SPAG7_HUMAN
ID SPAG7_HUMAN Reviewed; 227 AA.
AC O75391; Q96EU5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Sperm-associated antigen 7;
GN Name=SPAG7;
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].
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 TISSUE SPECIFICITY.
RX PubMed=7624517; DOI=10.1071/rd9940761;
RA Beaton S., Cleary A., ten Have J., Bradley M.P.;
RT "Cloning and characterization of a fox sperm protein FSA-1.";
RL Reprod. Fertil. Dev. 6:761-770(1994).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-158, AND
RP 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 [5]
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=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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND IDENTIFICATION BY
RP 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 [7]
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 [8]
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=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-158 AND SER-202, 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 [11]
RP STRUCTURE BY NMR OF 44-124.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the R3H domain of human sperm-associated antigen
RT 7.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- INTERACTION:
CC O75391; Q9BS40: LXN; NbExp=3; IntAct=EBI-348464, EBI-1044504;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in fetal brain.
CC {ECO:0000269|PubMed:7624517}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39888.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF047437; AAC39888.1; ALT_FRAME; mRNA.
DR EMBL; BC011934; AAH11934.1; -; mRNA.
DR CCDS; CCDS42240.1; -.
DR RefSeq; NP_004881.2; NM_004890.2.
DR PDB; 2CPM; NMR; -; A=44-124.
DR PDBsum; 2CPM; -.
DR AlphaFoldDB; O75391; -.
DR SMR; O75391; -.
DR BioGRID; 114924; 23.
DR IntAct; O75391; 8.
DR MINT; O75391; -.
DR STRING; 9606.ENSP00000206020; -.
DR GlyGen; O75391; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75391; -.
DR MetOSite; O75391; -.
DR PhosphoSitePlus; O75391; -.
DR BioMuta; SPAG7; -.
DR EPD; O75391; -.
DR jPOST; O75391; -.
DR MassIVE; O75391; -.
DR MaxQB; O75391; -.
DR PaxDb; O75391; -.
DR PeptideAtlas; O75391; -.
DR PRIDE; O75391; -.
DR ProteomicsDB; 49964; -.
DR Antibodypedia; 5775; 80 antibodies from 22 providers.
DR DNASU; 9552; -.
DR Ensembl; ENST00000206020.8; ENSP00000206020.3; ENSG00000091640.8.
DR GeneID; 9552; -.
DR KEGG; hsa:9552; -.
DR MANE-Select; ENST00000206020.8; ENSP00000206020.3; NM_004890.3; NP_004881.2.
DR UCSC; uc002gae.4; human.
DR CTD; 9552; -.
DR DisGeNET; 9552; -.
DR GeneCards; SPAG7; -.
DR HGNC; HGNC:11216; SPAG7.
DR HPA; ENSG00000091640; Tissue enhanced (skeletal).
DR MIM; 610056; gene.
DR neXtProt; NX_O75391; -.
DR OpenTargets; ENSG00000091640; -.
DR PharmGKB; PA36052; -.
DR VEuPathDB; HostDB:ENSG00000091640; -.
DR eggNOG; ENOG502QW1E; Eukaryota.
DR GeneTree; ENSGT00390000001520; -.
DR HOGENOM; CLU_091198_0_0_1; -.
DR InParanoid; O75391; -.
DR OMA; HRSVIHE; -.
DR OrthoDB; 1416114at2759; -.
DR PhylomeDB; O75391; -.
DR TreeFam; TF323631; -.
DR PathwayCommons; O75391; -.
DR SignaLink; O75391; -.
DR BioGRID-ORCS; 9552; 27 hits in 1090 CRISPR screens.
DR ChiTaRS; SPAG7; human.
DR EvolutionaryTrace; O75391; -.
DR GeneWiki; SPAG7; -.
DR GenomeRNAi; 9552; -.
DR Pharos; O75391; Tbio.
DR PRO; PR:O75391; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75391; protein.
DR Bgee; ENSG00000091640; Expressed in apex of heart and 210 other tissues.
DR ExpressionAtlas; O75391; baseline and differential.
DR Genevisible; O75391; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd02636; R3H_sperm-antigen; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034068; R3H_sperm-antigen.
DR InterPro; IPR017330; SPAG7.
DR PANTHER; PTHR13498; PTHR13498; 1.
DR Pfam; PF01424; R3H; 1.
DR PIRSF; PIRSF037943; Sperm-assoc_antigen_PAG7; 1.
DR SMART; SM00393; R3H; 1.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS51061; R3H; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..227
FT /note="Sperm-associated antigen 7"
FT /id="PRO_0000072097"
FT DOMAIN 46..109
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..51
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 122..139
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 18..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:2CPM"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2CPM"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:2CPM"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2CPM"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2CPM"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:2CPM"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:2CPM"
SQ SEQUENCE 227 AA; 26034 MW; 429566BE9B276EE4 CRC64;
MADLLGSILS SMEKPPSLGD QETRRKAREQ AARLKKLQEQ EKQQKVEFRK RMEKEVSDFI
QDSGQIKKKF QPMNKIERSI LHDVVEVAGL TSFSFGEDDD CRYVMIFKKE FAPSDEELDS
YRRGEEWDPQ KAEEKRKLKE LAQRQEEEAA QQGPVVVSPA SDYKDKYSHL IGKGAAKDAA
HMLQANKTYG CVPVANKRDT RSIEEAMNEI RAKKRLRQSG EELPPTS
