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   27-MAR-2024, entry version 166.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 29.
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; 9606-ENSP00000206020; -.
DR   PeptideAtlas; O75391; -.
DR   ProteomicsDB; 49964; -.
DR   Pumba; O75391; -.
DR   Antibodypedia; 5775; 98 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   AGR; HGNC:11216; -.
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; NGGFIAM; -.
DR   OrthoDB; 2912385at2759; -.
DR   PhylomeDB; O75391; -.
DR   TreeFam; TF323631; -.
DR   PathwayCommons; O75391; -.
DR   SignaLink; O75391; -.
DR   BioGRID-ORCS; 9552; 31 hits in 1175 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 212 other cell types or tissues.
DR   ExpressionAtlas; O75391; baseline and differential.
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; R3H-like domain; 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; SPERM ASSOCIATED ANTIGEN 7; 1.
DR   PANTHER; PTHR13498:SF3; SPERM-ASSOCIATED ANTIGEN 7; 1.
DR   Pfam; PF01424; R3H; 1.
DR   PIRSF; PIRSF037943; Sperm-assoc_antigen_PAG7; 1.
DR   SMART; SM00393; R3H; 1.
DR   SUPFAM; SSF82708; R3H domain; 1.
DR   PROSITE; PS51061; R3H; 1.
DR   Genevisible; O75391; HS.
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
//