AGGF1_HUMAN - dbPTM
AGGF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGGF1_HUMAN
UniProt AC Q8N302
Protein Name Angiogenic factor with G patch and FHA domains 1
Gene Name AGGF1
Organism Homo sapiens (Human).
Sequence Length 714
Subcellular Localization Cytoplasm . Secreted . Cytoplasmic in microvascular endothelial cells. Upon angiogenesis, when endothelial cell tube formation is initiated, it is secreted.
Protein Description Promotes angiogenesis and the proliferation of endothelial cells. Able to bind to endothelial cells and promote cell proliferation, suggesting that it may act in an autocrine fashion..
Protein Sequence MASEAPSPPRSPPPPTSPEPELAQLRRKVEKLERELRSCKRQVREIEKLLHHTERLYQNAESNNQELRTQVEELSKILQRGRNEDNKKSDVEVQTENHAPWSISDYFYQTYYNDVSLPNKVTELSDQQDQAIETSILNSKDHLQVENDAYPGTDRTENVKYRQVDHFASNSQEPASALATEDTSLEGSSLAESLRAAAEAAVSQTGFSYDENTGLYFDHSTGFYYDSENQLYYDPSTGIYYYCDVESGRYQFHSRVDLQPYPTSSTKQSKDKKLKKKRKDPDSSATNEEKDLNSEDQKAFSVEHTSCNEEENFANMKKKAKIGIHHKNSPPKVTVPTSGNTIESPLHENISNSTSFKDEKIMETDSEPEEGEITDSQTEDSYDEAITSEGNVTAEDSEDEDEDKIWPPCIRVIVIRSPVLQIGSLFIITAVNPATIGREKDMEHTLRIPEVGVSKFHAEIYFDHDLQSYVLVDQGSQNGTIVNGKQILQPKTKCDPYVLEHGDEVKIGETVLSFHIHPGSDTCDGCEPGQVRAHLRLDKKDESFVGPTLSKEEKELERRKELKKIRVKYGLQNTEYEDEKTLKNPKYKDRAGKRREQVGSEGTFQRDDAPASVHSEITDSNKGRKMLEKMGWKKGEGLGKDGGGMKTPIQLQLRRTHAGLGTGKPSSFEDVHLLQNKNKKNWDKARERFTENFPETKPQKDDPGTMPWVKGTLE
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
2Acetylation------MASEAPSPP
------CCCCCCCCC		18.9719413330
3Phosphorylation-----MASEAPSPPR
-----CCCCCCCCCC		32.7529255136
7Phosphorylation-MASEAPSPPRSPPP
-CCCCCCCCCCCCCC		55.3629255136
11PhosphorylationEAPSPPRSPPPPTSP
CCCCCCCCCCCCCCC		47.7529255136
16PhosphorylationPRSPPPPTSPEPELA
CCCCCCCCCCCHHHH		63.7929255136
17PhosphorylationRSPPPPTSPEPELAQ
CCCCCCCCCCHHHHH		32.8029255136
31UbiquitinationQLRRKVEKLERELRS
HHHHHHHHHHHHHHH		59.6524816145
48UbiquitinationRQVREIEKLLHHTER
HHHHHHHHHHHHHHH		63.1129967540
57PhosphorylationLHHTERLYQNAESNN
HHHHHHHHHHHHHCC		13.1227811184
62PhosphorylationRLYQNAESNNQELRT
HHHHHHHHCCHHHHH		38.3727811184
135PhosphorylationQDQAIETSILNSKDH
HHHHHHHHHHCCCCC		16.5828555341
169 (in isoform 3)Phosphorylation-35.7525072903
169PhosphorylationRQVDHFASNSQEPAS
EECCCCCCCCCCCHH		35.7527080861
171 (in isoform 3)Phosphorylation-33.1625072903
171PhosphorylationVDHFASNSQEPASAL
CCCCCCCCCCCHHHH		33.1628464451
176PhosphorylationSNSQEPASALATEDT
CCCCCCHHHHCCCCC		34.2327080861
180PhosphorylationEPASALATEDTSLEG
CCHHHHCCCCCCCCC		34.9327080861
184PhosphorylationALATEDTSLEGSSLA
HHCCCCCCCCCCHHH		36.4225627689
263PhosphorylationVDLQPYPTSSTKQSK
CCCCCCCCCCCCHHH		29.4821712546
264PhosphorylationDLQPYPTSSTKQSKD
CCCCCCCCCCCHHHC		31.3525159151
265PhosphorylationLQPYPTSSTKQSKDK
CCCCCCCCCCHHHCH		41.9428555341
266PhosphorylationQPYPTSSTKQSKDKK
CCCCCCCCCHHHCHH		32.6325627689
286PhosphorylationKDPDSSATNEEKDLN
CCCCCCCCHHHHHCC		45.1427134283
301PhosphorylationSEDQKAFSVEHTSCN
HHHHHHHCCCCCCCC		31.3023401153
305PhosphorylationKAFSVEHTSCNEEEN
HHHCCCCCCCCHHHH		22.8230624053
306PhosphorylationAFSVEHTSCNEEENF
HHCCCCCCCCHHHHH		19.4930576142
327AcetylationAKIGIHHKNSPPKVT
EEEECCCCCCCCCEE		44.9825953088
329PhosphorylationIGIHHKNSPPKVTVP
EECCCCCCCCCEECC		47.5930266825
334PhosphorylationKNSPPKVTVPTSGNT
CCCCCCEECCCCCCC		27.2223663014
337PhosphorylationPPKVTVPTSGNTIES
CCCEECCCCCCCCCC		44.9523663014
338PhosphorylationPKVTVPTSGNTIESP
CCEECCCCCCCCCCC		24.7923663014
341PhosphorylationTVPTSGNTIESPLHE
ECCCCCCCCCCCCCC		29.6429255136
344PhosphorylationTSGNTIESPLHENIS
CCCCCCCCCCCCCCC		28.9830266825
351PhosphorylationSPLHENISNSTSFKD
CCCCCCCCCCCCCCC		35.9923663014
353PhosphorylationLHENISNSTSFKDEK
CCCCCCCCCCCCCCC		20.7323403867
354PhosphorylationHENISNSTSFKDEKI
CCCCCCCCCCCCCCE		42.2923663014
355PhosphorylationENISNSTSFKDEKIM
CCCCCCCCCCCCCEE		30.0723403867
357AcetylationISNSTSFKDEKIMET
CCCCCCCCCCCEECC		65.8226051181
445PhosphorylationREKDMEHTLRIPEVG
CCCCCCCEECCCCCC		12.3946160373
454PhosphorylationRIPEVGVSKFHAEIY
CCCCCCCCEEEEEEE		24.5529396449
543PhosphorylationRLDKKDESFVGPTLS
ECCCCCCCCCCCCCC		35.0525159151
5602-HydroxyisobutyrylationEKELERRKELKKIRV
HHHHHHHHHHHHHHH		73.88-
574PhosphorylationVKYGLQNTEYEDEKT
HHHCCCCCCCCCHHH		27.3028796482
576PhosphorylationYGLQNTEYEDEKTLK
HCCCCCCCCCHHHHC		27.0028796482
615PhosphorylationDAPASVHSEITDSNK
CCCCCCCCCCCCCHH		28.6546160367
620PhosphorylationVHSEITDSNKGRKML
CCCCCCCCHHHHHHH		31.6225159151
622AcetylationSEITDSNKGRKMLEK
CCCCCCHHHHHHHHH		65.1323236377
647PhosphorylationKDGGGMKTPIQLQLR
CCCCCCCCCEEEEEH		19.4121815630
662PhosphorylationRTHAGLGTGKPSSFE
HHCCCCCCCCCCCHH		47.2628555341
664AcetylationHAGLGTGKPSSFEDV
CCCCCCCCCCCHHHH		41.3819608861
666PhosphorylationGLGTGKPSSFEDVHL
CCCCCCCCCHHHHHH		51.6629214152
667PhosphorylationLGTGKPSSFEDVHLL
CCCCCCCCHHHHHHH		40.9829214152
679AcetylationHLLQNKNKKNWDKAR
HHHCCCCCCCHHHHH		49.4420167786
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 AGGF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGGF1_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 AGGF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RU1C_HUMANSNRPCphysical
22365833
CHERP_HUMANCHERPphysical
22365833
AGGF1_HUMANAGGF1physical
22365833
TOE1_HUMANTOE1physical
22365833
AGGF1_HUMANAGGF1physical
25416956
MB213_HUMANMAB21L3physical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
149000Klippel-Trenaunay syndrome (KTS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AGGF1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-7 AND SER-11, AND MASS SPECTROMETRY.
"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-664, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-7 AND SER-11, AND MASS SPECTROMETRY.

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