CENPH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CENPH_HUMAN
• UniProt AC: Q9H3R5
• Protein Name: Centromere protein H
• Gene Name: CENPH {ECO:0000312|HGNC:HGNC:17268}
• Organism: Homo sapiens (Human).
• Sequence Length: 247
• Subcellular Localization: Nucleus. Chromosome, centromere, kinetochore. Associates with active centromere-kinetochore complexes throughout the cell cycle. Colocalizes with inner kinetochore plate proteins CENPA and CENPC during both interphase and metaphase.
• Protein Description: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate..
• Protein Sequence: MEEQPQMQDADEPADSGGEGRAGGPPQVAGAQAACSEDRMTLLLRLRAQTKQQLLEYKSMVDASEEKTPEQIMQEKQIEAKIEDLENEIEEVKVAFEIKKLALDRMRLSTALKKNLEKISRQSSVLMDNMKHLLELNKLIMKSQQESWDLEEKLLDIRKKRLQLKQASESKLLEIQTEKNKQKIDLDSMENSERIKIIRQNLQMEIKITTVIQHVFQNLILGSKVNWAEDPALKEIVLQLEKNVDMM

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
1	Acetylation	-------MEEQPQMQ -------CCCCCCCC	13.27	22814378
16	Phosphorylation	DADEPADSGGEGRAG CCCCCCCCCCCCCCC	51.29	19691289
21	Methylation	ADSGGEGRAGGPPQV CCCCCCCCCCCCCCC	26.25	-
41	Phosphorylation	ACSEDRMTLLLRLRA HCCCCHHHHHHHHHH	18.36	23403867
50	Phosphorylation	LLRLRAQTKQQLLEY HHHHHHHHHHHHHHH	29.81	25072903
51	Ubiquitination	LRLRAQTKQQLLEYK HHHHHHHHHHHHHHH	24.78	-
57	Phosphorylation	TKQQLLEYKSMVDAS HHHHHHHHHHHCCCC	14.34	25072903
58	Ubiquitination	KQQLLEYKSMVDASE HHHHHHHHHHCCCCC	23.77	-
59	Phosphorylation	QQLLEYKSMVDASEE HHHHHHHHHCCCCCC	24.12	23403867
64	Phosphorylation	YKSMVDASEEKTPEQ HHHHCCCCCCCCHHH	41.65	23403867
67	Sumoylation	MVDASEEKTPEQIMQ HCCCCCCCCHHHHHH	66.39	28112733
68	Phosphorylation	VDASEEKTPEQIMQE CCCCCCCCHHHHHHH	35.02	23401153
76	Ubiquitination	PEQIMQEKQIEAKIE HHHHHHHHHHHHHHH	39.42	21890473
81	Ubiquitination	QEKQIEAKIEDLENE HHHHHHHHHHHHHHH	33.56	-
118	Ubiquitination	ALKKNLEKISRQSSV HHHHHHHHHHHHHHH	49.50	-
120	Phosphorylation	KKNLEKISRQSSVLM HHHHHHHHHHHHHHH	35.02	26074081
123	Phosphorylation	LEKISRQSSVLMDNM HHHHHHHHHHHHHHH	22.70	26074081
124	Phosphorylation	EKISRQSSVLMDNMK HHHHHHHHHHHHHHH	15.78	26074081
131	Ubiquitination	SVLMDNMKHLLELNK HHHHHHHHHHHHHHH	37.04	21890473
138	Ubiquitination	KHLLELNKLIMKSQQ HHHHHHHHHHHHHHH	52.60	-
142	Ubiquitination	ELNKLIMKSQQESWD HHHHHHHHHHHHCCC	37.81	-
153	Ubiquitination	ESWDLEEKLLDIRKK HCCCHHHHHHHHHHH	45.00	-
165	Ubiquitination	RKKRLQLKQASESKL HHHHHHHHHHCHHHH	30.75	-
171	Ubiquitination	LKQASESKLLEIQTE HHHHCHHHHHHHHHH	53.71	-
179	Acetylation	LLEIQTEKNKQKIDL HHHHHHHHCCCCCCH	73.21	25953088
179	Ubiquitination	LLEIQTEKNKQKIDL HHHHHHHHCCCCCCH	73.21	-
181	Ubiquitination	EIQTEKNKQKIDLDS HHHHHHCCCCCCHHH	65.13	-
183	Ubiquitination	QTEKNKQKIDLDSME HHHHCCCCCCHHHCC	39.53	-
223	Phosphorylation	FQNLILGSKVNWAED HHHHHHCCCCCCCCC	29.95	-
224	Ubiquitination	QNLILGSKVNWAEDP HHHHHCCCCCCCCCH	37.48	-
234	Ubiquitination	WAEDPALKEIVLQLE CCCCHHHHHHHHHHH	47.72	-

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PMVK_HUMAN	PMVK	physical	17353931
CENPH_HUMAN	CENPH	physical	11092768
KIF2C_HUMAN	KIF2C	physical	11092768
CENPU_HUMAN	CENPU	physical	21454580
CENPI_HUMAN	CENPI	physical	16622420
CENPK_HUMAN	CENPK	physical	16622420
TRI36_HUMAN	TRIM36	physical	19232519
NDC80_HUMAN	NDC80	physical	15713649
NUF2_HUMAN	NUF2	physical	15713649
CENPH_HUMAN	CENPH	physical	25416956
CCD40_HUMAN	CCDC40	physical	27173435

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.

Related Literatures of Post-Translational Modification

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330