Home

NKEF-A (human)

Overview NKEF-A a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). May have a proliferative effect and play a role in cancer development or progression. Note: This description may include information from UniProtKB. Protein type: EC 1.11.1.15; Oxidoreductase Cellular Component: mitochondrion; cytoplasm; melanosome; nucleus Molecular Function: identical protein binding; protein binding; peroxidase activity; thioredoxin peroxidase activity Biological Process: regulation of stress-activated MAPK cascade; cell proliferation; erythrocyte homeostasis; removal of superoxide radicals; natural killer cell mediated cytotoxicity; hydrogen peroxide catabolic process; skeletal development; regulation of NF-kappaB import into nucleus Reference #:  Q06830 (UniProtKB) Alt. Names/Synonyms: MSP23; Natural killer cell-enhancing factor A; natural killer-enhancing factor A; NKEF-A; NKEFA; PAG; PAGA; PAGB; peroxiredoxin 1; Peroxiredoxin-1; PRDX1; proliferation-associated gene A; Proliferation-associated gene protein; PRX1; PRXI; TDPX2; Thioredoxin peroxidase 2; Thioredoxin-dependent peroxide reductase 2 Gene Symbols: PRDX1 Molecular weight: 22,110 Da Basal Isoelectric point: 8.27  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below NKEF-A 2RII - A/B=1-199 (human) 3HY2 - A/B=1-199 (human) 1QQ2 - A/B=1-199 (rat) 2Z9S - A/B/C/D/E/F/G/H/I/J=1-199 (rat)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 2RII 3HY2  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
apoptosis, altered: S32‑p enzymatic activity, induced: S32‑p enzymatic activity, inhibited: T90‑p, Y194‑p intracellular localization: Y194‑p molecular association, regulation: T90‑p, Y194‑p protein conformation: S32‑p, T90‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		K7-a	_MSSGNAkIGHPAPN
0	1		K7	_MSSGNAKIGHPAPN
0	44		H10	SGNAkIGHPAPNFkA
0	1		N14	kIGHPAPNFkAtAVM
0	4		K16-a	GHPAPNFkAtAVMPD
0	4		K16-u	GHPAPNFkAtAVMPD
1	1		T18-p	PAPNFkAtAVMPDGQ
0	6		K27-a	VMPDGQFkDISLsDy
0	10		K27-u	VMPDGQFkDISLsDy
1	1		S32-p	QFkDISLsDykGkYV
0	2		Y34-p	kDISLsDykGkYVVF
0	66		K35-a	DISLsDykGkYVVFF
0	36		K35-u	DISLsDykGkYVVFF
0	1		K37-a	SLsDykGkYVVFFFY
0	1		K37-u	SLsDykGkYVVFFFY
0	6		K67-a	SDRAEEFkkLNCQVI
0	2		K68-u	DRAEEFkkLNCQVIG
3	0		T90-p	CHLAWVNtPkkQGGL
0	2		K92-a	LAWVNtPkkQGGLGP
0	1		K93-a	AWVNtPkkQGGLGPM
0	4		K93-u	AWVNtPkkQGGLGPM
0	57		K109-a	IPLVSDPkRtIAQDy
0	9		K109-u	IPLVSDPkRtIAQDy
1	0		T111-p	LVSDPkRtIAQDyGV
0	5		Y116-p	kRtIAQDyGVLkADE
0	12		K120-u	AQDyGVLkADEGISF
0	2		K136-a	GLFIIDDkGILRQIT
0	14		K136-u	GLFIIDDkGILRQIT
1	0		T156-p	VGRSVDEtLRLVQAF
0	5		K168-a	QAFQFTDkHGEVCPA
0	6		K168-u	QAFQFTDkHGEVCPA
0	16		K178-u	EVCPAGWkPGSDtIk
0	1		K178	EVCPAGWKPGSDtIk
1	1		T183-p	GWkPGSDtIkPDVQk
0	5		K185-u	kPGSDtIkPDVQkSk
0	3		K190-u	tIkPDVQkSkEyFSk
0	1		K192	kPDVQkSKEyFSkQK
0	3		K192-u	kPDVQkSkEyFSkQK
1	146		Y194-p	DVQkSkEyFSkQK__
0	1		K197-a	kSkEyFSkQK_____
0	3		K197-u	kSkEyFSkQK_____

	mouse
K7	_MSSGNAKIGyPAPN
K7-u	_MSSGNAkIGyPAPN
Y10-p	SGNAkIGyPAPNFkA
N14	kIGyPAPNFkATAVM
K16-a	GyPAPNFkATAVMPD
K16-u	GyPAPNFkATAVMPD
T18	PAPNFkATAVMPDGQ
K27-a	VMPDGQFkDISLsEY
K27-u	VMPDGQFkDISLsEY
S32-p	QFkDISLsEYkGKYV
Y34	kDISLsEYkGKYVVF
K35-a	DISLsEYkGKYVVFF
K35-u	DISLsEYkGKYVVFF
K37	SLsEYkGKYVVFFFY
K37	SLsEYkGKYVVFFFY
K67-a	SDRADEFkKLNCQVI
K68	DRADEFkKLNCQVIG
T90	CHLAWINTPKkQGGL
K92	LAWINTPKkQGGLGP
K93	AWINTPKKQGGLGPM
K93-u	AWINTPKkQGGLGPM
K109-a	IPLISDPkRTIAQDY
K109-u	IPLISDPkRTIAQDY
T111	LISDPkRTIAQDYGV
Y116	kRTIAQDYGVLkADE
K120-u	AQDYGVLkADEGISF
K136-a	GLFIIDDkGILRQIT
K136-u	GLFIIDDkGILRQIT
I156	VGRSVDEIIRLVQAF
K168-a	QAFQFTDkHGEVCPA
K168-u	QAFQFTDkHGEVCPA
K178-u	EVCPAGWkPGSDTIk
K178-a	EVCPAGWkPGSDTIk
T183	GWkPGSDTIkPDVNk
K185-u	kPGSDTIkPDVNkSk
K190-u	TIkPDVNkSkEyFSK
K192-a	kPDVNkSkEyFSKQK
K192	kPDVNkSKEyFSKQK
Y194-p	DVNkSkEyFSKQK__
K197	kSkEyFSKQK_____
K197	kSkEyFSKQK_____

	rat
K7	_MSSGNAKIGHPAPs
K7	_MSSGNAKIGHPAPs
H10	SGNAKIGHPAPsFKA
S14-p	KIGHPAPsFKAtAVM
K16	GHPAPsFKAtAVMPD
K16	GHPAPsFKAtAVMPD
T18-p	PAPsFKAtAVMPDGQ
K27	VMPDGQFKDISLsDy
K27	VMPDGQFKDISLsDy
S32-p	QFKDISLsDyKGKYV
Y34-p	KDISLsDyKGKYVVF
K35	DISLsDyKGKYVVFF
K35	DISLsDyKGKYVVFF
K37	SLsDyKGKYVVFFFY
K37	SLsDyKGKYVVFFFY
K67	SDRAEEFKKLNCQVI
K68	DRAEEFKKLNCQVIG
T90	CHLAWINTPKKQGGL
K92	LAWINTPKKQGGLGP
K93	AWINTPKKQGGLGPM
K93	AWINTPKKQGGLGPM
K109	IPLVSDPKRTIAQDY
K109	IPLVSDPKRTIAQDY
T111	LVSDPKRTIAQDYGV
Y116	KRTIAQDYGVLKADE
K120	AQDYGVLKADEGISF
K136	GLFIIDDKGILRQIT
K136	GLFIIDDKGILRQIT
I156	VGRSVDEILRLVQAF
K168	QAFQFTDKHGEVCPA
K168	QAFQFTDKHGEVCPA
K178	EVCPAGWKPGSDTIK
K178	EVCPAGWKPGSDTIK
T183	GWKPGSDTIKPDVNK
K185	KPGSDTIKPDVNKSK
K190	TIKPDVNKSKEyFSK
K192	KPDVNKSKEyFSKQK
K192	KPDVNKSKEyFSKQK
Y194-p	DVNKSKEyFSKQK__
K197	KSKEyFSKQK_____
K197	KSKEyFSKQK_____

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.