CNDH2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CNDH2_MOUSE
• UniProt AC: Q8BSP2
• Protein Name: Condensin-2 complex subunit H2
• Gene Name: Ncaph2
• Organism: Mus musculus (Mouse).
• Sequence Length: 607
• Subcellular Localization: Nucleus.
• 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. Seems to have lineage-specific role in T-cell development..
• Protein Sequence: MEDVEVRFAHLLQPIRDLTKNWEVDVAAQLGEYLEELDQICISFDEGKTTMNFIEAALLIQGSACVYSKKVEYLYSLVYQALDFISGKRRAKQLSLVQEDGSKKTVNSETPCETENEFLSLDDFPDSRANVDLKNDQASSELLIIPLLPMALVAPDEVEKNSSPLYSCQGDILASRKDFRMNTCMPNPRGCFMLDPVGMCPVEPVVPVEPYPMSRSQKDPEDAEEQPMEVSRNGSPVPVPDISQEPDGPALSGGEEDAEDGAEPLEVALEPAEPRTSQQSAILPRRYMLRERQGAPEPASRLQETPDPWQSLDPFDSLESKVFQKGKPYSVPPGVEEAPGQKRKRKGATKLQDFHKWYLDAYAEHPDGRRARRKGPTFADMEVLYWKHVKEQLETLQKLRRRKINERWLPGAKQDLWPTEEDRLEESLEDLGVADDFLEPEEYVEEPAGVMPEEAADLDAEAMPESLRYEELVRRNVELFIATSQKFIQETELSQRIRDWEDTIQPLLQEQEQHVPFDIHIYGDQLASRFPQLNEWCPFSELVAGQPAFEVCRSMLASLQLANDYTVEITQQPGLEAAVDTMSLRLLTHQRAHTRFQTYAAPSMAQP

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
19	Phosphorylation	LQPIRDLTKNWEVDV HHHHHHHCCCCCHHH	26.99	-
95	Phosphorylation	KRRAKQLSLVQEDGS CCHHHHHEEEEECCC	24.81	28066266
162	Phosphorylation	PDEVEKNSSPLYSCQ CHHHHCCCCCCCCCC	44.38	25266776
163	Phosphorylation	DEVEKNSSPLYSCQG HHHHCCCCCCCCCCC	28.46	26824392
231	Phosphorylation	EEQPMEVSRNGSPVP HHCCCEECCCCCCCC	13.51	25619855
235	Phosphorylation	MEVSRNGSPVPVPDI CEECCCCCCCCCCCC	26.69	21082442
243	Phosphorylation	PVPVPDISQEPDGPA CCCCCCCCCCCCCCC	35.55	23649490
252	Phosphorylation	EPDGPALSGGEEDAE CCCCCCCCCCCCCCC	47.02	21082442
277	Phosphorylation	EPAEPRTSQQSAILP CCCCCCCHHHHCHHC	27.74	24759943
280	Phosphorylation	EPRTSQQSAILPRRY CCCCHHHHCHHCHHH	15.05	28066266
305	Phosphorylation	PASRLQETPDPWQSL CHHHHCCCCCCHHHC	21.74	24759943
311	Phosphorylation	ETPDPWQSLDPFDSL CCCCCHHHCCCCCCH	30.76	26643407
317	Phosphorylation	QSLDPFDSLESKVFQ HHCCCCCCHHHHHHH	34.12	24759943
320	Phosphorylation	DPFDSLESKVFQKGK CCCCCHHHHHHHCCC	39.14	26643407
321	Ubiquitination	PFDSLESKVFQKGKP CCCCHHHHHHHCCCC	37.38	-
491	Phosphorylation	SQKFIQETELSQRIR CHHHHHHHHHHHHHH	26.33	28066266
494	Phosphorylation	FIQETELSQRIRDWE HHHHHHHHHHHHHHH	15.92	17525332

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

Oops, there are no upstream regulatory protein records of CNDH2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CNDH2_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 CNDH2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CNDH2_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-494, AND MASSSPECTROMETRY.
PubMed: 17525332