CYTSA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CYTSA_MOUSE
• UniProt AC: Q2KN98
• Protein Name: Cytospin-A
• Gene Name: Specc1l
• Organism: Mus musculus (Mouse).
• Sequence Length: 1118
• Subcellular Localization: Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, spindle. Cell junction, gap junction. Colocalizes with beta-tubulin, acetylated alpha-tubulin and F-actin. Also observed in a ring around gamma-tubulin containing centrioles possibly in the microtubu
• 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 (By similarity)..
• Protein Sequence: MKKANRSAGSVPKVSGISKPQTVEKSKPENSSSAPTGVKPVRPGAAAALSKTKSNDDLLAGMAGGVNVTNGIKAKKSTCSSAAPSAPAPAMTISENKSKISTGTSSSAKRSTSAGNKESSSTRERLRERTRLNQSKKLPSVSQGANDVALAKRSRSRTAAEGDIRMSKSKSDNQISDKAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGISEDHCEGEDRSEVKETIIAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEKLFGYQSLSPEITPGNQSDGGGTLTSSVEGSAPGSVEDLLSQDENTLMDHQHSNSMDNLDSECSEVYQPLTSSDDALDAPSSSESEGVPSIERSRKGSSGNASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNAAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTSKPLTALSDKRSNYGELPVQEHLLRTSSTSRPASLPRVPAMESAKTISVSRRSSEEMKRDISASEGASPASLMAMGTTSPQLSLSSSPTASVTPSTRSRIREERKDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAESVGIKSTLDINEMARTERPDWQNVMLYVTAIYKYFET

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
52	Phosphorylation	AAAALSKTKSNDDLL HHHHHHCCCCCCCHH	36.01	27087446
54	Phosphorylation	AALSKTKSNDDLLAG HHHHCCCCCCCHHHH	51.20	27087446
62	Oxidation	NDDLLAGMAGGVNVT CCCHHHHHCCCEECC	2.32	17242355
69	Phosphorylation	MAGGVNVTNGIKAKK HCCCEECCCCCCCCC	23.64	21659605
92	Phosphorylation	SAPAPAMTISENKSK CCCCCCEEEECCCCC	24.37	28059163
94	Phosphorylation	PAPAMTISENKSKIS CCCCEEEECCCCCCC	26.42	28059163
107	Phosphorylation	ISTGTSSSAKRSTSA CCCCCCCCCCCCCCC	37.26	27841257
111	Phosphorylation	TSSSAKRSTSAGNKE CCCCCCCCCCCCCCC	26.46	-
140	Phosphorylation	NQSKKLPSVSQGAND HHHCCCCCCCCCHHH	44.85	29550500
142	Phosphorylation	SKKLPSVSQGANDVA HCCCCCCCCCHHHHH	27.51	25159016
156	Phosphorylation	ALAKRSRSRTAAEGD HHHHHHHCCCHHHCC	34.92	28066266
158	Phosphorylation	AKRSRSRTAAEGDIR HHHHHCCCHHHCCCC	31.31	28066266
169	Phosphorylation	GDIRMSKSKSDNQIS CCCCCCCCCCCCCCC	30.04	22817900
171	Phosphorylation	IRMSKSKSDNQISDK CCCCCCCCCCCCCHH	49.21	21454597
190	Phosphorylation	AKVKDLLTLAKTKDV HHHHHHHHHHHCCCC	31.78	-
278	Phosphorylation	RLNALGFSLEQRLDN HHHHHCCCHHHHCCC	29.24	25338131
381	Phosphorylation	GVPSIERSRKGSSGN CCCCCCCCCCCCCCC	26.08	26643407
385	Phosphorylation	IERSRKGSSGNASEV CCCCCCCCCCCHHHH	37.80	25521595
386	Phosphorylation	ERSRKGSSGNASEVS CCCCCCCCCCHHHHH	44.74	25521595
390	Phosphorylation	KGSSGNASEVSVACL CCCCCCHHHHHHHHH	42.40	26824392
393	Phosphorylation	SGNASEVSVACLTER CCCHHHHHHHHHHHH	10.43	23984901
398	Phosphorylation	EVSVACLTERIHQME HHHHHHHHHHHHHHH	24.09	25619855
489	Phosphorylation	EDVKSGRYMELEQRY CCHHHCCCCHHHHHH	9.85	28066266
496	Phosphorylation	YMELEQRYMDLAENA CCHHHHHHHHHHHHH	8.48	28066266
566	Phosphorylation	LAATLEEYKATVASD HHHHHHHHHHHHHHH	9.13	28066266
600	Phosphorylation	ELYSIHNSGDKSDIQ HHHHHHCCCCHHHHH	33.92	28066266
776	Acetylation	QEEIGDLKRRLHEAQ HHHHHHHHHHHHHHH	39.97	30988417
829	Phosphorylation	LRQGMGLSRRSSTSS HHHCCCCCCCCCCCC	21.66	29514104
832	Phosphorylation	GMGLSRRSSTSSEPT CCCCCCCCCCCCCCC	36.54	27742792
833	Phosphorylation	MGLSRRSSTSSEPTP CCCCCCCCCCCCCCC	30.42	25521595
834	Phosphorylation	GLSRRSSTSSEPTPT CCCCCCCCCCCCCCH	37.20	25521595
835	Phosphorylation	LSRRSSTSSEPTPTV CCCCCCCCCCCCCHH	34.35	27087446
836	Phosphorylation	SRRSSTSSEPTPTVK CCCCCCCCCCCCHHH	47.92	27087446
839	Phosphorylation	SSTSSEPTPTVKTLI CCCCCCCCCHHHHHH	27.78	28833060
841	Phosphorylation	TSSEPTPTVKTLIKS CCCCCCCHHHHHHHH	36.79	28833060
866	Phosphorylation	AAAAIPRTPLSPSPM HHHHCCCCCCCCCCC	24.19	26745281
869	Phosphorylation	AIPRTPLSPSPMKTP HCCCCCCCCCCCCCC	25.24	26824392
871	Phosphorylation	PRTPLSPSPMKTPPA CCCCCCCCCCCCCCC	33.96	26745281
875	Phosphorylation	LSPSPMKTPPAAAVS CCCCCCCCCCCCCCC	28.40	23527152
882	Phosphorylation	TPPAAAVSPMQRHSI CCCCCCCCCCCCCCC	15.21	23527152
888	Phosphorylation	VSPMQRHSISGPIST CCCCCCCCCCCCCCC	22.19	26824392
890	Phosphorylation	PMQRHSISGPISTSK CCCCCCCCCCCCCCC	41.34	25619855
894	Phosphorylation	HSISGPISTSKPLTA CCCCCCCCCCCCCHH	29.75	25619855
895	Phosphorylation	SISGPISTSKPLTAL CCCCCCCCCCCCHHH	41.30	25619855
896	Phosphorylation	ISGPISTSKPLTALS CCCCCCCCCCCHHHH	26.03	25619855
905	Ubiquitination	PLTALSDKRSNYGEL CCHHHHCCCCCCCCC	55.11	-
907	Phosphorylation	TALSDKRSNYGELPV HHHHCCCCCCCCCCH	39.89	28066266
909	Phosphorylation	LSDKRSNYGELPVQE HHCCCCCCCCCCHHH	17.14	28066266
921	Phosphorylation	VQEHLLRTSSTSRPA HHHHHHHCCCCCCCC	27.31	29176673
922	Phosphorylation	QEHLLRTSSTSRPAS HHHHHHCCCCCCCCC	25.78	29176673
923	Phosphorylation	EHLLRTSSTSRPASL HHHHHCCCCCCCCCC	29.77	24899341
924	Phosphorylation	HLLRTSSTSRPASLP HHHHCCCCCCCCCCC	28.64	29176673
925	Phosphorylation	LLRTSSTSRPASLPR HHHCCCCCCCCCCCC	37.91	29472430
929	Phosphorylation	SSTSRPASLPRVPAM CCCCCCCCCCCCCHH	41.40	29472430
940	Phosphorylation	VPAMESAKTISVSRR CCHHCCCCEEEECCC	56.52	24719451
943	Phosphorylation	MESAKTISVSRRSSE HCCCCEEEECCCCHH	21.19	22817900
945	Phosphorylation	SAKTISVSRRSSEEM CCCEEEECCCCHHHH	18.38	22817900
948	Phosphorylation	TISVSRRSSEEMKRD EEEECCCCHHHHHHH	40.78	23375375
949	Phosphorylation	ISVSRRSSEEMKRDI EEECCCCHHHHHHHH	35.45	26824392
957	Phosphorylation	EEMKRDISASEGASP HHHHHHHHHCCCCCH	29.99	23649490
959	Phosphorylation	MKRDISASEGASPAS HHHHHHHCCCCCHHH	29.76	26643407
963	Phosphorylation	ISASEGASPASLMAM HHHCCCCCHHHHHHC	31.68	23649490
966	Phosphorylation	SEGASPASLMAMGTT CCCCCHHHHHHCCCC	23.28	26643407
972	Phosphorylation	ASLMAMGTTSPQLSL HHHHHCCCCCCCCCC	15.83	26643407
973	Phosphorylation	SLMAMGTTSPQLSLS HHHHCCCCCCCCCCC	32.45	26643407
974	Phosphorylation	LMAMGTTSPQLSLSS HHHCCCCCCCCCCCC	15.53	26643407
978	Phosphorylation	GTTSPQLSLSSSPTA CCCCCCCCCCCCCCC	22.43	26643407
980	Phosphorylation	TSPQLSLSSSPTASV CCCCCCCCCCCCCCC	25.95	26643407
981	Phosphorylation	SPQLSLSSSPTASVT CCCCCCCCCCCCCCC	45.70	26643407
982	Phosphorylation	PQLSLSSSPTASVTP CCCCCCCCCCCCCCH	23.93	26643407
984	Phosphorylation	LSLSSSPTASVTPST CCCCCCCCCCCCHHH	33.25	26643407
986	Phosphorylation	LSSSPTASVTPSTRS CCCCCCCCCCHHHHH	29.06	26643407
988	Phosphorylation	SSPTASVTPSTRSRI CCCCCCCCHHHHHHH	14.71	26643407
990	Phosphorylation	PTASVTPSTRSRIRE CCCCCCHHHHHHHHH	27.38	25168779
991	Phosphorylation	TASVTPSTRSRIREE CCCCCHHHHHHHHHH	33.59	25168779

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of CYTSA_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, AND MASSSPECTROMETRY.
PubMed: 19367708

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND MASSSPECTROMETRY.
PubMed: 17242355