SYCP2_HUMAN
ID SYCP2_HUMAN Reviewed; 1530 AA.
AC Q9BX26; A2RUE5; O75763; Q5JX11; Q9NTX8; Q9UG27;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Synaptonemal complex protein 2;
DE Short=SCP-2;
DE AltName: Full=Synaptonemal complex lateral element protein;
DE Short=hsSCP2;
GN Name=SYCP2; Synonyms=SCP2;
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 [MRNA].
RC TISSUE=Testis;
RX PubMed=10341103; DOI=10.1007/s003359901062;
RA Schalk J.A., Offenberg H.H., Peters E., Groot N.P., Hoovers J.M.N.,
RA Heyting C.;
RT "Isolation and characterization of the human SCP2 cDNA and chromosomal
RT localization of the gene.";
RL Mamm. Genome 10:642-644(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-797.
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 [5]
RP INVOLVEMENT IN SPGF1.
RX PubMed=31866047; DOI=10.1016/j.ajhg.2019.11.013;
RA Schilit S.L.P., Menon S., Friedrich C., Kammin T., Wilch E., Hanscom C.,
RA Jiang S., Kliesch S., Talkowski M.E., Tuettelmann F., MacQueen A.J.,
RA Morton C.C.;
RT "SYCP2 translocation-mediated dysregulation and frameshift variants cause
RT human male infertility.";
RL Am. J. Hum. Genet. 106:41-57(2020).
CC -!- FUNCTION: Major component of the axial/lateral elements of synaptonemal
CC complexes (SCS) during meiotic prophase. Plays a role in the assembly
CC of synaptonemal complexes. Required for normal meiotic chromosome
CC synapsis during oocyte and spermatocyte development and for normal male
CC and female fertility. Required for insertion of SYCP3 into synaptonemal
CC complexes. May be involved in the organization of chromatin by
CC temporarily binding to DNA scaffold attachment regions. Requires SYCP3,
CC but not SYCP1, in order to be incorporated into the axial/lateral
CC elements. {ECO:0000250|UniProtKB:Q9CUU3}.
CC -!- SUBUNIT: Component of the lateral elements of synaptonemal complexes.
CC Heterodimer with SYCP3 (By similarity). Interacts with SMC1A and SMC3
CC (By similarity). Interacts with TEX11 (By similarity).
CC {ECO:0000250|UniProtKB:O70608, ECO:0000250|UniProtKB:Q9CUU3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9CUU3}.
CC Chromosome {ECO:0000250|UniProtKB:Q9CUU3}. Note=In axial/lateral
CC elements of the tripartite segments of synaptonemal complexes.
CC {ECO:0000250|UniProtKB:Q9CUU3}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9CUU3}.
CC -!- DISEASE: Spermatogenic failure 1 (SPGF1) [MIM:258150]: An infertility
CC disorder characterized by azoospermia due to spermatogenic arrest
CC during meiosis. Meiotic arrest is characterized by germ cells that
CC enter meiosis and undergo the first chromosomal reduction from 4n to
CC 2n, but that are then unable to proceed further. This results in
CC tubules containing spermatocytes as the latest developmental stage of
CC germ cells. Meiotically arrested spermatocytes accumulate in the
CC tubules and degenerate. Both autosomal recessive and autosomal dominant
CC inheritance have been reported. {ECO:0000269|PubMed:31866047}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the SYCP2 family. {ECO:0000305}.
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DR EMBL; Y08982; CAA70171.1; -; mRNA.
DR EMBL; AL109928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132864; AAI32865.1; -; mRNA.
DR EMBL; BC132870; AAI32871.1; -; mRNA.
DR EMBL; AL080226; CAB45780.1; -; mRNA.
DR CCDS; CCDS13482.1; -.
DR RefSeq; NP_055073.2; NM_014258.3.
DR RefSeq; XP_011526791.1; XM_011528489.2.
DR AlphaFoldDB; Q9BX26; -.
DR SMR; Q9BX26; -.
DR BioGRID; 115660; 3.
DR IntAct; Q9BX26; 2.
DR MINT; Q9BX26; -.
DR STRING; 9606.ENSP00000350162; -.
DR CarbonylDB; Q9BX26; -.
DR iPTMnet; Q9BX26; -.
DR PhosphoSitePlus; Q9BX26; -.
DR BioMuta; SYCP2; -.
DR DMDM; 23822155; -.
DR EPD; Q9BX26; -.
DR jPOST; Q9BX26; -.
DR MassIVE; Q9BX26; -.
DR PaxDb; Q9BX26; -.
DR PeptideAtlas; Q9BX26; -.
DR PRIDE; Q9BX26; -.
DR ProteomicsDB; 79343; -.
DR Antibodypedia; 58383; 94 antibodies from 18 providers.
DR DNASU; 10388; -.
DR Ensembl; ENST00000357552.8; ENSP00000350162.2; ENSG00000196074.13.
DR Ensembl; ENST00000371001.6; ENSP00000360040.2; ENSG00000196074.13.
DR GeneID; 10388; -.
DR KEGG; hsa:10388; -.
DR MANE-Select; ENST00000357552.8; ENSP00000350162.2; NM_014258.4; NP_055073.2.
DR UCSC; uc002yaz.4; human.
DR CTD; 10388; -.
DR DisGeNET; 10388; -.
DR GeneCards; SYCP2; -.
DR HGNC; HGNC:11490; SYCP2.
DR HPA; ENSG00000196074; Tissue enhanced (testis).
DR MalaCards; SYCP2; -.
DR MIM; 258150; phenotype.
DR MIM; 604105; gene.
DR neXtProt; NX_Q9BX26; -.
DR OpenTargets; ENSG00000196074; -.
DR PharmGKB; PA36272; -.
DR VEuPathDB; HostDB:ENSG00000196074; -.
DR eggNOG; ENOG502QVM5; Eukaryota.
DR GeneTree; ENSGT00530000063859; -.
DR InParanoid; Q9BX26; -.
DR OMA; MAHERNV; -.
DR OrthoDB; 285929at2759; -.
DR PhylomeDB; Q9BX26; -.
DR TreeFam; TF332368; -.
DR PathwayCommons; Q9BX26; -.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR SignaLink; Q9BX26; -.
DR SIGNOR; Q9BX26; -.
DR BioGRID-ORCS; 10388; 8 hits in 1066 CRISPR screens.
DR ChiTaRS; SYCP2; human.
DR GenomeRNAi; 10388; -.
DR Pharos; Q9BX26; Tbio.
DR PRO; PR:Q9BX26; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9BX26; protein.
DR Bgee; ENSG00000196074; Expressed in right testis and 116 other tissues.
DR ExpressionAtlas; Q9BX26; baseline and differential.
DR Genevisible; Q9BX26; HS.
DR GO; GO:0000800; C:lateral element; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0000795; C:synaptonemal complex; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0007143; P:female meiotic nuclear division; IBA:GO_Central.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0048808; P:male genitalia morphogenesis; IEA:Ensembl.
DR GO; GO:0007140; P:male meiotic nuclear division; IBA:GO_Central.
DR GO; GO:0140013; P:meiotic nuclear division; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0051093; P:negative regulation of developmental process; IEA:Ensembl.
DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0007130; P:synaptonemal complex assembly; NAS:UniProtKB.
DR InterPro; IPR024832; SYCP2.
DR InterPro; IPR024835; SYCP2-like.
DR InterPro; IPR041322; SYCP2_ARLD.
DR InterPro; IPR040560; SYCP2_SLD.
DR PANTHER; PTHR15607; PTHR15607; 1.
DR PANTHER; PTHR15607:SF12; PTHR15607:SF12; 1.
DR Pfam; PF18581; SYCP2_ARLD; 1.
DR Pfam; PF18584; SYCP2_SLD; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Chromosome; DNA-binding; Meiosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1530
FT /note="Synaptonemal complex protein 2"
FT /id="PRO_0000072366"
FT REGION 439..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 619
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70608"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 938
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1189
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70608"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70608"
FT MOD_RES 1295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT MOD_RES 1339
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CUU3"
FT VARIANT 353
FT /note="T -> K (in dbSNP:rs13039338)"
FT /id="VAR_054059"
FT VARIANT 523
FT /note="P -> L (in dbSNP:rs1359836)"
FT /id="VAR_014115"
FT VARIANT 751
FT /note="T -> I (in dbSNP:rs6071006)"
FT /id="VAR_054060"
FT VARIANT 1155
FT /note="V -> A (in dbSNP:rs6128714)"
FT /id="VAR_054061"
FT CONFLICT 218
FT /note="G -> A (in Ref. 1; CAA70171)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="K -> R (in Ref. 1; CAA70171)"
FT /evidence="ECO:0000305"
FT CONFLICT 794..797
FT /note="GKEF -> KKKK (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 1179
FT /note="I -> T (in Ref. 1; CAA70171)"
FT /evidence="ECO:0000305"
FT CONFLICT 1186
FT /note="P -> A (in Ref. 1; CAA70171)"
FT /evidence="ECO:0000305"
FT CONFLICT 1222
FT /note="S -> R (in Ref. 1; CAA70171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1530 AA; 175639 MW; 3676EB133C53F1FA CRC64;
MPIRPDLQQL EKCIDDALRK NDFKPLKTLL QIDICEDVKI KCSKQFFHKV DNLICRELNK
EDIHNVSAIL VSVGRCGKNI SVLGQAGLLT MIKQGLIQKM VAWFEKSKDI IQSQGNSKDE
AVLNMIEDLV DLLLVIHDVS DEGKKQVVES FVPRICSLVI DSRVNICIQQ EIIKKMNAML
DKMPQDARKI LSNQEMLILM SSMGERILDA GDYDLQVGIV EALCRMTTEK QRQELAHQWF
SMDFIAKAFK RIKDSEFETD CRIFLNLVNG MLGDKRRVFT FPCLSAFLDK YELQIPSDEK
LEEFWIDFNL GSQTLSFYIA GDNDDHQWEA VTVPEEKVQI YSIEVRESKK LLTIILKNTV
KISKREGKEL LLYFDASLEI TNVTQKIFGA TKHRESIRKQ GISVAKTSLH ILFDASGSQI
LVPESQISPV GEELVSLKEK SKSPKEFAKP SKYIKNSDKG NRNNSQLEKT TPSKRKMSEA
SMIVSGADRY TMRSPVLFSN TSIPPRRRRI KPPLQMTSSA EKPSVSQTSE NRVDNAASLK
SRSSEGRHRR DNIDKHIKTA KCVENTENKN VEFPNQNFSE LQDVIPDSQA AEKRDHTILP
GVLDNICGNK IHSKWACWTP VTNIELCNNQ RASTSSGDTL NQDIVINKKL TKQKSSSSIS
DHNSEGTGKV KYKKEQTDHI KIDKAEVEVC KKHNQQQNHP KYSGQKNTEN AKQSDWPVES
ETTFKSVLLN KTIEESLIYR KKYILSKDVN TATCDKNPSA SKNVQSHRKA EKELTSELNS
WDSKQKKMRE KSKGKEFTNV AESLISQINK RYKTKDDIKS TRKLKESLIN SGFSNKPVVQ
LSKEKVQKKS YRKLKTTFVN VTSECPVNDV YNFNLNGADD PIIKLGIQEF QATAKEACAD
RSIRLVGPRN HDELKSSVKT KDKKIITNHQ KKNLFSDTET EYRCDDSKTD ISWLREPKSK
PQLIDYSRNK NVKNHKSGKS RSSLEKGQPS SKMTPSKNIT KKMDKTIPEG RIRLPRKATK
TKKNYKDLSN SESECEQEFS HSFKENIPVK EENIHSRMKT VKLPKKQQKV FCAETEKELS
KQWKNSSLLK DAIRDNCLDL SPRSLSGSPS SIEVTRCIEK ITEKDFTQDY DCITKSISPY
PKTSSLESLN SNSGVGGTIK SPKNNEKNFL CASESCSPIP RPLFLPRHTP TKSNTIVNRK
KISSLVLTQE TQNSNSYSDV SSYSSEERFM EIESPHINEN YIQSKREESH LASSLSKSSE
GREKTWFDMP CDATHVSGPT QHLSRKRIYI EDNLSNSNEV EMEEKGERRA NLLPKKLCKI
EDADHHIHKM SESVSSLSTN DFSIPWETWQ NEFAGIEMTY ETYERLNSEF KRRNNIRHKM
LSYFTTQSWK TAQQHLRTMN HQSQDSRIKK LDKFQFIIIE ELENFEKDSQ SLKDLEKEFV
DFWEKIFQKF SAYQKSEQQR LHLLKTSLAK SVFCNTDSEE TVFTSEMCLM KEDMKVLQDR
LLKDMLEEEL LNVRRELMSV FMSHERNANV
