CYTSA_HUMAN - dbPTM
CYTSA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CYTSA_HUMAN
UniProt AC Q69YQ0
Protein Name Cytospin-A
Gene Name SPECC1L
Organism Homo sapiens (Human).
Sequence Length 1117
Subcellular Localization Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, spindle . Cell junction, gap junction . Colocalizes with acetylated alpha-tubulin, gamma-tubulin and F-actin. Also observed in a ring around gamma-tubulin containing centrioles possibly in the microt
Protein Description Involved in cytokinesis and spindle organization. May play a role in actin cytoskeleton organization and microtubule stabilization and hence required for proper cell adhesion and migration..
Protein Sequence MKKASRSVGSVPKVSAISKTQTAEKIKPENSSSASTGGKLVKPGTAASLSKTKSSDDLLAGMAGGVTVTNGVKGKKSTCPSAAPSASAPAMTTVENKSKISTGTASSTKRSTSTGNKESSSTRERLRERTRLNQSKKLPSAGQGANDMALAKRSRSRTATECDVRMSKSKSDNQISDRAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEKLFGYQSLSPEITPDNQSDGGGTLTSSVEGSAPGSVEDLLSQDENTLMDHQHSNSMDNLDSECSEVYQPLTSSDDALDAPSSSESEGIPSIERSRKGSSGNASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTSKPLTALSDKRPNYGEIPVQEHLLRTSSASRPASLPRVPAMESAKTLSVSRRSSEEVKRDISAQEGASPASLMAMGTTSPQLSLSSSPTASVTPTTRSRIREERKDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDINEMVRTERPDWQNVMLYVTAIYKYFET
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
5Phosphorylation---MKKASRSVGSVP
---CCCCCCCCCCCC
33.6922210691
7Phosphorylation-MKKASRSVGSVPKV
-CCCCCCCCCCCCCC
28.4722210691
10PhosphorylationKASRSVGSVPKVSAI
CCCCCCCCCCCCCEE
32.8422210691
20PhosphorylationKVSAISKTQTAEKIK
CCCEECCCCCCHHCC
25.10-
31PhosphorylationEKIKPENSSSASTGG
HHCCCCCCCCCCCCC
24.8128387310
33PhosphorylationIKPENSSSASTGGKL
CCCCCCCCCCCCCCC
26.5127251275
35PhosphorylationPENSSSASTGGKLVK
CCCCCCCCCCCCCCC
29.5428348404
36PhosphorylationENSSSASTGGKLVKP
CCCCCCCCCCCCCCC
50.0628387310
48PhosphorylationVKPGTAASLSKTKSS
CCCCCHHHHCCCCCC
30.6127251275
52PhosphorylationTAASLSKTKSSDDLL
CHHHHCCCCCCCCCH
32.5530266825
54PhosphorylationASLSKTKSSDDLLAG
HHHCCCCCCCCCHHH
44.2030266825
55PhosphorylationSLSKTKSSDDLLAGM
HHCCCCCCCCCHHHH
36.3830266825
67PhosphorylationAGMAGGVTVTNGVKG
HHHCCCEEEECCCCC
25.5323927012
69PhosphorylationMAGGVTVTNGVKGKK
HCCCEEEECCCCCCC
19.5223927012
78PhosphorylationGVKGKKSTCPSAAPS
CCCCCCCCCCCCCCC
37.0028555341
93PhosphorylationASAPAMTTVENKSKI
CCCCCEEEECCCCCC
16.85-
102PhosphorylationENKSKISTGTASSTK
CCCCCCCCCCCCCCC
41.8623403867
104PhosphorylationKSKISTGTASSTKRS
CCCCCCCCCCCCCCC
24.3723403867
106PhosphorylationKISTGTASSTKRSTS
CCCCCCCCCCCCCCC
38.0823403867
107PhosphorylationISTGTASSTKRSTST
CCCCCCCCCCCCCCC
35.1723403867
108PhosphorylationSTGTASSTKRSTSTG
CCCCCCCCCCCCCCC
28.1623403867
109AcetylationTGTASSTKRSTSTGN
CCCCCCCCCCCCCCC
46.4230592605
113PhosphorylationSSTKRSTSTGNKESS
CCCCCCCCCCCCCCH
35.25-
114PhosphorylationSTKRSTSTGNKESSS
CCCCCCCCCCCCCHH
44.88-
120PhosphorylationSTGNKESSSTRERLR
CCCCCCCHHHHHHHH
36.50-
122PhosphorylationGNKESSSTRERLRER
CCCCCHHHHHHHHHH
38.20-
140PhosphorylationNQSKKLPSAGQGAND
HHCCCCCCCCCCHHH
56.3128348404
156PhosphorylationALAKRSRSRTATECD
HHHHHHHCCCCCHHH
34.9227251275
158PhosphorylationAKRSRSRTATECDVR
HHHHHCCCCCHHHHH
38.9027251275
160PhosphorylationRSRSRTATECDVRMS
HHHCCCCCHHHHHCC
36.21-
169PhosphorylationCDVRMSKSKSDNQIS
HHHHCCCCCCCCCCC
30.0421406692
171PhosphorylationVRMSKSKSDNQISDR
HHCCCCCCCCCCCHH
49.2126657352
176PhosphorylationSKSDNQISDRAALEA
CCCCCCCCHHHHHHH
15.9828102081
195AcetylationLLTLAKTKDVEILHL
HHHHHHCCCCCHHHH
60.1026051181
220PhosphorylationLGINEDHSEGDEKSE
HCCCCCCCCCCHHHH
56.4429255136
226PhosphorylationHSEGDEKSEKETIMA
CCCCCHHHHHHHHHH
52.4329255136
277O-linked_GlycosylationRLNALGFSLEQRLDN
HHHHHCCCHHHHCCC
29.2430379171
277PhosphorylationRLNALGFSLEQRLDN
HHHHHCCCHHHHCCC
29.2428857561
295PhosphorylationLFGYQSLSPEITPDN
HCCEECCCCCCCCCC
26.2424275569
357PhosphorylationSEVYQPLTSSDDALD
HHHHCCCCCCCCCCC
32.6324275569
367PhosphorylationDDALDAPSSSESEGI
CCCCCCCCCCCCCCC
48.4924275569
371PhosphorylationDAPSSSESEGIPSIE
CCCCCCCCCCCCCCC
42.9724275569
380PhosphorylationGIPSIERSRKGSSGN
CCCCCCCCCCCCCCC
26.0823403867
382UbiquitinationPSIERSRKGSSGNAS
CCCCCCCCCCCCCHH
65.47-
384PhosphorylationIERSRKGSSGNASEV
CCCCCCCCCCCHHHH
37.8029255136
385PhosphorylationERSRKGSSGNASEVS
CCCCCCCCCCHHHHH
44.7423927012
389PhosphorylationKGSSGNASEVSVACL
CCCCCCHHHHHHHHH
42.4023927012
392PhosphorylationSGNASEVSVACLTER
CCCHHHHHHHHHHHH
10.4329209046
397PhosphorylationEVSVACLTERIHQME
HHHHHHHHHHHHHHH
24.0923927012
448PhosphorylationEKVILMESLCQQSDK
HHHHHHHHHHHCHHH
22.0827251275
576SulfoxidationVASDQIEMNRLKAQL
HHHHHHHHHHHHHHH
3.6521406390
594PhosphorylationKQKVAELYSIHNSGD
HHHHHHHHHHHCCCC
9.3325159151
599PhosphorylationELYSIHNSGDKSDIQ
HHHHHHCCCCHHHHH
33.9225159151
603PhosphorylationIHNSGDKSDIQDLLE
HHCCCCHHHHHHHHH
44.6926307563
6182-HydroxyisobutyrylationSVRLDKEKAETLASS
HHCCCHHHHHHHHHH
58.21-
618UbiquitinationSVRLDKEKAETLASS
HHCCCHHHHHHHHHH
58.21-
668PhosphorylationQIEDLNMTLEKLRSD
HHHHHHHHHHHHHHC
30.6021815630
687UbiquitinationETERSDMKETIFELE
HHHHHHHHHHHHHHH
57.61-
712PhosphorylationLHDNLIISDLENTVK
CCCCEEHHHHHHHHH
29.20-
743PhosphorylationHRRLREESAEWRQFQ
HHHHHHHHHHHHHHH
27.0827251275
775UbiquitinationQEEIGDLKRRLHEAQ
HHHHHHHHHHHHHHH
39.97-
808PhosphorylationEEERGRVYNYMNAVE
HHHHHHHHHHHHHHH
10.1422817900
810PhosphorylationERGRVYNYMNAVERD
HHHHHHHHHHHHHHH
3.6622817900
828PhosphorylationLRQGMGLSRRSSTSS
HHHCCCCCCCCCCCC
21.6624719451
831PhosphorylationGMGLSRRSSTSSEPT
CCCCCCCCCCCCCCC
36.5429255136
832PhosphorylationMGLSRRSSTSSEPTP
CCCCCCCCCCCCCCC
30.4229255136
833PhosphorylationGLSRRSSTSSEPTPT
CCCCCCCCCCCCCCH
37.2027273156
834PhosphorylationLSRRSSTSSEPTPTV
CCCCCCCCCCCCCHH
34.3529255136
835PhosphorylationSRRSSTSSEPTPTVK
CCCCCCCCCCCCHHH
47.9223927012
838PhosphorylationSSTSSEPTPTVKTLI
CCCCCCCCCHHHHHH
27.7823927012
840PhosphorylationTSSEPTPTVKTLIKS
CCCCCCCHHHHHHHH
36.7923927012
842UbiquitinationSEPTPTVKTLIKSFD
CCCCCHHHHHHHHCC
39.8421890473
842UbiquitinationSEPTPTVKTLIKSFD
CCCCCHHHHHHHHCC
39.8421890473
843PhosphorylationEPTPTVKTLIKSFDS
CCCCHHHHHHHHCCC
29.4029083192
846UbiquitinationPTVKTLIKSFDSASQ
CHHHHHHHHCCCHHC
48.4621890473
846UbiquitinationPTVKTLIKSFDSASQ
CHHHHHHHHCCCHHC
48.4621890473
847PhosphorylationTVKTLIKSFDSASQV
HHHHHHHHCCCHHCC
27.5629507054
850PhosphorylationTLIKSFDSASQVPNP
HHHHHCCCHHCCCCC
28.0122199227
852PhosphorylationIKSFDSASQVPNPAA
HHHCCCHHCCCCCHH
35.3527251275
865PhosphorylationAAAAIPRTPLSPSPM
HHHCCCCCCCCCCCC
24.1930266825
868PhosphorylationAIPRTPLSPSPMKTP
CCCCCCCCCCCCCCC
25.2430266825
870PhosphorylationPRTPLSPSPMKTPPA
CCCCCCCCCCCCCCC
33.9630266825
874PhosphorylationLSPSPMKTPPAAAVS
CCCCCCCCCCCCCCC
28.4023927012
881PhosphorylationTPPAAAVSPMQRHSI
CCCCCCCCCCCCCCC
15.2130266825
887PhosphorylationVSPMQRHSISGPIST
CCCCCCCCCCCCCCC
22.1923401153
889PhosphorylationPMQRHSISGPISTSK
CCCCCCCCCCCCCCC
41.3429255136
893PhosphorylationHSISGPISTSKPLTA
CCCCCCCCCCCCCHH
29.7525159151
894PhosphorylationSISGPISTSKPLTAL
CCCCCCCCCCCCHHH
41.3020068231
895PhosphorylationISGPISTSKPLTALS
CCCCCCCCCCCHHHC
26.0320068231
896UbiquitinationSGPISTSKPLTALSD
CCCCCCCCCCHHHCC
44.1021890473
896MalonylationSGPISTSKPLTALSD
CCCCCCCCCCHHHCC
44.1026320211
896UbiquitinationSGPISTSKPLTALSD
CCCCCCCCCCHHHCC
44.1021890473
902PhosphorylationSKPLTALSDKRPNYG
CCCCHHHCCCCCCCC
38.3322199227
904UbiquitinationPLTALSDKRPNYGEI
CCHHHCCCCCCCCCC
67.3921890473
904UbiquitinationPLTALSDKRPNYGEI
CCHHHCCCCCCCCCC
67.3921890473
908PhosphorylationLSDKRPNYGEIPVQE
HCCCCCCCCCCCHHH
20.8629978859
920PhosphorylationVQEHLLRTSSASRPA
HHHHHHHCCCCCCCC
27.3128555341
921PhosphorylationQEHLLRTSSASRPAS
HHHHHHCCCCCCCCC
19.9221712546
922PhosphorylationEHLLRTSSASRPASL
HHHHHCCCCCCCCCC
29.6525159151
924PhosphorylationLLRTSSASRPASLPR
HHHCCCCCCCCCCCC
40.5223312004
928PhosphorylationSSASRPASLPRVPAM
CCCCCCCCCCCCCHH
41.4025159151
937PhosphorylationPRVPAMESAKTLSVS
CCCCHHHCCCCCCCC
23.21-
939UbiquitinationVPAMESAKTLSVSRR
CCHHHCCCCCCCCCC
60.3121890473
939UbiquitinationVPAMESAKTLSVSRR
CCHHHCCCCCCCCCC
60.3121890473
942PhosphorylationMESAKTLSVSRRSSE
HHCCCCCCCCCCCHH
24.2328060719
944PhosphorylationSAKTLSVSRRSSEEV
CCCCCCCCCCCHHHH
20.7124719451
948PhosphorylationLSVSRRSSEEVKRDI
CCCCCCCHHHHHHHH
35.64-
956PhosphorylationEEVKRDISAQEGASP
HHHHHHHHHHCCCCH
28.3427251275
962PhosphorylationISAQEGASPASLMAM
HHHHCCCCHHHHHHC
31.6823090842
965PhosphorylationQEGASPASLMAMGTT
HCCCCHHHHHHCCCC
23.2823090842
971PhosphorylationASLMAMGTTSPQLSL
HHHHHCCCCCCCCCC
15.8330278072
972PhosphorylationSLMAMGTTSPQLSLS
HHHHCCCCCCCCCCC
32.4530278072
973PhosphorylationLMAMGTTSPQLSLSS
HHHCCCCCCCCCCCC
15.5320068231
977PhosphorylationGTTSPQLSLSSSPTA
CCCCCCCCCCCCCCC
22.4327050516
979PhosphorylationTSPQLSLSSSPTASV
CCCCCCCCCCCCCCC
25.9520068231
980PhosphorylationSPQLSLSSSPTASVT
CCCCCCCCCCCCCCC
45.7020068231
981PhosphorylationPQLSLSSSPTASVTP
CCCCCCCCCCCCCCC
23.9330576142
983PhosphorylationLSLSSSPTASVTPTT
CCCCCCCCCCCCCCC
33.2530278072
985PhosphorylationLSSSPTASVTPTTRS
CCCCCCCCCCCCCHH
29.0630278072
987PhosphorylationSSPTASVTPTTRSRI
CCCCCCCCCCCHHHH
16.6620068231
989PhosphorylationPTASVTPTTRSRIRE
CCCCCCCCCHHHHHH
26.0220068231
990PhosphorylationTASVTPTTRSRIREE
CCCCCCCCHHHHHHH
28.0520068231
992PhosphorylationSVTPTTRSRIREERK
CCCCCCHHHHHHHHC
29.9322210691
999UbiquitinationSRIREERKDPLSALA
HHHHHHHCCHHHHHH
67.96-
1003PhosphorylationEERKDPLSALAREYG
HHHCCHHHHHHHHHC
26.9921815630
1013AcetylationAREYGGSKRNALLKW
HHHHCCHHHHHHHHH
53.60-
1019AcetylationSKRNALLKWCQKKTE
HHHHHHHHHHHHHCC
46.93-
1081PhosphorylationLAFQAAESVGIKSTL
HHHHHHHHCCCCCCC
22.40-
1085AcetylationAAESVGIKSTLDINE
HHHHCCCCCCCCHHH
31.3119823681

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 CYTSA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CYTSA_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 CYTSA_HUMAN !!

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

Oops, there are no PPI records of CYTSA_HUMAN !!

Drug and Disease Associations
Kegg Disease
OMIM Disease
600251Facial clefting, oblique, 1 (OBLFC1)
145410Opitz GBBB syndrome 2 (GBBB2)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CYTSA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-868, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-881, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832; SER-868; THR-874AND SER-881, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-881, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASSSPECTROMETRY.

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