NIPS2_HUMAN - dbPTM
NIPS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NIPS2_HUMAN
UniProt AC O75323
Protein Name Protein NipSnap homolog 2
Gene Name NIPSNAP2 {ECO:0000312|HGNC:HGNC:4179}
Organism Homo sapiens (Human).
Sequence Length 286
Subcellular Localization Cytoplasm . Mitochondrion outer membrane .
Protein Description May act as a positive regulator of L-type calcium channels..
Protein Sequence MAARVLRARGAAWAGGLLQRAAPCSLLPRLRTWTSSSNRSREDSWLKSLFVRKVDPRKDAHSNLLAKKETSNLYKLQFHNVKPECLEAYNKICQEVLPKIHEDKHYPCTLVGTWNTWYGEQDQAVHLWRYEGGYPALTEVMNKLRENKEFLEFRKARSDMLLSRKNQLLLEFSFWNEPVPRSGPNIYELRSYQLRPGTMIEWGNYWARAIRFRQDGNEAVGGFFSQIGQLYMVHHLWAYRDLQTREDIRNAAWHKHGWEELVYYTVPLIQEMESRIMIPLKTSPLQ
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
32PhosphorylationSLLPRLRTWTSSSNR
CHHHHHHHHCCCCCC		37.37-
34PhosphorylationLPRLRTWTSSSNRSR
HHHHHHHCCCCCCCC		20.37-
40PhosphorylationWTSSSNRSREDSWLK
HCCCCCCCCCCHHHH		44.2526437602
47UbiquitinationSREDSWLKSLFVRKV
CCCCHHHHHHHHEEC		38.5622817900
47UbiquitinationSREDSWLKSLFVRKV
CCCCHHHHHHHHEEC		38.5621890473
58UbiquitinationVRKVDPRKDAHSNLL
HEECCCCCCHHHCHH		65.7329967540
67UbiquitinationAHSNLLAKKETSNLY
HHHCHHCHHHHCCCE		51.6221890473
67UbiquitinationAHSNLLAKKETSNLY
HHHCHHCHHHHCCCE		51.6221890473
672-HydroxyisobutyrylationAHSNLLAKKETSNLY
HHHCHHCHHHHCCCE		51.62-
68UbiquitinationHSNLLAKKETSNLYK
HHCHHCHHHHCCCEE		61.6929967540
682-HydroxyisobutyrylationHSNLLAKKETSNLYK
HHCHHCHHHHCCCEE		61.69-
75AcetylationKETSNLYKLQFHNVK
HHHCCCEEEEECCCC		38.6925953088
75MalonylationKETSNLYKLQFHNVK
HHHCCCEEEEECCCC		38.6926320211
82AcetylationKLQFHNVKPECLEAY
EEEECCCCHHHHHHH		40.1825953088
91AcetylationECLEAYNKICQEVLP
HHHHHHHHHHHHHHH		31.9825953088
104AcetylationLPKIHEDKHYPCTLV
HHHHHCCCCCCEEEE		41.8925038526
143AcetylationALTEVMNKLRENKEF
HHHHHHHHHHHCHHH		30.7225953088
148SuccinylationMNKLRENKEFLEFRK
HHHHHHCHHHHHHHH		45.1227452117
148AcetylationMNKLRENKEFLEFRK
HHHHHHCHHHHHHHH		45.1225825284
148UbiquitinationMNKLRENKEFLEFRK
HHHHHHCHHHHHHHH		45.1224816145
148MalonylationMNKLRENKEFLEFRK
HHHHHHCHHHHHHHH		45.1232601280
158PhosphorylationLEFRKARSDMLLSRK
HHHHHHHHHHHHHCC		32.0328348404
164MethylationRSDMLLSRKNQLLLE
HHHHHHHCCCEEEEE		41.75-
182PhosphorylationWNEPVPRSGPNIYEL
CCCCCCCCCCCCEEE		53.1619835603
187PhosphorylationPRSGPNIYELRSYQL
CCCCCCCEEEEEEEC		18.6219835603
190MethylationGPNIYELRSYQLRPG
CCCCEEEEEEECCCC		22.75-
205PhosphorylationTMIEWGNYWARAIRF
CEEEECCEEEEEEEE		9.12-
242UbiquitinationHLWAYRDLQTREDIR
HHHHHCCCCCHHHHH		4.0724816145
249MethylationLQTREDIRNAAWHKH
CCCHHHHHHHHHHHC		38.77-
263PhosphorylationHGWEELVYYTVPLIQ
CCHHHHHEEEHHHHH		13.17-
277SulfoxidationQEMESRIMIPLKTSP
HHHHHCCCCCCCCCC		2.2221406390
281UbiquitinationSRIMIPLKTSPLQ--
HCCCCCCCCCCCC--		41.4224816145
281AcetylationSRIMIPLKTSPLQ--
HCCCCCCCCCCCC--		41.4225953088
281SuccinylationSRIMIPLKTSPLQ--
HCCCCCCCCCCCC--		41.4223954790
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 NIPS2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NIPS2_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 NIPS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FOXO3_HUMANFOXO3physical
20562859
NIPS1_HUMANNIPSNAP1physical
20562859
PSA_HUMANNPEPPSphysical
20562859
ANFY1_HUMANANKFY1physical
20562859
FKBP4_HUMANFKBP4physical
20562859
PGK1_HUMANPGK1physical
20562859
PA2G4_HUMANPA2G4physical
20562859
SYTC_HUMANTARSphysical
20562859
SYLC_HUMANLARSphysical
20562859
PFKAP_HUMANPFKPphysical
20562859
ECHA_HUMANHADHAphysical
20562859
PARP1_HUMANPARP1physical
20562859
PUR4_HUMANPFASphysical
20562859
PRKDC_HUMANPRKDCphysical
20562859
HXK1_HUMANHK1physical
20562859
GANAB_HUMANGANABphysical
20562859
MTA2_HUMANMTA2physical
20562859
SYWC_HUMANWARSphysical
20562859
LONM_HUMANLONP1physical
20562859
DX39A_HUMANDDX39Aphysical
20562859
AL9A1_HUMANALDH9A1physical
20562859
NAMPT_HUMANNAMPTphysical
20562859
CH60_HUMANHSPD1physical
26496610
NIPS1_HUMANNIPSNAP1physical
26496610
WBP11_HUMANWBP11physical
26496610
SF3B5_HUMANSF3B5physical
26496610
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 NIPS2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-148, AND MASS SPECTROMETRY.

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