NLTP_HUMAN - dbPTM
NLTP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NLTP_HUMAN
UniProt AC P22307
Protein Name Non-specific lipid-transfer protein
Gene Name SCP2
Organism Homo sapiens (Human).
Sequence Length 547
Subcellular Localization Cytoplasm . Mitochondrion . Cytoplasmic in the liver and also associated with mitochondria especially in steroidogenic tissues.
Isoform SCPx: Peroxisome. Interaction with PEX5 is essential for peroxisomal import.
Isoform SCP2: Mitochondrion .
Protein Description Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis..
Protein Sequence MSSSPWEPATLRRVFVVGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFGDSTCGQRAIYHSLGMTGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLYKMGFPEAASSFRTHQIEAVPTSSASDGFKANLVFKEIEKKLEEEGEQFVKKIGGIFAFKVKDGPGGKEATWVVDVKNGKGSVLPNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMGLAMKLQNLQLQPGNAKL
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
31AcetylationFVKPGAENSRDYPDL
CCCCCCCCCCCCHHH		41.6419608861
31UbiquitinationFVKPGAENSRDYPDL
CCCCCCCCCCCCHHH		41.6419608861
34AcetylationPGAENSRDYPDLAEE
CCCCCCCCCHHHHHH		60.1719608861
34UbiquitinationPGAENSRDYPDLAEE
CCCCCCCCCHHHHHH		60.1719608861
46AcetylationAEEAGKKALADAQIP
HHHHHHHHHHHCCCC		16.0919608861
46UbiquitinationAEEAGKKALADAQIP
HHHHHHHHHHHCCCC		16.0919608861
47 (in isoform 5)Phosphorylation-6.4324719451
49UbiquitinationAGKKALADAQIPYSA
HHHHHHHHCCCCHHH		39.6019608861
49AcetylationAGKKALADAQIPYSA
HHHHHHHHCCCCHHH		39.6019608861
51AcetylationKKALADAQIPYSAVD
HHHHHHCCCCHHHCH		37.4219608861
56 (in isoform 5)Phosphorylation-11.7624719451
63AcetylationAVDQACVGYVFGDST
HCHHHHEEEECCCCC		16.8719608861
66AcetylationQACVGYVFGDSTCGQ
HHHEEEECCCCCCHH		7.2919608861
88AcetylationGMTGIPIINVNNNCA
CCCCCCEEECCCCCC		3.8519608861
102AcetylationATGSTALFMARQLIQ
CCCHHHHHHHHHHHH		3.1419608861
108AcetylationLFMARQLIQGGVAEC
HHHHHHHHHCCHHHH		2.4319608861
139AcetylationKFSDRTIPTDKHVDL
EECCCCCCCCHHHHH		33.6519608861
142AcetylationDRTIPTDKHVDLLIN
CCCCCCCHHHHHHHH		48.2625953088
159AcetylationGLSAHPVAPQMFGYA
CCCCCCCCHHHHCCC		7.9519608861
304AcetylationNDIDVIELHDCFSTN
CCCEEEEEECCCCCC		2.5819413330
357UbiquitinationLISKGHPLGATGLAQ
CCCCCCCCCHHHHHH		6.3819608861
357AcetylationLISKGHPLGATGLAQ
CCCCCCCCCHHHHHH		6.3819608861
361AcetylationGHPLGATGLAQCAEL
CCCCCHHHHHHHHHH		20.6219413330
372AcetylationCAELCWQLRGEAGKR
HHHHHHHHHCCHHCC		3.0819608861
372UbiquitinationCAELCWQLRGEAGKR
HHHHHHHHHCCHHCC		3.0819608861
389AcetylationPGAKVALQHNLGIGG
CCCHHHHHCCCCCCC		17.4319608861
399 (in isoform 2)Ubiquitination-2.4221890473
409 (in isoform 2)Ubiquitination-55.3921890473
414AcetylationFPEAASSFRTHQIEA
CHHHHHHCCCEEEEE		10.9419608861
414UbiquitinationFPEAASSFRTHQIEA
CHHHHHHCCCEEEEE		10.9419608861
418 (in isoform 2)Ubiquitination-34.3121890473
429AcetylationVPTSSASDGFKANLV
ECCCCCCCCHHHEEH		67.2819608861
429UbiquitinationVPTSSASDGFKANLV
ECCCCCCCCHHHEEH		67.2819608861
443 (in isoform 1)Ubiquitination-48.6321890473
446AcetylationEIEKKLEEEGEQFVK
HHHHHHHHHHHHHHH		80.0819608861
453 (in isoform 1)Ubiquitination-39.7121890473
454AcetylationEGEQFVKKIGGIFAF
HHHHHHHHHCCEEEE		41.0826051181
462 (in isoform 1)Ubiquitination-44.9721890473
462UbiquitinationIGGIFAFKVKDGPGG
HCCEEEEEECCCCCC		44.9721890473
462UbiquitinationIGGIFAFKVKDGPGG
HCCEEEEEECCCCCC		44.9721890473
479AcetylationATWVVDVKNGKGSVL
EEEEEEEECCCCCCC		56.3625953088
495S-nitrosylationNSDKKADCTITMADS
CCCCCCCEEEEEECH		3.3725040305
495GlutathionylationNSDKKADCTITMADS
CCCCCCCEEEEEECH		3.3722555962
534AcetylationGNMGLAMKLQNLQLQ
CCHHHHHHHCCCCCC		41.1125953088
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 NLTP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NLTP_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 NLTP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAV1_HUMANCAV1physical
15182174
RT28_HUMANMRPS28physical
22939629
TIM44_HUMANTIMM44physical
22939629
RAB8A_HUMANRAB8Aphysical
22939629
THIK_HUMANACAA1physical
22939629
UBL4A_HUMANUBL4Aphysical
22939629
RRBP1_HUMANRRBP1physical
22939629
STX7_HUMANSTX7physical
22939629
VDAC2_HUMANVDAC2physical
22939629
RBMS1_HUMANRBMS1physical
22939629
VDAC3_HUMANVDAC3physical
22939629
TBL2_HUMANTBL2physical
22939629
SCO2_HUMANSCO2physical
22939629
SUGP1_HUMANSUGP1physical
22939629
ECI2_HUMANECI2physical
22939629
RAB31_HUMANRAB31physical
22939629
SRRM2_HUMANSRRM2physical
22939629
SEPT9_HUMANSEPT9physical
22939629
RRFM_HUMANMRRFphysical
22939629
MPLKI_HUMANMPLKIPphysical
22939629
PCH2_HUMANTRIP13physical
25416956
MYO5A_HUMANMYO5Aphysical
26186194
MYO5C_HUMANMYO5Cphysical
26186194
RPA1_HUMANPOLR1Aphysical
26186194
RMP_HUMANURI1physical
26186194
PDRG1_HUMANPDRG1physical
26186194
UXT_HUMANUXTphysical
26186194
PCH2_HUMANTRIP13physical
21516116
MYO5C_HUMANMYO5Cphysical
28514442
RMP_HUMANURI1physical
28514442
MYO5A_HUMANMYO5Aphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613724Leukoencephalopathy, with dystonia and motor neuropathy (LDMN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NLTP_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-132; LYS-183; LYS-438 ANDLYS-470, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-197 AND TYR-204, ANDMASS SPECTROMETRY.

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