APLP2_HUMAN - dbPTM
APLP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APLP2_HUMAN
UniProt AC Q06481
Protein Name Amyloid-like protein 2
Gene Name APLP2
Organism Homo sapiens (Human).
Sequence Length 763
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Nucleus .
Protein Description May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein. Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts (By similarity)..
Protein Sequence MAATGTAAAAATGRLLLLLLVGLTAPALALAGYIEALAANAGTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKKQCKSRFVTPFKCLVGEFVSDVLLVPEKCQFFHKERMEVCENHQHWHTVVKEACLTQGMTLYSYGMLLPCGVDQFHGTEYVCCPQTKIIGSVSKEEEEEDEEEEEEEDEEEDYDVYKSEFPTEADLEDFTEAAVDEDDEDEEEGEEVVEDRDYYYDTFKGDDYNEENPTEPGSDGTMSDKEITHDVKAVCSQEAMTGPCRAVMPRWYFDLSKGKCVRFIYGGCGGNRNNFESEDYCMAVCKAMIPPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKAERQTLIQHFQAMVKALEKEAASEKQQLVETHLARVEAMLNDRRRMALENYLAALQSDPPRPHRILQALRRYVRAENKDRLHTIRHYQHVLAVDPEKAAQMKSQVMTHLHVIEERRNQSLSLLYKVPYVAQEIQEEIDELLQEQRADMDQFTASISETPVDVRVSSEESEEIPPFHPFHPFPALPENEDTQPELYHPMKKGSGVGEQDGGLIGAEEKVINSKNKVDENMVIDETLDVKEMIFNAERVGGLEEERESVGPLREDFSLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLEQMQI
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
43O-linked_GlycosylationALAANAGTGFAVAEP
HHHHHCCCCCEECCH		27.07OGP
75PhosphorylationGKWEPDPTGTKSCFE
CCCCCCCCCCCCHHC		65.9430631047
77PhosphorylationWEPDPTGTKSCFETK
CCCCCCCCCCHHCCH		23.4330631047
78UbiquitinationEPDPTGTKSCFETKE
CCCCCCCCCHHCCHH		46.72-
211PhosphorylationPQTKIIGSVSKEEEE
CCCEEEEEECHHHHH		16.8926657352
213PhosphorylationTKIIGSVSKEEEEED
CEEEEEECHHHHHCC		35.7322617229
214UbiquitinationKIIGSVSKEEEEEDE
EEEEEECHHHHHCCH		67.97-
233PhosphorylationEEDEEEDYDVYKSEF
HHHHHHCCHHHHHCC		15.5829514088
236PhosphorylationEEEDYDVYKSEFPTE
HHHCCHHHHHCCCCC		13.1029514088
296O-linked_GlycosylationTEPGSDGTMSDKEIT
CCCCCCCCCCCHHHC		20.63OGP
303PhosphorylationTMSDKEITHDVKAVC
CCCCHHHCCCHHHHH		17.0820068231
311PhosphorylationHDVKAVCSQEAMTGP
CCHHHHHCCHHHCCC		25.1830576142
316PhosphorylationVCSQEAMTGPCRAVM
HHCCHHHCCCCCCCC		45.0530576142
327PhosphorylationRAVMPRWYFDLSKGK
CCCCEEEEEECCCCE		6.62-
367O-linked_GlycosylationCKAMIPPTPLPTNDV
HHHHCCCCCCCCCCC		31.9155834349
371O-linked_GlycosylationIPPTPLPTNDVDVYF
CCCCCCCCCCCEEEE		52.3055834355
380O-linked_GlycosylationDVDVYFETSADDNEH
CCEEEEECCCCCCHH		21.2255834361
381O-linked_GlycosylationVDVYFETSADDNEHA
CEEEEECCCCCCHHH		23.6255834367
420UbiquitinationEEAELQAKNLPKAER
HHHHHHHCCCCHHHH		46.16-
465 (in isoform 2)Ubiquitination-27.88-
467MethylationVEAMLNDRRRMALEN
HHHHHHHHHHHHHHH		27.34-
503 (in isoform 5)Ubiquitination-70.7021890473
515 (in isoform 5)Ubiquitination-3.4521890473
527PhosphorylationEKAAQMKSQVMTHLH
HHHHHHHHHHHHHHH		23.7527174698
531PhosphorylationQMKSQVMTHLHVIEE
HHHHHHHHHHHHHHH		23.5620068231
576O-linked_GlycosylationRADMDQFTASISETP
HCCHHHHHHHHHCCC		17.54OGP
580O-linked_GlycosylationDQFTASISETPVDVR
HHHHHHHHCCCCEEE		32.68OGP
589PhosphorylationTPVDVRVSSEESEEI
CCCEEECCCCCCCCC		22.8226091039
590PhosphorylationPVDVRVSSEESEEIP
CCEEECCCCCCCCCC		42.3914702039
658O-linked_GlycosylationENMVIDETLDVKEMI
CCCEECCCCCHHHHH		25.2255828131
676 (in isoform 4)Ubiquitination-68.3521890473
688 (in isoform 4)Ubiquitination-7.2921890473
688 (in isoform 2)Ubiquitination-7.2921890473
700 (in isoform 2)Ubiquitination-2.9521890473
723PhosphorylationLRKRQYGTISHGIVE
HHHCCCCCCCCCEEE		17.8622817900
732UbiquitinationSHGIVEVDPMLTPEE
CCCEEEECCCCCHHH		14.9121890473
732 (in isoform 3)Ubiquitination-14.9121890473
736PhosphorylationVEVDPMLTPEERHLN
EEECCCCCHHHHHHH		23.5414970211
744UbiquitinationPEERHLNKMQNHGYE
HHHHHHHHHHHCCCC		48.5021890473
744UbiquitinationPEERHLNKMQNHGYE
HHHHHHHHHHHCCCC		48.5021890473
744 (in isoform 1)Ubiquitination-48.5021890473
744 (in isoform 3)Ubiquitination-48.5021890473
750PhosphorylationNKMQNHGYENPTYKY
HHHHHCCCCCCCHHH		12.6521945579
754PhosphorylationNHGYENPTYKYLEQM
HCCCCCCCHHHHHHH		44.2021945579
755PhosphorylationHGYENPTYKYLEQMQ
CCCCCCCHHHHHHHC		10.0121945579
756 (in isoform 1)Ubiquitination-45.9221890473
756UbiquitinationGYENPTYKYLEQMQI
CCCCCCHHHHHHHCC		45.9221890473
757PhosphorylationYENPTYKYLEQMQI-
CCCCCHHHHHHHCC-		12.6927259358
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
590SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
723TPhosphorylationKinasePRKCAP17252
GPS
723TPhosphorylationKinasePKC-FAMILY-GPS
723TPhosphorylationKinasePKC_GROUP-PhosphoELM
736TPhosphorylationKinaseCDK1P06493
PSP
736TPhosphorylationKinaseMAPK8P45983
GPS
736TPhosphorylationKinaseMAPK9P45984
GPS
736TPhosphorylationKinaseMAPK10P53779
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APLP2_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 APLP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BAG6_HUMANBAG6physical
22641691
RL26_HUMANRPL26physical
21988832
NKTR_HUMANNKTRphysical
27173435
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 APLP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-750, AND MASSSPECTROMETRY.
"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-750 AND TYR-755, ANDMASS SPECTROMETRY.

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