dbPTM

CKAP4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CKAP4_HUMAN
UniProt AC	Q07065
Protein Name	Cytoskeleton-associated protein 4
Gene Name	CKAP4
Organism	Homo sapiens (Human).
Sequence Length	602
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type II membrane protein. Cell membrane Single-pass type II membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Translocates to the perinuclear region upon APF-stimulation.
Protein Description	High-affinity epithelial cell surface receptor for APF.; Mediates the anchoring of the endoplasmic reticulum to microtubules..
Protein Sequence	MPSAKQRGSKGGHGAASPSEKGAHPSGGADDVAKKPPPAPQQPPPPPAPHPQQHPQQHPQNQAHGKGGHRGGGGGGGKSSSSSSASAAAAAAAASSSASCSRRLGRALNFLFYLALVAAAAFSGWCVHHVLEEVQQVRRSHQDFSRQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSINDNIAIFTEVQKRSQKEINDMKAKVASLEESEGNKQDLKALKEAVKEIQTSAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEAADTERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKSDSHGPKEDGGFRHSEAFEALQQKSQGLDSRLQHVEDGVLSMQVASARQTESLESLLSKSQEHEQRLAALQGRLEGLGSSEADQDGLASTVRSLGETQLVLYGDVEELKRSVGELPSTVESLQKVQEQVHTLLSQDQAQAARLPPQDFLDRLSSLDNLKASVSQVEADLKMLRTAVDSLVAYSVKIETNENNLESAKGLLDDLRNDLDRLFVKVEKIHEKV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MPSAKQRGSK -----CCCHHHCCCC	46.96	22536245
9	Phosphorylation	PSAKQRGSKGGHGAA CCHHHCCCCCCCCCC	30.25	24719451
17	Phosphorylation	KGGHGAASPSEKGAH CCCCCCCCCCCCCCC	28.55	30266825
19	Phosphorylation	GHGAASPSEKGAHPS CCCCCCCCCCCCCCC	49.82	30266825
21	2-Hydroxyisobutyrylation	GAASPSEKGAHPSGG CCCCCCCCCCCCCCC	66.78	-
21	Acetylation	GAASPSEKGAHPSGG CCCCCCCCCCCCCCC	66.78	-
21	Ubiquitination	GAASPSEKGAHPSGG CCCCCCCCCCCCCCC	66.78	-
26	Phosphorylation	SEKGAHPSGGADDVA CCCCCCCCCCCCCCC	39.74	29255136
78	Malonylation	GGGGGGGKSSSSSSA CCCCCCCCCCCCHHH	50.90	26320211
78	Ubiquitination	GGGGGGGKSSSSSSA CCCCCCCCCCCCHHH	50.90	-
79	Phosphorylation	GGGGGGKSSSSSSAS CCCCCCCCCCCHHHH	38.43	30576142
80	Phosphorylation	GGGGGKSSSSSSASA CCCCCCCCCCHHHHH	37.41	21406692
81	Phosphorylation	GGGGKSSSSSSASAA CCCCCCCCCHHHHHH	41.13	26657352
82	Phosphorylation	GGGKSSSSSSASAAA CCCCCCCCHHHHHHH	30.20	29978859
83	Phosphorylation	GGKSSSSSSASAAAA CCCCCCCHHHHHHHH	31.69	29978859
84	Phosphorylation	GKSSSSSSASAAAAA CCCCCCHHHHHHHHH	28.35	26657352
86	Phosphorylation	SSSSSSASAAAAAAA CCCCHHHHHHHHHHH	22.01	26657352
95	Phosphorylation	AAAAAAASSSASCSR HHHHHHHHCCHHHHH	21.79	29978859
96	Phosphorylation	AAAAAASSSASCSRR HHHHHHHCCHHHHHH	25.79	21406692
97	Phosphorylation	AAAAASSSASCSRRL HHHHHHCCHHHHHHH	23.00	21406692
99	Phosphorylation	AAASSSASCSRRLGR HHHHCCHHHHHHHHH	17.99	21406692
100	S-nitrosylation	AASSSASCSRRLGRA HHHCCHHHHHHHHHH	3.52	22178444
100	S-palmitoylation	AASSSASCSRRLGRA HHHCCHHHHHHHHHH	3.52	29575903
101	Phosphorylation	ASSSASCSRRLGRAL HHCCHHHHHHHHHHH	20.24	30576142
140	Phosphorylation	EVQQVRRSHQDFSRQ HHHHHHHHCHHHHHH	18.22	20860994
145	Phosphorylation	RRSHQDFSRQREELG HHHCHHHHHHHHHHH	35.47	20860994
182	2-Hydroxyisobutyrylation	ILRSSQHKQDLTEKA HHHHCHHHHHHHHHH	37.56	-
188	Ubiquitination	HKQDLTEKAVKQGES HHHHHHHHHHHHCHH	53.93	-
195	Phosphorylation	KAVKQGESEVSRISE HHHHHCHHHHHHHHH	50.55	-
198	Phosphorylation	KQGESEVSRISEVLQ HHCHHHHHHHHHHHH	21.61	-
201	Phosphorylation	ESEVSRISEVLQKLQ HHHHHHHHHHHHHHH	22.12	29449344
206	Ubiquitination	RISEVLQKLQNEILK HHHHHHHHHHHHHHH	48.13	-
213	2-Hydroxyisobutyrylation	KLQNEILKDLSDGIH HHHHHHHHHHHCCCE	63.38	-
213	Acetylation	KLQNEILKDLSDGIH HHHHHHHHHHHCCCE	63.38	26051181
213	Ubiquitination	KLQNEILKDLSDGIH HHHHHHHHHHHCCCE	63.38	21890473
213 (in isoform 1)	Ubiquitination	-	63.38	21890473
223	2-Hydroxyisobutyrylation	SDGIHVVKDARERDF HCCCEECCCHHHCCC	44.58	-
223	Acetylation	SDGIHVVKDARERDF HCCCEECCCHHHCCC	44.58	26051181
223	Malonylation	SDGIHVVKDARERDF HCCCEECCCHHHCCC	44.58	26320211
223	Ubiquitination	SDGIHVVKDARERDF HCCCEECCCHHHCCC	44.58	21906983
223 (in isoform 1)	Ubiquitination	-	44.58	21890473
231	Phosphorylation	DARERDFTSLENTVE CHHHCCCCCHHHHHH	36.37	29255136
232	Phosphorylation	ARERDFTSLENTVEE HHHCCCCCHHHHHHH	33.41	29255136
236	Phosphorylation	DFTSLENTVEERLTE CCCCHHHHHHHHHHH	21.66	25850435
247	Phosphorylation	RLTELTKSINDNIAI HHHHHHHHHHHCCHH	22.76	20446291
256	Phosphorylation	NDNIAIFTEVQKRSQ HHCCHHHHHHHHHCH	29.18	25599653
260	Acetylation	AIFTEVQKRSQKEIN HHHHHHHHHCHHHHH	60.23	26051181
270	2-Hydroxyisobutyrylation	QKEINDMKAKVASLE HHHHHHHHHHHHHHH	48.17	-
270	Acetylation	QKEINDMKAKVASLE HHHHHHHHHHHHHHH	48.17	25825284
272	2-Hydroxyisobutyrylation	EINDMKAKVASLEES HHHHHHHHHHHHHHC	32.58	-
275	Phosphorylation	DMKAKVASLEESEGN HHHHHHHHHHHCCCC	39.02	29507054
283	2-Hydroxyisobutyrylation	LEESEGNKQDLKALK HHHCCCCHHHHHHHH	56.92	-
283	Acetylation	LEESEGNKQDLKALK HHHCCCCHHHHHHHH	56.92	26051181
283	Malonylation	LEESEGNKQDLKALK HHHCCCCHHHHHHHH	56.92	26320211
283	Ubiquitination	LEESEGNKQDLKALK HHHCCCCHHHHHHHH	56.92	-
283 (in isoform 1)	Ubiquitination	-	56.92	21890473
287	2-Hydroxyisobutyrylation	EGNKQDLKALKEAVK CCCHHHHHHHHHHHH	61.02	-
287	Malonylation	EGNKQDLKALKEAVK CCCHHHHHHHHHHHH	61.02	26320211
287	Ubiquitination	EGNKQDLKALKEAVK CCCHHHHHHHHHHHH	61.02	-
290	2-Hydroxyisobutyrylation	KQDLKALKEAVKEIQ HHHHHHHHHHHHHHH	48.78	-
294	Succinylation	KALKEAVKEIQTSAK HHHHHHHHHHHHHHH	57.03	27452117
301	2-Hydroxyisobutyrylation	KEIQTSAKSREWDME HHHHHHHHHCCCCHH	50.22	-
301	Ubiquitination	KEIQTSAKSREWDME HHHHHHHHHCCCCHH	50.22	-
312	Phosphorylation	WDMEALRSTLQTMES CCHHHHHHHHHHHHH	34.03	18669648
313	Phosphorylation	DMEALRSTLQTMESD CHHHHHHHHHHHHHH	19.22	21712546
316	Phosphorylation	ALRSTLQTMESDIYT HHHHHHHHHHHHHHH	26.47	18669648
322	Phosphorylation	QTMESDIYTEVRELV HHHHHHHHHHHHHHH	11.22	27259358
323	Phosphorylation	TMESDIYTEVRELVS HHHHHHHHHHHHHHH	28.47	-
330	Phosphorylation	TEVRELVSLKQEQQA HHHHHHHHHHHHHHH	42.34	18669648
332	2-Hydroxyisobutyrylation	VRELVSLKQEQQAFK HHHHHHHHHHHHHHH	44.26	-
355	2-Hydroxyisobutyrylation	ALQALTEKLLRSEES HHHHHHHHHHCCHHH	47.81	-
355	Acetylation	ALQALTEKLLRSEES HHHHHHHHHHCCHHH	47.81	26051181
355	Ubiquitination	ALQALTEKLLRSEES HHHHHHHHHHCCHHH	47.81	21890473
355 (in isoform 1)	Ubiquitination	-	47.81	21890473
362	Phosphorylation	KLLRSEESVSRLPEE HHHCCHHHHHHCHHH	22.72	26546556
388	2-Hydroxyisobutyrylation	KSDSHGPKEDGGFRH HHCCCCCCCCCCCCH	73.38	-
405	2-Hydroxyisobutyrylation	AFEALQQKSQGLDSR HHHHHHHHHCCHHHH	31.61	-
405	Acetylation	AFEALQQKSQGLDSR HHHHHHHHHCCHHHH	31.61	26051181
405	Ubiquitination	AFEALQQKSQGLDSR HHHHHHHHHCCHHHH	31.61	-
422	Phosphorylation	HVEDGVLSMQVASAR HHHHCHHHHHCCCHH	12.55	20068231
427	Phosphorylation	VLSMQVASARQTESL HHHHHCCCHHCHHHH	25.73	20068231
431	O-linked_Glycosylation	QVASARQTESLESLL HCCCHHCHHHHHHHH	23.22	OGP
431	Phosphorylation	QVASARQTESLESLL HCCCHHCHHHHHHHH	23.22	23532336
436	Phosphorylation	RQTESLESLLSKSQE HCHHHHHHHHHCCHH	39.65	21712546
440	Acetylation	SLESLLSKSQEHEQR HHHHHHHCCHHHHHH	57.01	27452117
460	Phosphorylation	GRLEGLGSSEADQDG HHHCCCCCCHHHHCC	30.01	29255136
461	Phosphorylation	RLEGLGSSEADQDGL HHCCCCCCHHHHCCH	34.70	29255136
474	Phosphorylation	GLASTVRSLGETQLV CHHHHHHHHCCCEEE	36.07	25867546
478	Phosphorylation	TVRSLGETQLVLYGD HHHHHCCCEEEEECC	25.96	25867546
483	Phosphorylation	GETQLVLYGDVEELK CCCEEEEECCHHHHH	12.10	25867546
490	Acetylation	YGDVEELKRSVGELP ECCHHHHHHHHCCCC	46.00	26051181
490	Ubiquitination	YGDVEELKRSVGELP ECCHHHHHHHHCCCC	46.00	-
492	Phosphorylation	DVEELKRSVGELPST CHHHHHHHHCCCCHH	32.65	20068231
498	Phosphorylation	RSVGELPSTVESLQK HHHCCCCHHHHHHHH	58.68	25338102
499	O-linked_Glycosylation	SVGELPSTVESLQKV HHCCCCHHHHHHHHH	26.76	OGP
499	Phosphorylation	SVGELPSTVESLQKV HHCCCCHHHHHHHHH	26.76	20068231
502	Phosphorylation	ELPSTVESLQKVQEQ CCCHHHHHHHHHHHH	31.59	20068231
512	O-linked_Glycosylation	KVQEQVHTLLSQDQA HHHHHHHHHHCHHHH	30.45	55826817
515	Phosphorylation	EQVHTLLSQDQAQAA HHHHHHHCHHHHHHH	34.52	23312004
534	Phosphorylation	QDFLDRLSSLDNLKA HHHHHHHHHHHHHHH	29.74	22817900
535	Phosphorylation	DFLDRLSSLDNLKAS HHHHHHHHHHHHHHH	44.31	22817900
540	2-Hydroxyisobutyrylation	LSSLDNLKASVSQVE HHHHHHHHHHHHHHH	44.89	-
540	Ubiquitination	LSSLDNLKASVSQVE HHHHHHHHHHHHHHH	44.89	-
542	O-linked_Glycosylation	SLDNLKASVSQVEAD HHHHHHHHHHHHHHH	22.25	OGP
542	Phosphorylation	SLDNLKASVSQVEAD HHHHHHHHHHHHHHH	22.25	21712546
544	Phosphorylation	DNLKASVSQVEADLK HHHHHHHHHHHHHHH	26.47	21712546
551	Trimethylation	SQVEADLKMLRTAVD HHHHHHHHHHHHHHH	36.11	-
551	Methylation	SQVEADLKMLRTAVD HHHHHHHHHHHHHHH	36.11	-
551	Ubiquitination	SQVEADLKMLRTAVD HHHHHHHHHHHHHHH	36.11	2189047
551 (in isoform 1)	Ubiquitination	-	36.11	21890473
555	O-linked_Glycosylation	ADLKMLRTAVDSLVA HHHHHHHHHHHHHHH	27.37	OGP
559	Phosphorylation	MLRTAVDSLVAYSVK HHHHHHHHHHHHHEE	20.39	28152594
563	Phosphorylation	AVDSLVAYSVKIETN HHHHHHHHHEEEECC	13.40	28152594
564	O-linked_Glycosylation	VDSLVAYSVKIETNE HHHHHHHHEEEECCC	13.75	OGP
564	Phosphorylation	VDSLVAYSVKIETNE HHHHHHHHEEEECCC	13.75	28152594
576	Phosphorylation	TNENNLESAKGLLDD CCCCCHHHHHHHHHH	38.15	21712546
578	2-Hydroxyisobutyrylation	ENNLESAKGLLDDLR CCCHHHHHHHHHHHH	60.41	-
578	Ubiquitination	ENNLESAKGLLDDLR CCCHHHHHHHHHHHH	60.41	-
590	Methylation	DLRNDLDRLFVKVEK HHHHHHHHHHHHHHH	37.00	-
594	2-Hydroxyisobutyrylation	DLDRLFVKVEKIHEK HHHHHHHHHHHHHHC	37.02	-
594	Acetylation	DLDRLFVKVEKIHEK HHHHHHHHHHHHHHC	37.02	26051181
597	2-Hydroxyisobutyrylation	RLFVKVEKIHEKV-- HHHHHHHHHHHCC--	52.96	-

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
232	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
100	C	Palmitoylation		18296695
Palmitoylation at Cys-100 by ZDHHC2 is required for its trafficking from the ER to the plasma membrane and for its perinuclear localization.

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 CKAP4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HEPC_HUMAN	HAMP	physical	21988832
TSNAX_HUMAN	TSNAX	physical	21988832
NDUB7_HUMAN	NDUFB7	physical	21988832
MVP_HUMAN	MVP	physical	21988832
CKAP4_HUMAN	CKAP4	physical	21988832
THOC7_HUMAN	THOC7	physical	21988832

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 CKAP4_HUMAN

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"Palmitoylation of cytoskeleton associated protein 4 by DHHC2regulates antiproliferative factor-mediated signaling."; Planey S.L., Keay S.K., Zhang C.O., Zacharias D.A.; Mol. Biol. Cell 20:1454-1463(2009). Cited for: SUBCELLULAR LOCATION, AND PALMITOYLATION AT CYS-100 BY ZDHHC2.	19144824 [Abstract]
"A reversibly palmitoylated resident protein(p63) of an ER-Golgiintermediate compartment is related to a circulatory shockresuscitation protein."; Schweizer A., Rohrer J., Jenoe P., De Maio A., Buchman T.G.,Hauri H.-P.; J. Cell Sci. 104:685-694(1993). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 312-326; 413-429 AND491-504, SUBCELLULAR LOCATION, AND PALMITOYLATION.	8314870 [Abstract]
Phosphorylation
Reference	PubMed
"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-312; THR-316 ANDSER-330, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Phosphorylation controls CLIMP-63-mediated anchoring of theendoplasmic reticulum to microtubules."; Vedrenne C., Klopfenstein D.R., Hauri H.P.; Mol. Biol. Cell 16:1928-1937(2005). Cited for: FUNCTION IN CYTOSKELETON ANCHORING, AND PHOSPHORYLATION AT SER-3;SER-17 AND SER-19.	15703217 [Abstract]

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