SYCP2_HUMAN - dbPTM
SYCP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYCP2_HUMAN
UniProt AC Q9BX26
Protein Name Synaptonemal complex protein 2
Gene Name SYCP2
Organism Homo sapiens (Human).
Sequence Length 1530
Subcellular Localization Nucleus . Chromosome . In axial/lateral elements of the tripartite segments of synaptonemal complexes.
Protein Description Major component of the axial/lateral elements of synaptonemal complexes (SCS) during meiotic prophase. Plays a role in the assembly of synaptonemal complexes. Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility. Required for insertion of SYCP3 into synaptonemal complexes. May be involved in the organization of chromatin by temporarily binding to DNA scaffold attachment regions. Requires SYCP3, but not SYCP1, in order to be incorporated into the axial/lateral elements..
Protein Sequence MPIRPDLQQLEKCIDDALRKNDFKPLKTLLQIDICEDVKIKCSKQFFHKVDNLICRELNKEDIHNVSAILVSVGRCGKNISVLGQAGLLTMIKQGLIQKMVAWFEKSKDIIQSQGNSKDEAVLNMIEDLVDLLLVIHDVSDEGKKQVVESFVPRICSLVIDSRVNICIQQEIIKKMNAMLDKMPQDARKILSNQEMLILMSSMGERILDAGDYDLQVGIVEALCRMTTEKQRQELAHQWFSMDFIAKAFKRIKDSEFETDCRIFLNLVNGMLGDKRRVFTFPCLSAFLDKYELQIPSDEKLEEFWIDFNLGSQTLSFYIAGDNDDHQWEAVTVPEEKVQIYSIEVRESKKLLTIILKNTVKISKREGKELLLYFDASLEITNVTQKIFGATKHRESIRKQGISVAKTSLHILFDASGSQILVPESQISPVGEELVSLKEKSKSPKEFAKPSKYIKNSDKGNRNNSQLEKTTPSKRKMSEASMIVSGADRYTMRSPVLFSNTSIPPRRRRIKPPLQMTSSAEKPSVSQTSENRVDNAASLKSRSSEGRHRRDNIDKHIKTAKCVENTENKNVEFPNQNFSELQDVIPDSQAAEKRDHTILPGVLDNICGNKIHSKWACWTPVTNIELCNNQRASTSSGDTLNQDIVINKKLTKQKSSSSISDHNSEGTGKVKYKKEQTDHIKIDKAEVEVCKKHNQQQNHPKYSGQKNTENAKQSDWPVESETTFKSVLLNKTIEESLIYRKKYILSKDVNTATCDKNPSASKNVQSHRKAEKELTSELNSWDSKQKKMREKSKGKEFTNVAESLISQINKRYKTKDDIKSTRKLKESLINSGFSNKPVVQLSKEKVQKKSYRKLKTTFVNVTSECPVNDVYNFNLNGADDPIIKLGIQEFQATAKEACADRSIRLVGPRNHDELKSSVKTKDKKIITNHQKKNLFSDTETEYRCDDSKTDISWLREPKSKPQLIDYSRNKNVKNHKSGKSRSSLEKGQPSSKMTPSKNITKKMDKTIPEGRIRLPRKATKTKKNYKDLSNSESECEQEFSHSFKENIPVKEENIHSRMKTVKLPKKQQKVFCAETEKELSKQWKNSSLLKDAIRDNCLDLSPRSLSGSPSSIEVTRCIEKITEKDFTQDYDCITKSISPYPKTSSLESLNSNSGVGGTIKSPKNNEKNFLCASESCSPIPRPLFLPRHTPTKSNTIVNRKKISSLVLTQETQNSNSYSDVSSYSSEERFMEIESPHINENYIQSKREESHLASSLSKSSEGREKTWFDMPCDATHVSGPTQHLSRKRIYIEDNLSNSNEVEMEEKGERRANLLPKKLCKIEDADHHIHKMSESVSSLSTNDFSIPWETWQNEFAGIEMTYETYERLNSEFKRRNNIRHKMLSYFTTQSWKTAQQHLRTMNHQSQDSRIKKLDKFQFIIIEELENFEKDSQSLKDLEKEFVDFWEKIFQKFSAYQKSEQQRLHLLKTSLAKSVFCNTDSEETVFTSEMCLMKEDMKVLQDRLLKDMLEEELLNVRRELMSVFMSHERNANV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
201PhosphorylationQEMLILMSSMGERIL
HHHHHHHHHCCCHHH
17.4624043423
202PhosphorylationEMLILMSSMGERILD
HHHHHHHHCCCHHHC
19.4924043423
332PhosphorylationDHQWEAVTVPEEKVQ
CCCEEEEECCHHHEE
37.0722210691
342PhosphorylationEEKVQIYSIEVRESK
HHHEEEEEEEEECCH
17.5722210691
357AcetylationKLLTIILKNTVKISK
HHHEEHHHCCEEECH
39.9230592729
361AcetylationIILKNTVKISKREGK
EHHHCCEEECHHCCC
38.9430592735
436PhosphorylationPVGEELVSLKEKSKS
CCCHHHCHHHHHCCC
46.47-
457PhosphorylationPSKYIKNSDKGNRNN
CHHHCCCCCCCCCCC
35.38-
465PhosphorylationDKGNRNNSQLEKTTP
CCCCCCCHHHCCCCC
39.43-
470PhosphorylationNNSQLEKTTPSKRKM
CCHHHCCCCCCHHCC
34.2717322306
471PhosphorylationNSQLEKTTPSKRKMS
CHHHCCCCCCHHCCC
36.3122817900
478PhosphorylationTPSKRKMSEASMIVS
CCCHHCCCCHHEEEC
32.8020363803
481PhosphorylationKRKMSEASMIVSGAD
HHCCCCHHEEECCCC
12.65-
485PhosphorylationSEASMIVSGADRYTM
CCHHEEECCCCCCCC
19.83-
494PhosphorylationADRYTMRSPVLFSNT
CCCCCCCCCEECCCC
14.4526552605
499PhosphorylationMRSPVLFSNTSIPPR
CCCCEECCCCCCCCC
34.7326552605
501PhosphorylationSPVLFSNTSIPPRRR
CCEECCCCCCCCCCC
27.1726552605
502PhosphorylationPVLFSNTSIPPRRRR
CEECCCCCCCCCCCC
37.0326552605
519PhosphorylationPPLQMTSSAEKPSVS
CCCCCCCCCCCCCCC
31.14-
529PhosphorylationKPSVSQTSENRVDNA
CCCCCCCCCCCCCCH
25.82-
538PhosphorylationNRVDNAASLKSRSSE
CCCCCHHHHHCCCCC
33.64-
543PhosphorylationAASLKSRSSEGRHRR
HHHHHCCCCCCCCCH
39.57-
544PhosphorylationASLKSRSSEGRHRRD
HHHHCCCCCCCCCHH
42.85-
619PhosphorylationHSKWACWTPVTNIEL
CCCCCEECCCCCEEE
14.04-
660PhosphorylationQKSSSSISDHNSEGT
CCCCCCCCCCCCCCC
34.46-
664PhosphorylationSSISDHNSEGTGKVK
CCCCCCCCCCCCCCE
33.70-
681UbiquitinationKEQTDHIKIDKAEVE
CCCCCCCEECHHHHH
41.24-
743PhosphorylationSLIYRKKYILSKDVN
HHHHHHHEEECCCCC
15.3217081983
798PhosphorylationKSKGKEFTNVAESLI
HHCCHHHHHHHHHHH
29.8529978859
803PhosphorylationEFTNVAESLISQINK
HHHHHHHHHHHHHHH
22.6729978859
806PhosphorylationNVAESLISQINKRYK
HHHHHHHHHHHHHCC
30.2429978859
927PhosphorylationTKDKKIITNHQKKNL
CCCCEECCCCHHCCC
30.0729978859
936PhosphorylationHQKKNLFSDTETEYR
CHHCCCCCCCCCEEE
46.9529978859
938PhosphorylationKKNLFSDTETEYRCD
HCCCCCCCCCEEECC
43.5429978859
940PhosphorylationNLFSDTETEYRCDDS
CCCCCCCCEEECCCC
40.1729978859
942PhosphorylationFSDTETEYRCDDSKT
CCCCCCEEECCCCCC
24.7829978859
966PhosphorylationSKPQLIDYSRNKNVK
CCCCCCCCCCCCCCC
11.5323312004
967PhosphorylationKPQLIDYSRNKNVKN
CCCCCCCCCCCCCCC
26.1523312004
992AcetylationEKGQPSSKMTPSKNI
CCCCCCCCCCCCCCC
51.647977321
1019PhosphorylationIRLPRKATKTKKNYK
CCCCCCCCCCCCCHH
42.13-
1021PhosphorylationLPRKATKTKKNYKDL
CCCCCCCCCCCHHHC
42.78-
1040PhosphorylationSECEQEFSHSFKENI
HHHHHHHHHHHHHCC
19.92-
1042PhosphorylationCEQEFSHSFKENIPV
HHHHHHHHHHHCCCC
36.49-
1056PhosphorylationVKEENIHSRMKTVKL
CCCCHHHHCCCCCCC
30.21-
1060PhosphorylationNIHSRMKTVKLPKKQ
HHHHCCCCCCCCHHH
17.33-
1065AcetylationMKTVKLPKKQQKVFC
CCCCCCCHHHCCEEE
73.907851919
1066AcetylationKTVKLPKKQQKVFCA
CCCCCCHHHCCEEEH
56.907851927
1087PhosphorylationSKQWKNSSLLKDAIR
HHHHHCCHHHHHHHH
47.3024719451
1101PhosphorylationRDNCLDLSPRSLSGS
HHCCCCCCCCCCCCC
20.2424719451
1110PhosphorylationRSLSGSPSSIEVTRC
CCCCCCCCHHHHHHH
45.7224719451
1111PhosphorylationSLSGSPSSIEVTRCI
CCCCCCCHHHHHHHH
26.59-
1130PhosphorylationEKDFTQDYDCITKSI
CCCCCCCCCCCCCCC
11.6922817900
1136PhosphorylationDYDCITKSISPYPKT
CCCCCCCCCCCCCCC
21.4626307563
1138PhosphorylationDCITKSISPYPKTSS
CCCCCCCCCCCCCCC
26.0225056879
1140PhosphorylationITKSISPYPKTSSLE
CCCCCCCCCCCCCCH
15.5722817900
1145PhosphorylationSPYPKTSSLESLNSN
CCCCCCCCCHHCCCC
41.19-
1161PhosphorylationGVGGTIKSPKNNEKN
CCCCCCCCCCCCCCC
36.94-
1177PhosphorylationLCASESCSPIPRPLF
EEECCCCCCCCCCCC
34.8324719451
1189PhosphorylationPLFLPRHTPTKSNTI
CCCCCCCCCCCCCCE
33.65-
1204PhosphorylationVNRKKISSLVLTQET
ECHHHCCEEEEEECC
26.43-
1234PhosphorylationERFMEIESPHINENY
HHCCCCCCCCCCHHH
27.69-
1241PhosphorylationSPHINENYIQSKREE
CCCCCHHHHHCHHHH
8.31-
1249PhosphorylationIQSKREESHLASSLS
HHCHHHHHHHHHHCC
21.03-
1253PhosphorylationREESHLASSLSKSSE
HHHHHHHHHCCCCCC
37.87-
1254PhosphorylationEESHLASSLSKSSEG
HHHHHHHHCCCCCCC
30.93-
1256PhosphorylationSHLASSLSKSSEGRE
HHHHHHCCCCCCCCC
32.23-
1295PhosphorylationIYIEDNLSNSNEVEM
EEEECCCCCCCCCCC
44.46-
1297PhosphorylationIEDNLSNSNEVEMEE
EECCCCCCCCCCCHH
30.87-
1339PhosphorylationESVSSLSTNDFSIPW
HHHHHCCCCCCCCCH
44.06-
1368PhosphorylationETYERLNSEFKRRNN
HHHHHHHHHHHHHHC
49.3428270605
1523PhosphorylationELMSVFMSHERNANV
HHHHHHHHHHHCCCC
15.6720363803

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SYCP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYCP2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SYCP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SYCP2_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYCP2_HUMAN

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Related Literatures of Post-Translational Modification

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