CNDH2_HUMAN - dbPTM
CNDH2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNDH2_HUMAN
UniProt AC Q6IBW4
Protein Name Condensin-2 complex subunit H2
Gene Name NCAPH2
Organism Homo sapiens (Human).
Sequence Length 605
Subcellular Localization Nucleus . Chromosome . Distributed along the arms of chromosomes assembled in vivo and in vitro.
Protein Description Regulatory subunit of the condensin-2 complex, a complex that seems to provide chromosomes with an additional level of organization and rigidity and in establishing mitotic chromosome architecture. May play a role in lineage-specific role in T-cell development (By similarity)..
Protein Sequence MEDVEARFAHLLQPIRDLTKNWEVDVAAQLGEYLEELDQICISFDEGKTTMNFIEAALLIQGSACVYSKKVEYLYSLVYQALDFISGKRRAKQLSSVQEDRANGVASSGVPQEAENEFLSLDDFPDSRTNVDLKNDQTPSEVLIIPLLPMALVAPDEMEKNNNPLYSRQGEVLASRKDFRMNTCVPHPRGAFMLEPEGMSPMEPAGVSPMPGTQKDTGRTEEQPMEVSVCRSPVPALGFSQEPGPSPEGPMPLGGGEDEDAEEAVELPEASAPKAALEPKESRSPQQSAALPRRYMLREREGAPEPASCVKETPDPWQSLDPFDSLESKPFKKGRPYSVPPCVEEALGQKRKRKGAAKLQDFHQWYLAAYADHADSRRLRRKGPSFADMEVLYWTHVKEQLETLRKLQRREVAEQWLRPAEEDHLEDSLEDLGAADDFLEPEEYMEPEGADPREAADLDAVPMSLSYEELVRRNVELFIATSQKFVQETELSQRIRDWEDTVQPLLQEQEQHVPFDIHTYGDQLVSRFPQLNEWCPFAELVAGQPAFEVCRSMLASLQLANDYTVEITQQPGLEMAVDTMSLRLLTHQRAHKRFQTYAAPSMAQP
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
19PhosphorylationLQPIRDLTKNWEVDV
HHHHHHHCCCCCHHH		26.9920068231
50PhosphorylationSFDEGKTTMNFIEAA
ECCCCCCHHHHHHHH		17.38-
65UbiquitinationLLIQGSACVYSKKVE
HHHCCCCCHHHCCHH		2.9424816145
75PhosphorylationSKKVEYLYSLVYQAL
HCCHHHHHHHHHHHH		10.08-
79PhosphorylationEYLYSLVYQALDFIS
HHHHHHHHHHHHHHC		8.05-
92 (in isoform 5)Ubiquitination-50.3821906983
92 (in isoform 4)Ubiquitination-50.3821906983
92 (in isoform 2)Ubiquitination-50.3821906983
92 (in isoform 1)Ubiquitination-50.3821906983
92UbiquitinationISGKRRAKQLSSVQE
HCCCHHHHHHHCHHH		50.3821906983
95PhosphorylationKRRAKQLSSVQEDRA
CHHHHHHHCHHHHHH		26.4325159151
96PhosphorylationRRAKQLSSVQEDRAN
HHHHHHHCHHHHHHC		36.0919691289
107PhosphorylationDRANGVASSGVPQEA
HHHCCCCCCCCCHHH		25.8120068231
108PhosphorylationRANGVASSGVPQEAE
HHCCCCCCCCCHHHH		33.7920068231
120PhosphorylationEAENEFLSLDDFPDS
HHHHCCCCCCCCCCC		34.7620068231
127PhosphorylationSLDDFPDSRTNVDLK
CCCCCCCCCCCCCCC		41.0420068231
129PhosphorylationDDFPDSRTNVDLKND
CCCCCCCCCCCCCCC		43.4721712546
134SumoylationSRTNVDLKNDQTPSE
CCCCCCCCCCCCCCC		54.75-
138PhosphorylationVDLKNDQTPSEVLII
CCCCCCCCCCCEEEE		31.4829496963
140PhosphorylationLKNDQTPSEVLIIPL
CCCCCCCCCEEEEEC		43.6629496963
149UbiquitinationVLIIPLLPMALVAPD
EEEEECHHEEHHCCH		17.4322505724
152UbiquitinationIPLLPMALVAPDEME
EECHHEEHHCCHHHH		2.4822505724
153UbiquitinationPLLPMALVAPDEMEK
ECHHEEHHCCHHHHH		5.4322505724
167PhosphorylationKNNNPLYSRQGEVLA
HCCCCCCCHHCHHHH		26.3024719451
175PhosphorylationRQGEVLASRKDFRMN
HHCHHHHCCCCCCCC		35.3825159151
183PhosphorylationRKDFRMNTCVPHPRG
CCCCCCCCCCCCCCC		12.9224719451
200 (in isoform 4)Phosphorylation-31.7724719451
200PhosphorylationMLEPEGMSPMEPAGV
EECCCCCCCCCCCCC		31.7725159151
208PhosphorylationPMEPAGVSPMPGTQK
CCCCCCCCCCCCCCC		17.9823401153
208 (in isoform 4)Phosphorylation-17.9824719451
213PhosphorylationGVSPMPGTQKDTGRT
CCCCCCCCCCCCCCC		26.9522115753
220PhosphorylationTQKDTGRTEEQPMEV
CCCCCCCCCCCCEEE		45.2625627689
225SulfoxidationGRTEEQPMEVSVCRS
CCCCCCCEEEEEECC		8.7421406390
228PhosphorylationEEQPMEVSVCRSPVP
CCCCEEEEEECCCCC		11.3719691289
232PhosphorylationMEVSVCRSPVPALGF
EEEEEECCCCCCCCC		25.7320873877
240PhosphorylationPVPALGFSQEPGPSP
CCCCCCCCCCCCCCC		31.6620873877
246PhosphorylationFSQEPGPSPEGPMPL
CCCCCCCCCCCCCCC		41.3118669648
246 (in isoform 4)Phosphorylation-41.3127251275
271PhosphorylationAVELPEASAPKAALE
HHCCCCCCCCHHHCC		43.3626074081
282PhosphorylationAALEPKESRSPQQSA
HHCCCCCCCCHHHHH		44.1522167270
284 (in isoform 4)Phosphorylation-36.0224719451
284PhosphorylationLEPKESRSPQQSAAL
CCCCCCCCHHHHHHC		36.0229255136
284 (in isoform 5)Phosphorylation-36.0216565220
288PhosphorylationESRSPQQSAALPRRY
CCCCHHHHHHCCHHH		15.4022167270
295PhosphorylationSAALPRRYMLREREG
HHHCCHHHHHHHCCC		11.2026074081
302UbiquitinationYMLREREGAPEPASC
HHHHHCCCCCCCHHH		53.2922505724
305UbiquitinationREREGAPEPASCVKE
HHCCCCCCCHHHCCC		53.6222505724
306UbiquitinationEREGAPEPASCVKET
HCCCCCCCHHHCCCC		28.5422505724
308PhosphorylationEGAPEPASCVKETPD
CCCCCCHHHCCCCCC		30.1119691289
311UbiquitinationPEPASCVKETPDPWQ
CCCHHHCCCCCCCHH		61.2629967540
313PhosphorylationPASCVKETPDPWQSL
CHHHCCCCCCCHHCC		27.5523312004
319PhosphorylationETPDPWQSLDPFDSL
CCCCCHHCCCCCCCC		30.7626074081
325PhosphorylationQSLDPFDSLESKPFK
HCCCCCCCCCCCCCC		34.1220068231
328PhosphorylationDPFDSLESKPFKKGR
CCCCCCCCCCCCCCC		51.4220068231
329 (in isoform 4)Ubiquitination-45.13-
329UbiquitinationPFDSLESKPFKKGRP
CCCCCCCCCCCCCCC		45.1322505724
329SumoylationPFDSLESKPFKKGRP
CCCCCCCCCCCCCCC		45.13-
332UbiquitinationSLESKPFKKGRPYSV
CCCCCCCCCCCCCCC		63.9522505724
333 (in isoform 4)Ubiquitination-61.61-
333UbiquitinationLESKPFKKGRPYSVP
CCCCCCCCCCCCCCC		61.6122505724
337PhosphorylationPFKKGRPYSVPPCVE
CCCCCCCCCCCHHHH		22.4218083107
350UbiquitinationVEEALGQKRKRKGAA
HHHHHCCHHHHCCCH		59.0829967540
354AcetylationLGQKRKRKGAAKLQD
HCCHHHHCCCHHHHH		56.8125953088
358AcetylationRKRKGAAKLQDFHQW
HHHCCCHHHHHHHHH		46.2625953088
376PhosphorylationAYADHADSRRLRRKG
HHHCHHHHHHHHHHC		21.78-
382UbiquitinationDSRRLRRKGPSFADM
HHHHHHHHCCCHHHH		69.60-
382 (in isoform 4)Ubiquitination-69.60-
385PhosphorylationRLRRKGPSFADMEVL
HHHHHCCCHHHHHHH		41.56-
403PhosphorylationHVKEQLETLRKLQRR
HHHHHHHHHHHHHHH		40.2220860994
428PhosphorylationEEDHLEDSLEDLGAA
HHHHHHHHHHHHCCC		25.04-
464PhosphorylationDLDAVPMSLSYEELV
CCCCCCCCCCHHHHH		14.2221712546
465 (in isoform 4)Phosphorylation-5.2724719451
466PhosphorylationDAVPMSLSYEELVRR
CCCCCCCCHHHHHHH		24.1621712546
467PhosphorylationAVPMSLSYEELVRRN
CCCCCCCHHHHHHHC		20.7924732914
467 (in isoform 4)Phosphorylation-20.7927251275
481PhosphorylationNVELFIATSQKFVQE
CHHHHEECCHHHHHH		27.2020860994
482PhosphorylationVELFIATSQKFVQET
HHHHEECCHHHHHHH		23.5020068231
489PhosphorylationSQKFVQETELSQRIR
CHHHHHHHHHHHHHH		25.7419691289
492PhosphorylationFVQETELSQRIRDWE
HHHHHHHHHHHHHHH		15.9217525332
501PhosphorylationRIRDWEDTVQPLLQE
HHHHHHHHHHHHHHH		14.99-
552PhosphorylationPAFEVCRSMLASLQL
HHHHHHHHHHHHHHH		17.0224043423
556PhosphorylationVCRSMLASLQLANDY
HHHHHHHHHHHCCCE		16.8224043423
563PhosphorylationSLQLANDYTVEITQQ
HHHHCCCEEEEEECC		16.7024043423
564PhosphorylationLQLANDYTVEITQQP
HHHCCCEEEEEECCC		17.9624043423
568PhosphorylationNDYTVEITQQPGLEM
CCEEEEEECCCCCHH		13.9824719451
579PhosphorylationGLEMAVDTMSLRLLT
CCHHHHHHHHHHHHH		11.3224043423
581PhosphorylationEMAVDTMSLRLLTHQ
HHHHHHHHHHHHHHH		16.6624043423
597PhosphorylationAHKRFQTYAAPSMAQ
HHHHHHHCCCCCCCC		7.03-
601PhosphorylationFQTYAAPSMAQP---
HHHCCCCCCCCC---		23.2528555341
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
288SPhosphorylationKinasePLK1P53350
PSP
492SPhosphorylationKinaseTTKP33981
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNDH2_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 CNDH2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNDD3_HUMANNCAPD3physical
17268547
CNDG2_HUMANNCAPG2physical
17268547
SMC4_HUMANSMC4physical
17268547
SMC2_HUMANSMC2physical
17268547
CNDG2_HUMANNCAPG2physical
14532007
SMC4_HUMANSMC4physical
14532007
SMC2_HUMANSMC2physical
14532007
CNDD3_HUMANNCAPD3physical
14532007
USBP1_HUMANUSHBP1physical
25416956
EGLN3_HUMANEGLN3physical
25416956
CNDD3_HUMANNCAPD3physical
26344197
CNDG2_HUMANNCAPG2physical
26344197
RBM8A_HUMANRBM8Aphysical
26344197
SMRC1_HUMANSMARCC1physical
26344197
TRAF2_HUMANTRAF2physical
21516116
TTC25_HUMANTTC25physical
21516116
ESR1_HUMANESR1physical
26166704
SMC2_HUMANSMC2physical
26166704
SMC4_HUMANSMC4physical
26166704
CNDD3_HUMANNCAPD3physical
26166704
CNDG2_HUMANNCAPG2physical
26166704
CNDH2_HUMANNCAPH2physical
26166704
CND3_HUMANNCAPGphysical
26166704
HECD1_HUMANHECTD1physical
26166704
M18BP_HUMANMIS18BP1physical
28514442
SATB2_HUMANSATB2physical
28514442
TALD3_HUMANKIAA0586physical
28514442
SMC2_HUMANSMC2physical
28514442
ZN318_HUMANZNF318physical
28514442
FIGL1_HUMANFIGNL1physical
28514442
DUS3L_HUMANDUS3Lphysical
28514442
SMC4_HUMANSMC4physical
28514442
TROP_HUMANTROphysical
28514442
SNPC4_HUMANSNAPC4physical
28514442
CE164_HUMANCEP164physical
28514442
SAM11_HUMANSAMD11physical
28514442
CNDD3_HUMANNCAPD3physical
28514442
CN080_HUMANC14orf80physical
28514442
CNDG2_HUMANNCAPG2physical
28514442
BUB1_HUMANBUB1physical
28514442
ASPM_HUMANASPMphysical
28514442
F208B_HUMANFAM208Bphysical
28514442
JMJD4_HUMANJMJD4physical
28514442
TRI37_HUMANTRIM37physical
28514442
FANCJ_HUMANBRIP1physical
28514442
ALMS1_HUMANALMS1physical
28514442
BCOR_HUMANBCORphysical
28514442
RGPD5_HUMANRGPD5physical
28514442
SMG8_HUMANSMG8physical
28514442
CO039_HUMANC15orf39physical
28514442
GTSE1_HUMANGTSE1physical
28514442
MS18B_HUMANOIP5physical
28514442
HOOK1_HUMANHOOK1physical
28514442
TBL1R_HUMANTBL1XR1physical
28514442
BRCA2_HUMANBRCA2physical
28514442
BPTF_HUMANBPTFphysical
28514442
LRIF1_HUMANLRIF1physical
28514442
CTR9_HUMANCTR9physical
28514442
RICTR_HUMANRICTORphysical
28514442
IQCB1_HUMANIQCB1physical
28514442
PRI1_HUMANPRIM1physical
28514442
NCOR1_HUMANNCOR1physical
28514442
IQGA3_HUMANIQGAP3physical
28514442
MTO1_HUMANMTO1physical
28514442
CDC23_HUMANCDC23physical
28514442
HOOK3_HUMANHOOK3physical
28514442
OFD1_HUMANOFD1physical
28514442
ADNP_HUMANADNPphysical
28514442
SALL2_HUMANSALL2physical
28514442
MBIP1_HUMANMBIPphysical
28514442
MYO9A_HUMANMYO9Aphysical
28514442
FA83H_HUMANFAM83Hphysical
28514442
APC5_HUMANANAPC5physical
28514442
AL3A2_HUMANALDH3A2physical
28514442
P3C2A_HUMANPIK3C2Aphysical
28514442
K1671_HUMANKIAA1671physical
28514442
MS18A_HUMANMIS18Aphysical
28514442
CHD8_HUMANCHD8physical
28514442
ZN644_HUMANZNF644physical
28514442
RTEL1_HUMANRTEL1physical
28514442
ZZZ3_HUMANZZZ3physical
28514442
N42L2_HUMANN4BP2L2physical
28514442
GGYF2_HUMANGIGYF2physical
28514442
P66B_HUMANGATAD2Bphysical
28514442
KNL1_HUMANCASC5physical
28514442
EMSY_HUMANC11orf30physical
28514442
TIGD5_HUMANTIGD5physical
28514442
MED12_HUMANMED12physical
28514442
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 CNDH2_HUMAN

loading...

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-208, 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-284, 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-282; SER-284 ANDSER-492, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND SER-492, ANDMASS SPECTROMETRY.
"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-492, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-120; SER-200;SER-228; SER-284; SER-319; SER-466 AND SER-492, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, 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-284, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory