NIT1_HUMAN - dbPTM
NIT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NIT1_HUMAN
UniProt AC Q86X76
Protein Name Deaminated glutathione amidase
Gene Name NIT1
Organism Homo sapiens (Human).
Sequence Length 327
Subcellular Localization Isoform 2: Mitochondrion .
Isoform 1: Cytoplasm .
Protein Description Catalyzes the hydrolysis of the amide bond in N-(4-oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite repair reaction to dispose of the harmful deaminated glutathione. Plays a role in cell growth and apoptosis: loss of expression promotes cell growth, resistance to DNA damage stress and increased incidence to NMBA-induced tumors. Has tumor suppressor properties that enhances the apoptotic responsiveness in cancer cells; this effect is additive to the tumor suppressor activity of FHIT. It is also a negative regulator of primary T-cells..
Protein Sequence MLGFITRPPHRFLSLLCPGLRIPQLSVLCAQPRPRAMAISSSSCELPLVAVCQVTSTPDKQQNFKTCAELVREAARLGACLAFLPEAFDFIARDPAETLHLSEPLGGKLLEEYTQLARECGLWLSLGGFHERGQDWEQTQKIYNCHVLLNSKGAVVATYRKTHLCDVEIPGQGPMCESNSTMPGPSLESPVSTPAGKIGLAVCYDMRFPELSLALAQAGAEILTYPSAFGSITGPAHWEVLLRARAIETQCYVVAAAQCGRHHEKRASYGHSMVVDPWGTVVARCSEGPGLCLARIDLNYLRQLRRHLPVFQHRRPDLYGNLGHPLS
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 Orthologous
Protein Cluster
40PhosphorylationRPRAMAISSSSCELP
CCCEEEECCCCCCCC
18.0325693802
41PhosphorylationPRAMAISSSSCELPL
CCEEEECCCCCCCCE
21.8425693802
42PhosphorylationRAMAISSSSCELPLV
CEEEECCCCCCCCEE
32.0225693802
43PhosphorylationAMAISSSSCELPLVA
EEEECCCCCCCCEEE
17.3525693802
65UbiquitinationPDKQQNFKTCAELVR
CCHHHCHHHHHHHHH
50.69-
72 (in isoform 2)Ubiquitination-40.2221906983
77 (in isoform 3)Ubiquitination-4.35-
93 (in isoform 4)Ubiquitination-45.7021906983
102PhosphorylationPAETLHLSEPLGGKL
HHHHCCCCCCCCHHH
26.8120071362
108UbiquitinationLSEPLGGKLLEEYTQ
CCCCCCHHHHHHHHH
48.372190698
108 (in isoform 1)Ubiquitination-48.3721906983
125 (in isoform 3)Ubiquitination-17.2421906983
141UbiquitinationQDWEQTQKIYNCHVL
CCHHHHHHHHEEEEE
51.01-
143PhosphorylationWEQTQKIYNCHVLLN
HHHHHHHHEEEEEEC
20.8322817900
151PhosphorylationNCHVLLNSKGAVVAT
EEEEEECCCCEEEEE
32.2228634298
152AcetylationCHVLLNSKGAVVATY
EEEEECCCCEEEEEE
50.2230590753
158 (in isoform 3)Ubiquitination-16.55-
158PhosphorylationSKGAVVATYRKTHLC
CCCEEEEEEEECCCC
16.5521406692
159PhosphorylationKGAVVATYRKTHLCD
CCEEEEEEEECCCCC
10.6025072903
178PhosphorylationGQGPMCESNSTMPGP
CCCCCCCCCCCCCCC
31.02-
180PhosphorylationGPMCESNSTMPGPSL
CCCCCCCCCCCCCCC
35.05-
268PhosphorylationRHHEKRASYGHSMVV
CCCCHHHHCCCCEEE
35.3628857561
269PhosphorylationHHEKRASYGHSMVVD
CCCHHHHCCCCEEEC
20.2028857561
272PhosphorylationKRASYGHSMVVDPWG
HHHHCCCCEEECCCC
14.6528857561
319PhosphorylationQHRRPDLYGNLGHPL
CCCCCCCCCCCCCCC
16.0227642862
327PhosphorylationGNLGHPLS-------
CCCCCCCC-------
42.5026091039

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 NIT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NIT1_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 NIT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC6_HUMANXRCC6physical
16169070
CUX1_HUMANCUX1physical
26344197
CASP_HUMANCUX1physical
26344197
PSMG4_HUMANPSMG4physical
26344197
NIT1_HUMANNIT1physical
27499296
UCP4_HUMANSLC25A27physical
27499296
CAF17_HUMANIBA57physical
27499296
MPPB_HUMANPMPCBphysical
27499296
MPPA_HUMANPMPCAphysical
27499296
HOGA1_HUMANHOGA1physical
27499296
NUDT8_HUMANNUDT8physical
27499296
BOLA3_HUMANBOLA3physical
27499296
PREP_HUMANPITRM1physical
27499296
ECH1_HUMANECH1physical
27499296
PDIP2_HUMANPOLDIP2physical
27499296
C1QBP_HUMANC1QBPphysical
27499296
IDE_HUMANIDEphysical
27499296
GTPB8_HUMANGTPBP8physical
28514442
MRM2_HUMANFTSJ2physical
28514442
DPOG1_HUMANPOLGphysical
28514442
ACSF2_HUMANACSF2physical
28514442
SYLM_HUMANLARS2physical
28514442
MCAT_HUMANSLC25A20physical
28514442
NPS3A_HUMANNIPSNAP3Aphysical
28514442
ADRO_HUMANFDXRphysical
28514442
MRRP3_HUMANKIAA0391physical
28514442
NUD19_HUMANNUDT19physical
28514442
SYNM_HUMANNARS2physical
28514442
RUSD3_HUMANRPUSD3physical
28514442
FOLC_HUMANFPGSphysical
28514442
TOP3A_HUMANTOP3Aphysical
28514442
BCKD_HUMANBCKDKphysical
28514442
SIR3_HUMANSIRT3physical
28514442
HEMH_HUMANFECHphysical
28514442
TAZ_HUMANTAZphysical
28514442
BCAT2_HUMANBCAT2physical
28514442
CQ080_HUMANC17orf80physical
28514442
PDPR_HUMANPDPRphysical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
CLPX_HUMANCLPXphysical
28514442

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 NIT1_HUMAN

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Related Literatures of Post-Translational Modification

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