SZRD1_HUMAN
ID SZRD1_HUMAN Reviewed; 152 AA.
AC Q7Z422; A8MXJ2; C9K0U0; Q7Z424; Q8IVM2; Q8TBV3; Q9Y403;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=SUZ domain-containing protein 1;
DE AltName: Full=Putative MAPK-activating protein PM18/PM20/PM22;
GN Name=SZRD1; Synonyms=C1orf144;
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] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Skeletal muscle;
RA Ievolella C., Zara I., Millino C., Faulkner G., Lanfranchi G.;
RT "Full length sequencing of some human and murine muscular transcripts
RT (Telethon Italy project B41).";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Kidney, and Pancreas;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-39; SER-105 AND
RP SER-107, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-39 AND SER-51, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-107, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-39 AND SER-105, AND
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).
CC -!- INTERACTION:
CC Q7Z422-4; Q9Y3F4: STRAP; NbExp=3; IntAct=EBI-23877111, EBI-727414;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q7Z422-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z422-2; Sequence=VSP_027995;
CC Name=3;
CC IsoId=Q7Z422-3; Sequence=VSP_027997;
CC Name=4;
CC IsoId=Q7Z422-4; Sequence=VSP_027996;
CC Name=5;
CC IsoId=Q7Z422-5; Sequence=VSP_055690;
CC -!- SIMILARITY: Belongs to the SZRD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43245.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC82500.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB097042; BAC77395.1; -; mRNA.
DR EMBL; AB097044; BAC77397.1; -; mRNA.
DR EMBL; AB097046; BAC77399.1; -; mRNA.
DR EMBL; AJ295987; CAC82500.1; ALT_INIT; mRNA.
DR EMBL; AL050028; CAB43245.1; ALT_INIT; mRNA.
DR EMBL; AL358794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023988; AAH23988.1; -; mRNA.
DR EMBL; BC065538; AAH65538.1; -; mRNA.
DR CCDS; CCDS44065.1; -. [Q7Z422-1]
DR CCDS; CCDS60000.1; -. [Q7Z422-5]
DR PIR; T08712; T08712.
DR RefSeq; NP_001108072.1; NM_001114600.2. [Q7Z422-1]
DR RefSeq; NP_001258798.1; NM_001271869.1. [Q7Z422-5]
DR AlphaFoldDB; Q7Z422; -.
DR SMR; Q7Z422; -.
DR BioGRID; 117549; 17.
DR IntAct; Q7Z422; 6.
DR STRING; 9606.ENSP00000383866; -.
DR iPTMnet; Q7Z422; -.
DR PhosphoSitePlus; Q7Z422; -.
DR BioMuta; SZRD1; -.
DR EPD; Q7Z422; -.
DR jPOST; Q7Z422; -.
DR MassIVE; Q7Z422; -.
DR MaxQB; Q7Z422; -.
DR PaxDb; Q7Z422; -.
DR PeptideAtlas; Q7Z422; -.
DR PRIDE; Q7Z422; -.
DR ProteomicsDB; 12590; -.
DR ProteomicsDB; 69131; -. [Q7Z422-1]
DR ProteomicsDB; 69132; -. [Q7Z422-2]
DR ProteomicsDB; 69133; -. [Q7Z422-3]
DR ProteomicsDB; 69134; -. [Q7Z422-4]
DR TopDownProteomics; Q7Z422-1; -. [Q7Z422-1]
DR TopDownProteomics; Q7Z422-2; -. [Q7Z422-2]
DR TopDownProteomics; Q7Z422-3; -. [Q7Z422-3]
DR TopDownProteomics; Q7Z422-4; -. [Q7Z422-4]
DR Antibodypedia; 29172; 152 antibodies from 18 providers.
DR DNASU; 26099; -.
DR Ensembl; ENST00000401088.9; ENSP00000383866.4; ENSG00000055070.17. [Q7Z422-1]
DR Ensembl; ENST00000401089.3; ENSP00000383867.3; ENSG00000055070.17. [Q7Z422-4]
DR Ensembl; ENST00000471507.5; ENSP00000419589.1; ENSG00000055070.17. [Q7Z422-5]
DR Ensembl; ENST00000492354.1; ENSP00000418012.1; ENSG00000055070.17. [Q7Z422-2]
DR GeneID; 26099; -.
DR KEGG; hsa:26099; -.
DR MANE-Select; ENST00000401088.9; ENSP00000383866.4; NM_001114600.3; NP_001108072.1.
DR UCSC; uc001ayi.6; human. [Q7Z422-1]
DR CTD; 26099; -.
DR DisGeNET; 26099; -.
DR GeneCards; SZRD1; -.
DR HGNC; HGNC:30232; SZRD1.
DR HPA; ENSG00000055070; Low tissue specificity.
DR neXtProt; NX_Q7Z422; -.
DR OpenTargets; ENSG00000055070; -.
DR PharmGKB; PA142672461; -.
DR VEuPathDB; HostDB:ENSG00000055070; -.
DR eggNOG; ENOG502RZH5; Eukaryota.
DR GeneTree; ENSGT00390000005532; -.
DR HOGENOM; CLU_120658_0_0_1; -.
DR InParanoid; Q7Z422; -.
DR OMA; DNPGQDR; -.
DR OrthoDB; 1630870at2759; -.
DR PhylomeDB; Q7Z422; -.
DR TreeFam; TF324643; -.
DR PathwayCommons; Q7Z422; -.
DR SignaLink; Q7Z422; -.
DR BioGRID-ORCS; 26099; 22 hits in 1084 CRISPR screens.
DR ChiTaRS; SZRD1; human.
DR GenomeRNAi; 26099; -.
DR Pharos; Q7Z422; Tdark.
DR PRO; PR:Q7Z422; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z422; protein.
DR Bgee; ENSG00000055070; Expressed in mucosa of stomach and 202 other tissues.
DR ExpressionAtlas; Q7Z422; baseline and differential.
DR Genevisible; Q7Z422; HS.
DR InterPro; IPR024771; SUZ.
DR InterPro; IPR024642; SUZ-C.
DR InterPro; IPR039228; SZRD1.
DR PANTHER; PTHR31796; PTHR31796; 1.
DR Pfam; PF12752; SUZ; 1.
DR Pfam; PF12901; SUZ-C; 1.
DR PROSITE; PS51673; SUZ; 1.
DR PROSITE; PS51938; SUZ_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Phosphoprotein; Reference proteome.
FT CHAIN 1..152
FT /note="SUZ domain-containing protein 1"
FT /id="PRO_0000303068"
FT DOMAIN 42..107
FT /note="SUZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01009"
FT DOMAIN 111..152
FT /note="SUZ-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01287"
FT REGION 30..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..35
FT /note="MEDEEVAESWEEAADSGEIDRRLEKKLKITQKESR -> MRRSLRAGKRRQT
FT AG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12761501,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_027995"
FT VAR_SEQ 1..34
FT /note="MEDEEVAESWEEAADSGEIDRRLEKKLKITQKES -> MRRSLRAGKRRQTA
FT G (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12761501,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_027996"
FT VAR_SEQ 18..35
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_027997"
FT VAR_SEQ 34
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_055690"
SQ SEQUENCE 152 AA; 16997 MW; 07F735690D669778 CRC64;
MEDEEVAESW EEAADSGEID RRLEKKLKIT QKESRKSKSP PKVPIVIQDD SLPAGPPPQI
RILKRPTSNG VVSSPNSTSR PTLPVKSLAQ REAEYAEARK RILGSASPEE EQEKPILDRP
TRISQPEDSR QPNNVIRQPL GPDGSQGFKQ RR
