dbPTM

CATA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CATA_HUMAN
UniProt AC	P04040
Protein Name	Catalase
Gene Name	CAT
Organism	Homo sapiens (Human).
Sequence Length	527
Subcellular Localization	Peroxisome.
Protein Description	Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells..
Protein Sequence	MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADSRDPAS ------CCCCCCCHH	24.40	25944712
4	Phosphorylation	----MADSRDPASDQ ----CCCCCCCHHHH	29.10	28348404
9	Phosphorylation	ADSRDPASDQMQHWK CCCCCCHHHHHHHHH	33.49	24275569
16	Acetylation	SDQMQHWKEQRAAQK HHHHHHHHHHHHHHH	41.67	26822725
16	Ubiquitination	SDQMQHWKEQRAAQK HHHHHHHHHHHHHHH	41.67	-
23	Ubiquitination	KEQRAAQKADVLTTG HHHHHHHHCCEEECC	41.65	21890473
23	Acetylation	KEQRAAQKADVLTTG HHHHHHHHCCEEECC	41.65	25953088
28	Phosphorylation	AQKADVLTTGAGNPV HHHCCEEECCCCCCC	24.04	24275569
29	Phosphorylation	QKADVLTTGAGNPVG HHCCEEECCCCCCCC	22.37	24275569
38	Ubiquitination	AGNPVGDKLNVITVG CCCCCCCCCEEEEEC	35.71	-
38	Acetylation	AGNPVGDKLNVITVG CCCCCCCCCEEEEEC	35.71	23954790
47	Methylation	NVITVGPRGPLLVQD EEEEECCCCCEEEEE	54.13	-
77	Ubiquitination	PERVVHAKGAGAFGY CHHEEECCCCCCCCE	34.12	-
84	Phosphorylation	KGAGAFGYFEVTHDI CCCCCCCEEEEECCC	7.07	20090780
88	Phosphorylation	AFGYFEVTHDITKYS CCCEEEEECCCHHHC	13.46	28176486
92	Phosphorylation	FEVTHDITKYSKAKV EEEECCCHHHCHHHH	29.95	28152594
93	Acetylation	EVTHDITKYSKAKVF EEECCCHHHCHHHHH	48.11	25953088
98	Ubiquitination	ITKYSKAKVFEHIGK CHHHCHHHHHHHCCC	51.71	21890473
105	Ubiquitination	KVFEHIGKKTPIAVR HHHHHCCCCCCEEEE	53.52	-
105	2-Hydroxyisobutyrylation	KVFEHIGKKTPIAVR HHHHHCCCCCCEEEE	53.52	-
107	Phosphorylation	FEHIGKKTPIAVRFS HHHCCCCCCEEEEEE	24.34	-
114	O-linked_Glycosylation	TPIAVRFSTVAGESG CCEEEEEEECCCCCC	16.06	26374642
114	Phosphorylation	TPIAVRFSTVAGESG CCEEEEEEECCCCCC	16.06	-
115	Phosphorylation	PIAVRFSTVAGESGS CEEEEEEECCCCCCC	16.21	22817900
120	Phosphorylation	FSTVAGESGSADTVR EEECCCCCCCCCCCC	36.81	24275569
150	Phosphorylation	WDLVGNNTPIFFIRD EECCCCCCCEEEECC	23.04	-
167	Phosphorylation	LFPSFIHSQKRNPQT CCHHHHHCCCCCCCC	32.36	-
169	2-Hydroxyisobutyrylation	PSFIHSQKRNPQTHL HHHHHCCCCCCCCCC	58.10	-
187	Phosphorylation	DMVWDFWSLRPESLH HHEEEHHHCCHHHHH	17.94	24719451
221	Succinylation	GYGSHTFKLVNANGE CCCCEEEEEECCCCC	53.32	-
221	Succinylation	GYGSHTFKLVNANGE CCCCEEEEEECCCCC	53.32	-
221	Acetylation	GYGSHTFKLVNANGE CCCCEEEEEECCCCC	53.32	26051181
231	Phosphorylation	NANGEAVYCKFHYKT CCCCCEEEEEEEEEC	9.29	21082442
232	S-nitrosylation	ANGEAVYCKFHYKTD CCCCEEEEEEEEECC	2.81	25040305
233	Ubiquitination	NGEAVYCKFHYKTDQ CCCEEEEEEEEECCC	19.93	-
233	Acetylation	NGEAVYCKFHYKTDQ CCCEEEEEEEEECCC	19.93	-
237	Ubiquitination	VYCKFHYKTDQGIKN EEEEEEEECCCCCCC	36.74	-
237	Acetylation	VYCKFHYKTDQGIKN EEEEEEEECCCCCCC	36.74	27178108
243	2-Hydroxyisobutyrylation	YKTDQGIKNLSVEDA EECCCCCCCCCHHHH	59.67	-
243	Ubiquitination	YKTDQGIKNLSVEDA EECCCCCCCCCHHHH	59.67	21890473
243	Malonylation	YKTDQGIKNLSVEDA EECCCCCCCCCHHHH	59.67	26320211
243	Acetylation	YKTDQGIKNLSVEDA EECCCCCCCCCHHHH	59.67	23236377
254	Phosphorylation	VEDAARLSQEDPDYG HHHHHHHCCCCCCCC	26.43	-
254	O-linked_Glycosylation	VEDAARLSQEDPDYG HHHHHHHCCCCCCCC	26.43	26374642
260	Phosphorylation	LSQEDPDYGIRDLFN HCCCCCCCCHHHHHH	21.60	21951684
306	Succinylation	LTKVWPHKDYPLIPV CCCCCCCCCCCEEEC	55.68	-
306	Ubiquitination	LTKVWPHKDYPLIPV CCCCCCCCCCCEEEC	55.68	-
306	Acetylation	LTKVWPHKDYPLIPV CCCCCCCCCCCEEEC	55.68	26051181
306	Succinylation	LTKVWPHKDYPLIPV CCCCCCCCCCCEEEC	55.68	-
308	Phosphorylation	KVWPHKDYPLIPVGK CCCCCCCCCEEECCE	12.54	22817900
315	Ubiquitination	YPLIPVGKLVLNRNP CCEEECCEEEECCCC	35.34	-
358	Phosphorylation	LQGRLFAYPDTHRHR CCCCEEECCCCCCCC	8.36	-
370	Phosphorylation	RHRLGPNYLHIPVNC CCCCCCCCCCCCCCC	11.64	27642862
379	Phosphorylation	HIPVNCPYRARVANY CCCCCCCCHHCCCCC	21.07	21552520
386	Phosphorylation	YRARVANYQRDGPMC CHHCCCCCCCCCCCC	8.66	12777400
417	Phosphorylation	GAPEQQPSALEHSIQ CCCCCCCCHHHHHEE	40.94	-
422	Phosphorylation	QPSALEHSIQYSGEV CCCHHHHHEEECCEE	11.30	24275569
425	Phosphorylation	ALEHSIQYSGEVRRF HHHHHEEECCEEEEE	19.57	-
426	Phosphorylation	LEHSIQYSGEVRRFN HHHHEEECCEEEEEE	16.47	24275569
441	Phosphorylation	TANDDNVTQVRAFYV CCCCCCCCEEEEEEH	27.83	20068231
447	Phosphorylation	VTQVRAFYVNVLNEE CCEEEEEEHCCCCHH	7.07	-
460	S-nitrosylation	EEQRKRLCENIAGHL HHHHHHHHHHHHHHH	4.34	24105792
460	Glutathionylation	EEQRKRLCENIAGHL HHHHHHHHHHHHHHH	4.34	22555962
468	Acetylation	ENIAGHLKDAQIFIQ HHHHHHHHHHHHHHH	45.39	20167786
468	Ubiquitination	ENIAGHLKDAQIFIQ HHHHHHHHHHHHHHH	45.39	-
476	Acetylation	DAQIFIQKKAVKNFT HHHHHHHHHHHCCCC	37.57	23749302
476	Ubiquitination	DAQIFIQKKAVKNFT HHHHHHHHHHHCCCC	37.57	-
477	Ubiquitination	AQIFIQKKAVKNFTE HHHHHHHHHHCCCCC	41.87	-
480	Ubiquitination	FIQKKAVKNFTEVHP HHHHHHHCCCCCCCC	51.72	21890473
480	Acetylation	FIQKKAVKNFTEVHP HHHHHHHCCCCCCCC	51.72	155707
480	Succinylation	FIQKKAVKNFTEVHP HHHHHHHCCCCCCCC	51.72	21890473
480	Succinylation	FIQKKAVKNFTEVHP HHHHHHHCCCCCCCC	51.72	-
499	Ubiquitination	HIQALLDKYNAEKPK HHHHHHHHHCCCCCC	40.13	-
499	Acetylation	HIQALLDKYNAEKPK HHHHHHHHHCCCCCC	40.13	25953088
506	Ubiquitination	KYNAEKPKNAIHTFV HHCCCCCCCHHHHHH	70.81	-
511	Phosphorylation	KPKNAIHTFVQSGSH CCCCHHHHHHHCCCH	21.27	26657352
515	Phosphorylation	AIHTFVQSGSHLAAR HHHHHHHCCCHHHHH	36.64	23401153
517	Phosphorylation	HTFVQSGSHLAAREK HHHHHCCCHHHHHHH	22.15	23401153

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
167	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
231	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
231	Y	Phosphorylation	Kinase	ABL2	P42684	PhosphoELM
231	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
386	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
386	Y	Phosphorylation	Kinase	ABL2	P42684	PhosphoELM
386	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ABL1_HUMAN	ABL1	physical	12777400
ABL2_HUMAN	ABL2	physical	12777400
CATA_HUMAN	CAT	physical	10666617
PEX5_HUMAN	PEX5	physical	10567403
A4_HUMAN	APP	physical	21832049
DHB4_HUMAN	HSD17B4	physical	22939629
STIM1_HUMAN	STIM1	physical	22939629
MECP2_HUMAN	MECP2	physical	22939629
ECHP_HUMAN	EHHADH	physical	16781659
TBA8_HUMAN	EHHADH	physical	16781659
CATA_HUMAN	CAT	physical	21988832
KEAP1_HUMAN	KEAP1	physical	21988832
CYC_HUMAN	CYCS	physical	26344197
FAHD1_HUMAN	FAHD1	physical	26344197
FAH2A_HUMAN	FAHD2A	physical	26344197
PRDX1_HUMAN	PRDX1	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
PRDX5_HUMAN	PRDX5	physical	26344197
TNG2_HUMAN	TANGO2	physical	26344197
GNAS3_HUMAN	GNAS	physical	26496610
GNAS2_HUMAN	GNAS	physical	26496610
ALEX_HUMAN	GNAS	physical	26496610
GNAS1_HUMAN	GNAS	physical	26496610
PLAK_HUMAN	JUP	physical	26496610
SMCA4_HUMAN	SMARCA4	physical	26496610
ARP3_HUMAN	ACTR3	physical	26496610

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614097	Acatalasemia (ACATLAS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01213	Fomepizole

Regulatory Network of CATA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-231 AND TYR-308, ANDMASS SPECTROMETRY.	18083107 [Abstract]