dbPTM

CND1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CND1_MOUSE
UniProt AC	Q8K2Z4
Protein Name	Condensin complex subunit 1
Gene Name	Ncapd2
Organism	Mus musculus (Mouse).
Sequence Length	1392
Subcellular Localization	Nucleus. Cytoplasm. Chromosome. In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromos
Protein Description	Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. May target the condensin complex to DNA via its C-terminal domain (By similarity)..
Protein Sequence	MSPHNFEFHLPLSPEELLKSGGVNQYVVREVLPVKHLSSQLRAFQSAFRAQGPLAILEHFDTVYSILHHFRSIEPGLKEDTLEFLKKVVSRHSQELSSILDDAALSGSDRSAHLNALKMNCYALIRLLESFENMTSQTSLIDLDIGGKGKRARAKATLGFDWEEERQPVLQLLTQLLQLDIRHLWNHSAIEEEFVSLVTGCCYRLLENPTISHQKNRSTKEAIAHLLGVALVRYNHMLSATVKIIQMLQHFEHLPPVLVTAVSLWATDYGMKSIVGEIVREIGQKCPQELSRDTAGAKGFAAFLTELAERIPAVLMANMCILLDHLDGENYMMRNAVLAAIAEMVLQVLNGDQLEESARETRDQFLDILQAHGHDVNSFVRSRVLQLFARIVQQKALPLTRFQAVVALAVGRLADKSVLVCKNAIQLLASFLANNPFSCKLSDIDLAGPLQKEIQKLQEMRAQRRSAAATAALDPEEEWDAMLPELKSTLQQLLKLPQEEGDHQIADAETAEEVKGRIRQLLAKASYKQAIVLTREATSHFQESEPFSHTEPEENSFLNLLGLIFKGPEASTQDSHGDTDPGLTGSKDSPSVPEPEGSQSNDELVKQEMLVQYLQDAYGFSQKITEAIGIISKMMYENTTTVVQEVIEFFVMVFQFGVPQALFGVRRMLPLIWSKEPGVREAVLNAYRQLYLNPKGDSARAKAQTLIHNLSLLLVDASVGTIQCLEEILCEFVQKDEVKPAVIQLLWERATEKVPSSPLERCSSVMLLGMMARGKPEIVGSNLDALVRVGLDEKSPQDYRLAQQVCLAIANISDRRKPSLGERHPPFRLPQEHRLFERLQDMVTKGFAHPDPLWIPFKEVAVTLTYQLAESPDVLCAQMLQGCAKQVLEKLEKNATEADPKETAPRLPTFLLMNLLSLAGDVALQQLVHLEQAVSGELGRRRVLREEQEHRAKEPKEKTASSETTMEEELGLVGGATADDTEAELIRSICEKELLDGNQVLAAFVPLLLKVCNNPGLYSNPELCAAASLALGKFCMISAPFCDSQLRLLFTMLEKSSLPTVRSNLMVATGDLAIRFPNLVDPWTPHLYARLRDPAQQVRKTAGLVMTHLILKDMVKVKGQVSEMAVLLIDPVPQIAALAKNFFNELSHKGNAIYNLLPDIISRLSDPEGGVEEEPFHTIMKQLLSYITKDKQTESLVEKLCQRFRTARTERQYRDLAYCMSQLPLTERGLQKMLDNFECFGDKLLDESVFSAFLSIVGKLRRGAKPEGKAIIDEFEQKLRACHTRGMDGIEEFETGQGGSQRALSAKKPSAVSRLQPLTSVDSDNDFVTPKPRRTKPGRPQTQQRKKSQRKAKVVFLSDESSEDELSAEMTEEETPKRTTPIRRASGRRHRS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSPHNFEFH ------CCCCCEEEC	46.28	25619855
13	Phosphorylation	FEFHLPLSPEELLKS EEECCCCCHHHHHHC	28.46	26745281
20	Phosphorylation	SPEELLKSGGVNQYV CHHHHHHCCCCCHHE	40.52	-
93	Phosphorylation	KKVVSRHSQELSSIL HHHHHHCHHHHHHHH	25.00	26370283
122	Phosphorylation	NALKMNCYALIRLLE HHHHHHHHHHHHHHH	10.23	25777480
130	Phosphorylation	ALIRLLESFENMTSQ HHHHHHHHHCCCCCC	37.52	25777480
135	Phosphorylation	LESFENMTSQTSLID HHHHCCCCCCCCEEE	29.30	25777480
136	Phosphorylation	ESFENMTSQTSLIDL HHHCCCCCCCCEEEE	22.23	25777480
138	Phosphorylation	FENMTSQTSLIDLDI HCCCCCCCCEEEEEC	25.85	25777480
139	Phosphorylation	ENMTSQTSLIDLDIG CCCCCCCCEEEEECC	18.72	25777480
273	Phosphorylation	ATDYGMKSIVGEIVR HHHHCHHHHHHHHHH	17.39	28059163
466	Phosphorylation	EMRAQRRSAAATAAL HHHHHHHHHHHHHHC	25.17	21149613
470	Phosphorylation	QRRSAAATAALDPEE HHHHHHHHHHCCHHH	14.03	26643407
572	Phosphorylation	FKGPEASTQDSHGDT HCCCCCCCCCCCCCC	43.36	25338131
575	Phosphorylation	PEASTQDSHGDTDPG CCCCCCCCCCCCCCC	21.39	25338131
584	Phosphorylation	GDTDPGLTGSKDSPS CCCCCCCCCCCCCCC	45.37	28507225
586	Phosphorylation	TDPGLTGSKDSPSVP CCCCCCCCCCCCCCC	28.23	25338131
589	Phosphorylation	GLTGSKDSPSVPEPE CCCCCCCCCCCCCCC	23.86	21183079
591	Phosphorylation	TGSKDSPSVPEPEGS CCCCCCCCCCCCCCC	55.01	22942356
598	Phosphorylation	SVPEPEGSQSNDELV CCCCCCCCCCHHHHH	28.86	26643407
600	Phosphorylation	PEPEGSQSNDELVKQ CCCCCCCCHHHHHHH	48.20	26643407
675	Ubiquitination	MLPLIWSKEPGVREA HHHHHHCCCCCHHHH	53.59	-
757	Phosphorylation	ATEKVPSSPLERCSS HHCCCCCCHHHHHCH	27.68	29514104
977	Phosphorylation	LGLVGGATADDTEAE HCCCCCCCCCHHHHH	33.62	25367039
981	Phosphorylation	GGATADDTEAELIRS CCCCCCHHHHHHHHH	37.33	25367039
1186	Phosphorylation	IMKQLLSYITKDKQT HHHHHHHHHCCCHHH	16.75	18779572
1278	Ubiquitination	IIDEFEQKLRACHTR HHHHHHHHHHHHHHC	32.51	-
1295	Phosphorylation	DGIEEFETGQGGSQR CCCCCCCCCCCCCHH	39.88	28066266
1300	Phosphorylation	FETGQGGSQRALSAK CCCCCCCCHHHHHCC	24.26	17525332
1305	Phosphorylation	GGSQRALSAKKPSAV CCCHHHHHCCCCCHH	36.74	25266776
1313	Phosphorylation	AKKPSAVSRLQPLTS CCCCCHHHHCCCCCC	27.30	26745281
1319	Phosphorylation	VSRLQPLTSVDSDND HHHCCCCCCCCCCCC	33.13	27087446
1320	Phosphorylation	SRLQPLTSVDSDNDF HHCCCCCCCCCCCCC	31.45	27087446
1323	Phosphorylation	QPLTSVDSDNDFVTP CCCCCCCCCCCCCCC	35.84	27087446
1329	Phosphorylation	DSDNDFVTPKPRRTK CCCCCCCCCCCCCCC	26.11	26824392
1358	Phosphorylation	KAKVVFLSDESSEDE HCEEEEECCCCCHHH	28.06	21082442
1361	Phosphorylation	VVFLSDESSEDELSA EEEECCCCCHHHHHH	43.98	21082442
1362	Phosphorylation	VFLSDESSEDELSAE EEECCCCCHHHHHHH	47.20	21082442
1367	Phosphorylation	ESSEDELSAEMTEEE CCCHHHHHHHCCCCC	21.82	21659605
1371	Phosphorylation	DELSAEMTEEETPKR HHHHHHCCCCCCCCC	31.58	25293948
1375	Phosphorylation	AEMTEEETPKRTTPI HHCCCCCCCCCCCCC	37.07	22345495
1379	Phosphorylation	EEETPKRTTPIRRAS CCCCCCCCCCCCCCC	42.95	25159016
1380	Phosphorylation	EETPKRTTPIRRASG CCCCCCCCCCCCCCC	22.28	21659605
1386	Phosphorylation	TTPIRRASGRRHRS- CCCCCCCCCCCCCC-	30.90	-

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
1375	T	Phosphorylation	Kinase	CDK1	P11440	Uniprot
1380	T	Phosphorylation	Kinase	CDK1	P11440	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CND1_MOUSE !!

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 CND1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CND1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of CND1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1320 AND SER-1323, ANDMASS SPECTROMETRY.	19131326 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1300, AND MASSSPECTROMETRY.	17525332 [Abstract]