MFAP1_HUMAN - dbPTM
MFAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MFAP1_HUMAN
UniProt AC P55081
Protein Name Microfibrillar-associated protein 1 {ECO:0000312|HGNC:HGNC:7032}
Gene Name MFAP1 {ECO:0000312|HGNC:HGNC:7032}
Organism Homo sapiens (Human).
Sequence Length 439
Subcellular Localization Nucleus .
Protein Description May be required for pre-mRNA splicing..
Protein Sequence MSVPSALMKQPPIQSTAGAVPVRNEKGEISMEKVKVKRYVSGKRPDYAPMESSDEEDEEFQFIKKAKEQEAEPEEQEEDSSSDPRLRRLQNRISEDVEERLARHRKIVEPEVVGESDSEVEGDAWRMEREDSSEEEEEEIDDEEIERRRGMMRQRAQERKNEEMEVMEVEDEGRSGEESESESEYEEYTDSEDEMEPRLKPVFIRKKDRVTVQEREAEALKQKELEQEAKRMAEERRKYTLKIVEEETKKELEENKRSLAALDALNTDDENDEEEYEAWKVRELKRIKRDREDREALEKEKAEIERMRNLTEEERRAELRANGKVITNKAVKGKYKFLQKYYHRGAFFMDEDEEVYKRDFSAPTLEDHFNKTILPKVMQVKNFGRSGRTKYTHLVDQDTTSFDSAWGQESAQNTKFFKQKAAGVRDVFERPSAKKRKTT
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------MSVPSALMK
------CCCCHHHHC		42.6122223895
2Phosphorylation------MSVPSALMK
------CCCCHHHHC		42.6128348404
5Phosphorylation---MSVPSALMKQPP
---CCCCHHHHCCCC		31.7025599653
15PhosphorylationMKQPPIQSTAGAVPV
HCCCCCCCCCCCEEC		22.4226074081
16PhosphorylationKQPPIQSTAGAVPVR
CCCCCCCCCCCEECC		16.8525599653
26AcetylationAVPVRNEKGEISMEK
CEECCCCCCCCCEEE		66.4525953088
30PhosphorylationRNEKGEISMEKVKVK
CCCCCCCCEEEEEEE		19.3121712546
33AcetylationKGEISMEKVKVKRYV
CCCCCEEEEEEEECC		38.4226051181
35UbiquitinationEISMEKVKVKRYVSG
CCCEEEEEEEECCCC		53.7824816145
39PhosphorylationEKVKVKRYVSGKRPD
EEEEEEECCCCCCCC		8.0226074081
41PhosphorylationVKVKRYVSGKRPDYA
EEEEECCCCCCCCCC		29.6626074081
43AcetylationVKRYVSGKRPDYAPM
EEECCCCCCCCCCCC		53.9319823569
47PhosphorylationVSGKRPDYAPMESSD
CCCCCCCCCCCCCCC		18.4530266825
52PhosphorylationPDYAPMESSDEEDEE
CCCCCCCCCCCCCHH		36.5226846344
53PhosphorylationDYAPMESSDEEDEEF
CCCCCCCCCCCCHHH		35.4226846344
65AcetylationEEFQFIKKAKEQEAE
HHHHHHHHHHHCCCC		60.9319823579
67AcetylationFQFIKKAKEQEAEPE
HHHHHHHHHCCCCHH		69.6626051181
67SumoylationFQFIKKAKEQEAEPE
HHHHHHHHHCCCCHH		69.6628112733
80PhosphorylationPEEQEEDSSSDPRLR
HHHHHCCCCCCHHHH		34.7125159151
81PhosphorylationEEQEEDSSSDPRLRR
HHHHCCCCCCHHHHH		51.5925159151
82PhosphorylationEQEEDSSSDPRLRRL
HHHCCCCCCHHHHHH		56.4323401153
94PhosphorylationRRLQNRISEDVEERL
HHHHHHHCHHHHHHH		25.2225159151
116PhosphorylationEPEVVGESDSEVEGD
CCCCCCCCCCCCCCC		40.2719664994
118PhosphorylationEVVGESDSEVEGDAW
CCCCCCCCCCCCCCC		53.4722167270
132PhosphorylationWRMEREDSSEEEEEE
CCCCCCCCCHHHHHH		34.5922167270
133PhosphorylationRMEREDSSEEEEEEI
CCCCCCCCHHHHHHC		62.4422167270
160UbiquitinationRQRAQERKNEEMEVM
HHHHHHHHHHHCCEE		68.8824816145
175PhosphorylationEVEDEGRSGEESESE
EEECCCCCCCCCCCH		62.5018452278
179PhosphorylationEGRSGEESESESEYE
CCCCCCCCCCHHHHH		41.9618452278
183PhosphorylationGEESESESEYEEYTD
CCCCCCHHHHHHCCC		55.5518452278
200AcetylationDEMEPRLKPVFIRKK
CCCCCCCCCEEEECC		40.1823749302
200UbiquitinationDEMEPRLKPVFIRKK
CCCCCCCCCEEEECC		40.1827667366
221UbiquitinationEREAEALKQKELEQE
HHHHHHHHHHHHHHH		67.3924816145
230UbiquitinationKELEQEAKRMAEERR
HHHHHHHHHHHHHHH		41.79-
230AcetylationKELEQEAKRMAEERR
HHHHHHHHHHHHHHH		41.7925953088
239PhosphorylationMAEERRKYTLKIVEE
HHHHHHHHHHHHHHH		18.5926074081
240PhosphorylationAEERRKYTLKIVEEE
HHHHHHHHHHHHHHH		25.3026074081
242UbiquitinationERRKYTLKIVEEETK
HHHHHHHHHHHHHHH		36.5829967540
248PhosphorylationLKIVEEETKKELEEN
HHHHHHHHHHHHHHH		51.1726074081
249SumoylationKIVEEETKKELEENK
HHHHHHHHHHHHHHH		47.7528112733
249SumoylationKIVEEETKKELEENK
HHHHHHHHHHHHHHH		47.75-
256UbiquitinationKKELEENKRSLAALD
HHHHHHHHHHHHHHH		46.7929967540
256AcetylationKKELEENKRSLAALD
HHHHHHHHHHHHHHH		46.7926051181
258PhosphorylationELEENKRSLAALDAL
HHHHHHHHHHHHHHC		24.7823927012
267PhosphorylationAALDALNTDDENDEE
HHHHHCCCCCCCCHH		45.7519664994
276PhosphorylationDENDEEEYEAWKVRE
CCCCHHHHHHHHHHH		17.7723927012
280UbiquitinationEEEYEAWKVRELKRI
HHHHHHHHHHHHHHH		38.16-
299UbiquitinationEDREALEKEKAEIER
HHHHHHHHHHHHHHH		66.4224816145
324UbiquitinationAELRANGKVITNKAV
HHHHHCCEEECCHHH		30.2129967540
329UbiquitinationNGKVITNKAVKGKYK
CCEEECCHHHCCHHH		46.0029967540
329AcetylationNGKVITNKAVKGKYK
CCEEECCHHHCCHHH		46.0025953088
336SumoylationKAVKGKYKFLQKYYH
HHHCCHHHHHHHHHH		42.98-
336SumoylationKAVKGKYKFLQKYYH
HHHCCHHHHHHHHHH		42.98-
340AcetylationGKYKFLQKYYHRGAF
CHHHHHHHHHHCCCE		50.3419608861
340UbiquitinationGKYKFLQKYYHRGAF
CHHHHHHHHHHCCCE		50.3419608861
356PhosphorylationMDEDEEVYKRDFSAP
CCCCHHHHCCCCCCC		12.0028674419
357SumoylationDEDEEVYKRDFSAPT
CCCHHHHCCCCCCCC		51.1428112733
357UbiquitinationDEDEEVYKRDFSAPT
CCCHHHHCCCCCCCC		51.1421906983
361PhosphorylationEVYKRDFSAPTLEDH
HHHCCCCCCCCHHHH		37.3125159151
364PhosphorylationKRDFSAPTLEDHFNK
CCCCCCCCHHHHCCC		42.3623186163
371SumoylationTLEDHFNKTILPKVM
CHHHHCCCCHHHHHH		35.6828112733
371UbiquitinationTLEDHFNKTILPKVM
CHHHHCCCCHHHHHH		35.6821906983
376UbiquitinationFNKTILPKVMQVKNF
CCCCHHHHHHHCCCC		47.0622817900
381SumoylationLPKVMQVKNFGRSGR
HHHHHHCCCCCCCCC		29.66-
381UbiquitinationLPKVMQVKNFGRSGR
HHHHHHCCCCCCCCC		29.6621906983
3812-HydroxyisobutyrylationLPKVMQVKNFGRSGR
HHHHHHCCCCCCCCC		29.66-
381SumoylationLPKVMQVKNFGRSGR
HHHHHHCCCCCCCCC		29.6628112733
386PhosphorylationQVKNFGRSGRTKYTH
HCCCCCCCCCCCEEE		32.76-
390UbiquitinationFGRSGRTKYTHLVDQ
CCCCCCCCEEEEECC		46.9522817900
390AcetylationFGRSGRTKYTHLVDQ
CCCCCCCCEEEEECC		46.9526051181
392PhosphorylationRSGRTKYTHLVDQDT
CCCCCCEEEEECCCC		15.4121712546
399PhosphorylationTHLVDQDTTSFDSAW
EEEECCCCCCCCCCC		20.7827251275
400PhosphorylationHLVDQDTTSFDSAWG
EEECCCCCCCCCCCC		35.3727251275
401PhosphorylationLVDQDTTSFDSAWGQ
EECCCCCCCCCCCCC		29.2028985074
404PhosphorylationQDTTSFDSAWGQESA
CCCCCCCCCCCCHHH		24.7427251275
415UbiquitinationQESAQNTKFFKQKAA
CHHHHHHHHHHHHHH		57.2521906983
415SumoylationQESAQNTKFFKQKAA
CHHHHHHHHHHHHHH		57.2528112733
418SumoylationAQNTKFFKQKAAGVR
HHHHHHHHHHHHCCH		54.7628112733
418UbiquitinationAQNTKFFKQKAAGVR
HHHHHHHHHHHHCCH		54.7622817900
420UbiquitinationNTKFFKQKAAGVRDV
HHHHHHHHHHCCHHH		40.5722817900
432PhosphorylationRDVFERPSAKKRKTT
HHHHCCCCCCCCCCC		59.9623401153
434AcetylationVFERPSAKKRKTT--
HHCCCCCCCCCCC--		58.4025953088
434UbiquitinationVFERPSAKKRKTT--
HHCCCCCCCCCCC--		58.4024816145
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
116SPhosphorylationKinaseCDC7O00311
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MFAP1_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 MFAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SR140_HUMANU2SURPphysical
22939629
RL37_HUMANRPL37physical
22939629
PR40B_HUMANPRPF40Bphysical
22939629
U2AF1_HUMANU2AF1physical
22365833
PRPF3_HUMANPRPF3physical
22365833
SNUT1_HUMANSART1physical
22365833
SNW1_HUMANSNW1physical
22365833
SNIP1_HUMANSNIP1physical
22365833
RED_HUMANIKphysical
22365833
SMU1_HUMANSMU1physical
22365833
HSPB1_HUMANHSPB1physical
22365833
DHX8_HUMANDHX8physical
22365833
PRP16_HUMANDHX38physical
22365833
F10C1_HUMANFRA10AC1physical
22365833
VPS52_HUMANVPS52physical
25416956
TAD2A_HUMANTADA2Aphysical
25416956
ZBT14_HUMANZBTB14physical
25416956
COIL_HUMANCOILphysical
25416956
MD1L1_HUMANMAD1L1physical
25416956
STX11_HUMANSTX11physical
25416956
FXR2_HUMANFXR2physical
25416956
NDC80_HUMANNDC80physical
25416956
TRIM1_HUMANMID2physical
25416956
MTUS2_HUMANMTUS2physical
25416956
LDOC1_HUMANLDOC1physical
25416956
AMOL2_HUMANAMOTL2physical
25416956
CEP55_HUMANCEP55physical
25416956
CDA7L_HUMANCDCA7Lphysical
25416956
ZF64A_HUMANZFP64physical
25416956
ZF64B_HUMANZFP64physical
25416956
TRI54_HUMANTRIM54physical
25416956
ZN398_HUMANZNF398physical
25416956
CARD9_HUMANCARD9physical
25416956
HMBX1_HUMANHMBOX1physical
25416956
KTBL1_HUMANKATNBL1physical
25416956
GKAP1_HUMANGKAP1physical
25416956
CEP70_HUMANCEP70physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
K1C40_HUMANKRT40physical
25416956
MIPO1_HUMANMIPOL1physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
BEND7_HUMANBEND7physical
25416956
CCD57_HUMANCCDC57physical
25416956
CE57L_HUMANCEP57L1physical
25416956
TRI42_HUMANTRIM42physical
25416956
ZBT8A_HUMANZBTB8Aphysical
25416956
PR38A_HUMANPRPF38Aphysical
26186194
PR38A_HUMANPRPF38Aphysical
28514442
EAF1_HUMANEAF1physical
27173435
DPOD1_HUMANPOLD1physical
27173435
NAF1_HUMANNAF1physical
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 MFAP1_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-340, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-118;SER-132; SER-133 AND THR-267, AND MASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47; SER-52; SER-53;SER-116; SER-118 AND THR-267, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118 ANDTHR-267, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-52; SER-53;SER-116; SER-118; SER-132; SER-133; THR-267 AND SER-432, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116;SER-118 AND THR-267, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-118, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND MASSSPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118 ANDTHR-267, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-116 AND THR-267,AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116;SER-118; SER-132; SER-133 AND THR-267, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118; SER-132;SER-133 AND THR-267, AND MASS SPECTROMETRY.

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