dbPTM

NKAP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NKAP_HUMAN
UniProt AC	Q8N5F7
Protein Name	NF-kappa-B-activating protein
Gene Name	NKAP
Organism	Homo sapiens (Human).
Sequence Length	415
Subcellular Localization	Nucleus .
Protein Description	Acts as a transcriptional repressor. Plays a role as a transcriptional corepressor of the Notch-mediated signaling required for T-cell development. Also involved in the TNF and IL-1 induced NF-kappa-B activation. Associates with chromatin at the Notch-regulated SKP2 promoter..
Protein Sequence	MAPVSGSRSPDREASGSGGRRRSSSKSPKPSKSARSPRGRRSRSHSCSRSGDRNGLTHQLGGLSQGSRNQSYRSRSRSRSRERPSAPRGIPFASASSSVYYGSYSRPYGSDKPWPSLLDKEREESLRQKRLSERERIGELGAPEVWGLSPKNPEPDSDEHTPVEDEEPKKSTTSASTSEEEKKKKSSRSKERSKKRRKKKSSKRKHKKYSEDSDSDSDSETDSSDEDNKRRAKKAKKKEKKKKHRSKKYKKKRSKKSRKESSDSSSKESQEEFLENPWKDRTKAEEPSDLIGPEAPKTLTSQDDKPLNYGHALLPGEGAAMAEYVKAGKRIPRRGEIGLTSEEIASFECSGYVMSGSRHRRMEAVRLRKENQIYSADEKRALASFNQEERRKRENKILASFREMVYRKTKGKDDK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MAPVSGSRSPDR ---CCCCCCCCCCCC	29.96	23401153
7	Phosphorylation	-MAPVSGSRSPDREA -CCCCCCCCCCCCCC	23.29	23401153
9	Phosphorylation	APVSGSRSPDREASG CCCCCCCCCCCCCCC	32.61	23401153
15	Phosphorylation	RSPDREASGSGGRRR CCCCCCCCCCCCCCC	28.83	23927012
17	Phosphorylation	PDREASGSGGRRRSS CCCCCCCCCCCCCCC	35.26	23927012
23	Phosphorylation	GSGGRRRSSSKSPKP CCCCCCCCCCCCCCC	36.83	28985074
24	Phosphorylation	SGGRRRSSSKSPKPS CCCCCCCCCCCCCCC	39.72	28985074
25	Phosphorylation	GGRRRSSSKSPKPSK CCCCCCCCCCCCCCC	38.10	28985074
27	Phosphorylation	RRRSSSKSPKPSKSA CCCCCCCCCCCCCCC	39.85	33259812
31	Phosphorylation	SSKSPKPSKSARSPR CCCCCCCCCCCCCCC	45.42	30177828
33	Phosphorylation	KSPKPSKSARSPRGR CCCCCCCCCCCCCCC	33.00	20860994
46	Phosphorylation	GRRSRSHSCSRSGDR CCCCCCCCCCCCCCC	18.29	-
50	Phosphorylation	RSHSCSRSGDRNGLT CCCCCCCCCCCCCCC	28.84	28450419
57	Phosphorylation	SGDRNGLTHQLGGLS CCCCCCCCCCCCCCC	14.69	28450419
64	Phosphorylation	THQLGGLSQGSRNQS CCCCCCCCCCCCCHH	35.45	17525332
67	Phosphorylation	LGGLSQGSRNQSYRS CCCCCCCCCCHHHHH	22.03	28450419
78	Phosphorylation	SYRSRSRSRSRERPS HHHHHHCCCCCCCCC	35.54	20068231
80	Phosphorylation	RSRSRSRSRERPSAP HHHHCCCCCCCCCCC	39.48	20363803
85	Phosphorylation	SRSRERPSAPRGIPF CCCCCCCCCCCCCCC	58.06	23312004
94	Phosphorylation	PRGIPFASASSSVYY CCCCCCCCCCCCEEE	29.12	24144214
96	Phosphorylation	GIPFASASSSVYYGS CCCCCCCCCCEEEEC	22.20	24144214
97	Phosphorylation	IPFASASSSVYYGSY CCCCCCCCCEEEECC	24.44	24144214
98	Phosphorylation	PFASASSSVYYGSYS CCCCCCCCEEEECCC	16.19	24144214
100	Phosphorylation	ASASSSVYYGSYSRP CCCCCCEEEECCCCC	12.21	24144214
101	Phosphorylation	SASSSVYYGSYSRPY CCCCCEEEECCCCCC	9.46	24144214
103	Phosphorylation	SSSVYYGSYSRPYGS CCCEEEECCCCCCCC	12.10	24144214
104	Phosphorylation	SSVYYGSYSRPYGSD CCEEEECCCCCCCCC	12.34	24144214
105	Phosphorylation	SVYYGSYSRPYGSDK CEEEECCCCCCCCCC	28.60	24144214
108	Phosphorylation	YGSYSRPYGSDKPWP EECCCCCCCCCCCCH	28.31	24144214
110	Phosphorylation	SYSRPYGSDKPWPSL CCCCCCCCCCCCHHH	36.30	24144214
112	Acetylation	SRPYGSDKPWPSLLD CCCCCCCCCCHHHCC	51.16	19608861
149	Phosphorylation	APEVWGLSPKNPEPD CCCCCCCCCCCCCCC	29.86	19664994
151	Ubiquitination	EVWGLSPKNPEPDSD CCCCCCCCCCCCCCC	80.09	-
157	Phosphorylation	PKNPEPDSDEHTPVE CCCCCCCCCCCCCCC	56.46	29255136
161	Phosphorylation	EPDSDEHTPVEDEEP CCCCCCCCCCCCCCC	27.29	29255136
171	Phosphorylation	EDEEPKKSTTSASTS CCCCCCCCCCCCCCC	42.94	28102081
172	Phosphorylation	DEEPKKSTTSASTSE CCCCCCCCCCCCCCH	33.38	28102081
173	Phosphorylation	EEPKKSTTSASTSEE CCCCCCCCCCCCCHH	29.41	28102081
174	Phosphorylation	EPKKSTTSASTSEEE CCCCCCCCCCCCHHH	21.95	28102081
176	Phosphorylation	KKSTTSASTSEEEKK CCCCCCCCCCHHHHH	32.03	28985074
177	Phosphorylation	KSTTSASTSEEEKKK CCCCCCCCCHHHHHH	39.61	30576142
178	Phosphorylation	STTSASTSEEEKKKK CCCCCCCCHHHHHHH	40.28	30576142
209	Phosphorylation	SKRKHKKYSEDSDSD HHHHHHHCCCCCCCC	23.30	30576142
210	Phosphorylation	KRKHKKYSEDSDSDS HHHHHHCCCCCCCCC	43.75	30576142
213	Phosphorylation	HKKYSEDSDSDSDSE HHHCCCCCCCCCCCC	34.66	30576142
215	Phosphorylation	KYSEDSDSDSDSETD HCCCCCCCCCCCCCC	42.86	30576142
224	Phosphorylation	SDSETDSSDEDNKRR CCCCCCCCHHHHHHH	48.07	-
249	Phosphorylation	KKHRSKKYKKKRSKK HHHHHHHHHHHHHHH	31.60	-
261	Phosphorylation	SKKSRKESSDSSSKE HHHHHHHCCCCCCHH	42.34	17081983
262	Phosphorylation	KKSRKESSDSSSKES HHHHHHCCCCCCHHH	42.47	17081983
264	Phosphorylation	SRKESSDSSSKESQE HHHHCCCCCCHHHHH	38.16	17081983
265	Phosphorylation	RKESSDSSSKESQEE HHHCCCCCCHHHHHH	50.88	17081983
266	Phosphorylation	KESSDSSSKESQEEF HHCCCCCCHHHHHHH	44.38	17081983
269	Phosphorylation	SDSSSKESQEEFLEN CCCCCHHHHHHHHHC	46.78	17081983
280	Ubiquitination	FLENPWKDRTKAEEP HHHCCCCCCCCCCCC	60.66	24816145
282	Phosphorylation	ENPWKDRTKAEEPSD HCCCCCCCCCCCCHH	44.75	28555341
283	Sumoylation	NPWKDRTKAEEPSDL CCCCCCCCCCCCHHC	55.48	-
283	Ubiquitination	NPWKDRTKAEEPSDL CCCCCCCCCCCCHHC	55.48	-
283	Sumoylation	NPWKDRTKAEEPSDL CCCCCCCCCCCCHHC	55.48	28112733
298	Phosphorylation	IGPEAPKTLTSQDDK CCCCCCCCCCCCCCC	33.92	29978859
300	Phosphorylation	PEAPKTLTSQDDKPL CCCCCCCCCCCCCCC	29.58	29978859
301	Phosphorylation	EAPKTLTSQDDKPLN CCCCCCCCCCCCCCC	34.42	28464451
305	Ubiquitination	TLTSQDDKPLNYGHA CCCCCCCCCCCCCCC	60.74	29967540
305	Acetylation	TLTSQDDKPLNYGHA CCCCCCCCCCCCCCC	60.74	26051181
305	Sumoylation	TLTSQDDKPLNYGHA CCCCCCCCCCCCCCC	60.74	28112733
309	Phosphorylation	QDDKPLNYGHALLPG CCCCCCCCCCCCCCC	20.26	29978859
324	Phosphorylation	EGAAMAEYVKAGKRI CHHHHHHHHHCCCCC	9.56	27642862
326	Ubiquitination	AAMAEYVKAGKRIPR HHHHHHHHCCCCCCC	50.98	29967540
334	Methylation	AGKRIPRRGEIGLTS CCCCCCCCCCCCCCH	41.56	115485057
352	Phosphorylation	ASFECSGYVMSGSRH HEEECCEEECCCCHH	4.08	-
355	Phosphorylation	ECSGYVMSGSRHRRM ECCEEECCCCHHHHH	24.47	-
357	Phosphorylation	SGYVMSGSRHRRMEA CEEECCCCHHHHHHH	20.01	-
374	Phosphorylation	LRKENQIYSADEKRA HHHHCCCCCHHHHHH	6.50	30576142
375	Phosphorylation	RKENQIYSADEKRAL HHHCCCCCHHHHHHH	30.76	21815630
379	Ubiquitination	QIYSADEKRALASFN CCCCHHHHHHHHHCC	43.44	24816145
400	Phosphorylation	RENKILASFREMVYR HHHHHHHHHHHHHHH	22.76	24719451

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

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
F124A_HUMAN	FAM124A	physical	16189514
CEP70_HUMAN	CEP70	physical	16189514
LC7L2_HUMAN	LUC7L2	physical	16169070
PR40A_HUMAN	PRPF40A	physical	22365833
DHX15_HUMAN	DHX15	physical	22365833
U2AF1_HUMAN	U2AF1	physical	22365833
BUB3_HUMAN	BUB3	physical	22365833
RBM39_HUMAN	RBM39	physical	22365833
PRPF3_HUMAN	PRPF3	physical	22365833
RBMX2_HUMAN	RBMX2	physical	22365833
DDX41_HUMAN	DDX41	physical	22365833
DHX8_HUMAN	DHX8	physical	22365833
PPIG_HUMAN	PPIG	physical	22365833
F10C1_HUMAN	FRA10AC1	physical	22365833
PCBP2_HUMAN	PCBP2	physical	22365833
NKAP_HUMAN	NKAP	physical	22365833
TTC14_HUMAN	TTC14	physical	22365833
NKAPL_HUMAN	NKAPL	physical	28514442
CAPON_HUMAN	NOS1AP	physical	28514442
DDX41_HUMAN	DDX41	physical	28514442
CA226_HUMAN	C1orf226	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	28514442
JMJD6_HUMAN	JMJD6	physical	28514442
NINL_HUMAN	NINL	physical	28514442
CHD9_HUMAN	CHD9	physical	28514442
CSK2B_HUMAN	CSNK2B	physical	28514442
FRIL_HUMAN	FTL	physical	28514442
TOPRS_HUMAN	TOPORS	physical	28514442
UBP7_HUMAN	USP7	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
ZZEF1_HUMAN	ZZEF1	physical	28514442
RBM25_HUMAN	RBM25	physical	28514442
PININ_HUMAN	PNN	physical	28514442
ARMC8_HUMAN	ARMC8	physical	28514442
ZCH18_HUMAN	ZC3H18	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442
HECD3_HUMAN	HECTD3	physical	28514442
CBY1_HUMAN	CBY1	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.

Regulatory Network of NKAP_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-149; SER-157 ANDTHR-161, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-149, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-149, AND MASSSPECTROMETRY.	18691976 [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-64, AND MASSSPECTROMETRY.	17525332 [Abstract]
"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-9; SER-149; SER-261;SER-262; SER-264; SER-265; SER-266 AND SER-269, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASSSPECTROMETRY.	16097034 [Abstract]