NC0; -.
DR STRING; 9606.ENSP00000274712; -.
DR iPTMnet; Q96NC0; -.
DR PhosphoSitePlus; Q96NC0; -.
DR BioMuta; ZMAT2; -.
DR DMDM; 52783532; -.
DR EPD; Q96NC0; -.
DR jPOST; Q96NC0; -.
DR MassIVE; Q96NC0; -.
DR MaxQB; Q96NC0; -.
DR PaxDb; Q96NC0; -.
DR PeptideAtlas; Q96NC0; -.
DR PRIDE; Q96NC0; -.
DR ProteomicsDB; 77501; -.
DR TopDownProteomics; Q96NC0; -.
DR Antibodypedia; 27104; 170 antibodies from 24 providers.
DR DNASU; 153527; -.
DR Ensembl; ENST00000274712.8; ENSP00000274712.2; ENSG00000146007.11.
DR GeneID; 153527; -.
DR KEGG; hsa:153527; -.
DR MANE-Select; ENST00000274712.8; ENSP00000274712.2; NM_144723.3; NP_653324.1.
DR UCSC; uc003lgy.2; human.
DR CTD; 153527; -.
DR DisGeNET; 153527; -.
DR GeneCards; ZMAT2; -.
DR HGNC; HGNC:26433; ZMAT2.
DR HPA; ENSG00000146007; Low tissue specificity.
DR neXtProt; NX_Q96NC0; -.
DR OpenTargets; ENSG00000146007; -.
DR PharmGKB; PA134931664; -.
DR VEuPathDB; HostDB:ENSG00000146007; -.
DR eggNOG; KOG4727; Eukaryota.
DR GeneTree; ENSGT00390000010712; -.
DR HOGENOM; CLU_067237_1_1_1; -.
DR InParanoid; Q96NC0; -.
DR OMA; FKDNLQW; -.
DR OrthoDB; 1626636at2759; -.
DR PhylomeDB; Q96NC0; -.
DR TreeFam; TF314475; -.
DR PathwayCommons; Q96NC0; -.
DR SignaLink; Q96NC0; -.
DR BioGRID-ORCS; 153527; 565 hits in 1087 CRISPR screens.
DR ChiTaRS; ZMAT2; human.
DR GenomeRNAi; 153527; -.
DR Pharos; Q96NC0; Tbio.
DR PRO; PR:Q96NC0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96NC0; protein.
DR Bgee; ENSG00000146007; Expressed in cortical plate and 181 other tissues.
DR ExpressionAtlas; Q96NC0; baseline and differential.
DR Genevisible; Q96NC0; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA: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; IDA: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 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA-binding; Isopeptide bond; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Spliceosome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..199
FT /note="Zinc finger matrin-type protein 2"
FT /id="PRO_0000047327"
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:0007744|PubMed:22814378"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 45
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 55
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
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
