MMRN1_HUMAN - dbPTM
MMRN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MMRN1_HUMAN
UniProt AC Q13201
Protein Name Multimerin-1
Gene Name MMRN1
Organism Homo sapiens (Human).
Sequence Length 1228
Subcellular Localization Secreted .
Protein Description Carrier protein for platelet (but not plasma) factor V/Va. Plays a role in the storage and stabilization of factor V in platelets. Upon release following platelet activation, may limit platelet and plasma factor Va-dependent thrombin generation. Ligand for integrin alpha-IIb/beta-3 and integrin alpha-V/beta-3 on activated platelets, and may function as an extracellular matrix or adhesive protein..
Protein Sequence MKGARLFVLLSSLWSGGIGLNNSKHSWTIPEDGNSQKTMPSASVPPNKIQSLQILPTTRVMSAEIATTPEARTSEDSLLKSTLPPSETSAPAEGVRNQTLTSTEKAEGVVKLQNLTLPTNASIKFNPGAESVVLSNSTLKFLQSFARKSNEQATSLNTVGGTGGIGGVGGTGGVGNRAPRETYLSRGDSSSSQRTDYQKSNFETTRGKNWCAYVHTRLSPTVILDNQVTYVPGGKGPCGWTGGSCPQRSQKISNPVYRMQHKIVTSLDWRCCPGYSGPKCQLRAQEQQSLIHTNQAESHTAVGRGVAEQQQQQGCGDPEVMQKMTDQVNYQAMKLTLLQKKIDNISLTVNDVRNTYSSLEGKVSEDKSREFQSLLKGLKSKSINVLIRDIVREQFKIFQNDMQETVAQLFKTVSSLSEDLESTRQIIQKVNESVVSIAAQQKFVLVQENRPTLTDIVELRNHIVNVRQEMTLTCEKPIKELEVKQTHLEGALEQEHSRSILYYESLNKTLSKLKEVHEQLLSTEQVSDQKNAPAAESVSNNVTEYMSTLHENIKKQSLMMLQMFEDLHIQESKINNLTVSLEMEKESLRGECEDMLSKCRNDFKFQLKDTEENLHVLNQTLAEVLFPMDNKMDKMSEQLNDLTYDMEILQPLLEQGASLRQTMTYEQPKEAIVIRKKIENLTSAVNSLNFIIKELTKRHNLLRNEVQGRDDALERRINEYALEMEDGLNKTMTIINNAIDFIQDNYALKETLSTIKDNSEIHHKCTSDMETILTFIPQFHRLNDSIQTLVNDNQRYNFVLQVAKTLAGIPRDEKLNQSNFQKMYQMFNETTSQVRKYQQNMSHLEEKLLLTTKISKNFETRLQDIESKVTQTLIPYYISVKKGSVVTNERDQALQLQVLNSRFKALEAKSIHLSINFFSLNKTLHEVLTMCHNASTSVSELNATIPKWIKHSLPDIQLLQKGLTEFVEPIIQIKTQAALSNLTCCIDRSLPGSLANVVKSQKQVKSLPKKINALKKPTVNLTTVLIGRTQRNTDNIIYPEEYSSCSRHPCQNGGTCINGRTSFTCACRHPFTGDNCTIKLVEENALAPDFSKGSYRYAPMVAFFASHTYGMTIPGPILFNNLDVNYGASYTPRTGKFRIPYLGVYVFKYTIESFSAHISGFLVVDGIDKLAFESENINSEIHCDRVLTGDALLELNYGQEVWLRLAKGTIPAKFPPVTTFSGYLLYRT
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
21N-linked_GlycosylationWSGGIGLNNSKHSWT
HHCCCCCCCCCCCEE		45.58UniProtKB CARBOHYD
26PhosphorylationGLNNSKHSWTIPEDG
CCCCCCCCEECCCCC		29.65-
28O-linked_GlycosylationNNSKHSWTIPEDGNS
CCCCCCEECCCCCCC		29.66OGP
28PhosphorylationNNSKHSWTIPEDGNS
CCCCCCEECCCCCCC		29.66-
38PhosphorylationEDGNSQKTMPSASVP
CCCCCCCCCCCCCCC		27.0320886841
73O-linked_GlycosylationATTPEARTSEDSLLK
CCCCCCCCCCCCHHH		43.44OGP
73PhosphorylationATTPEARTSEDSLLK
CCCCCCCCCCCCHHH		43.4428060719
74PhosphorylationTTPEARTSEDSLLKS
CCCCCCCCCCCHHHC		33.5828060719
77PhosphorylationEARTSEDSLLKSTLP
CCCCCCCCHHHCCCC		31.3924719451
97N-linked_GlycosylationAPAEGVRNQTLTSTE
CCCCCCCCCCCCCCC		36.46UniProtKB CARBOHYD
114N-linked_GlycosylationEGVVKLQNLTLPTNA
CCEEEEECCCCCCCC		45.4916335952
116PhosphorylationVVKLQNLTLPTNASI
EEEEECCCCCCCCEE		37.9423403867
119PhosphorylationLQNLTLPTNASIKFN
EECCCCCCCCEEEEC		46.6723403867
120N-linked_GlycosylationQNLTLPTNASIKFNP
ECCCCCCCCEEEECC		29.7416335952
122PhosphorylationLTLPTNASIKFNPGA
CCCCCCCEEEECCCC		28.5123403867
126N-linked_GlycosylationTNASIKFNPGAESVV
CCCEEEECCCCCEEE		29.1516263699
136N-linked_GlycosylationAESVVLSNSTLKFLQ
CCEEEECHHHHHHHH		34.5516335952
136N-linked_GlycosylationAESVVLSNSTLKFLQ
CCEEEECHHHHHHHH		34.5517623646
144PhosphorylationSTLKFLQSFARKSNE
HHHHHHHHHHHHCCC		24.03-
149PhosphorylationLQSFARKSNEQATSL
HHHHHHHCCCCCCCC		39.7927174698
154PhosphorylationRKSNEQATSLNTVGG
HHCCCCCCCCCCCCC		33.1827174698
154O-linked_GlycosylationRKSNEQATSLNTVGG
HHCCCCCCCCCCCCC		33.18OGP
155PhosphorylationKSNEQATSLNTVGGT
HCCCCCCCCCCCCCC		23.7227174698
158PhosphorylationEQATSLNTVGGTGGI
CCCCCCCCCCCCCCC		26.3127174698
158O-linked_GlycosylationEQATSLNTVGGTGGI
CCCCCCCCCCCCCCC		26.31OGP
162PhosphorylationSLNTVGGTGGIGGVG
CCCCCCCCCCCCCCC		26.7227174698
171PhosphorylationGIGGVGGTGGVGNRA
CCCCCCCCCCCCCCC		25.4927174698
189PhosphorylationTYLSRGDSSSSQRTD
EECCCCCCCCCCCCC		34.64-
265PhosphorylationRMQHKIVTSLDWRCC
HHCCEEECCCCCCCC		27.35-
275PhosphorylationDWRCCPGYSGPKCQL
CCCCCCCCCCCCCCC		8.80-
276PhosphorylationWRCCPGYSGPKCQLR
CCCCCCCCCCCCCCC		55.31-
289PhosphorylationLRAQEQQSLIHTNQA
CCHHHHHHHCCCCCC		29.0528270605
293PhosphorylationEQQSLIHTNQAESHT
HHHHHCCCCCCHHHC		23.2528270605
298PhosphorylationIHTNQAESHTAVGRG
CCCCCCHHHCCCCCH		29.2028270605
344N-linked_GlycosylationLLQKKIDNISLTVND
HHHHHHCCEEEEHHH		29.2616263699
358PhosphorylationDVRNTYSSLEGKVSE
HHHHHHHHHCCCCCC		21.7424501219
368PhosphorylationGKVSEDKSREFQSLL
CCCCCHHHHHHHHHH		49.7323403867
373PhosphorylationDKSREFQSLLKGLKS
HHHHHHHHHHHHHHH		40.7824719451
382PhosphorylationLKGLKSKSINVLIRD
HHHHHHCCHHHHHHH		26.8728270605
417PhosphorylationFKTVSSLSEDLESTR
HHHHHHHCHHHHHHH		30.8929507054
422PhosphorylationSLSEDLESTRQIIQK
HHCHHHHHHHHHHHH		35.8718452278
431N-linked_GlycosylationRQIIQKVNESVVSIA
HHHHHHHHHHHHHHH		42.7516263699
507N-linked_GlycosylationILYYESLNKTLSKLK
HHHHHHHHHHHHHHH		44.5416263699
541N-linked_GlycosylationAAESVSNNVTEYMST
CHHHHHHHHHHHHHH		34.28UniProtKB CARBOHYD
576N-linked_GlycosylationIQESKINNLTVSLEM
CCHHHHCCEEEEEEH		40.3317660510
618N-linked_GlycosylationEENLHVLNQTLAEVL
HHHHHHHHHHHHHHH		31.5316335952
669AcetylationTMTYEQPKEAIVIRK
CCCCCCCCEEEEEHH		60.5219413330
680N-linked_GlycosylationVIRKKIENLTSAVNS
EEHHHHHHHHHHHHH		52.68UniProtKB CARBOHYD
687PhosphorylationNLTSAVNSLNFIIKE
HHHHHHHHHHHHHHH		20.3524719451
729N-linked_GlycosylationLEMEDGLNKTMTIIN
HHCCCCCCHHHHHHH		43.1917660510
783N-linked_GlycosylationIPQFHRLNDSIQTLV
HHHHHHCCHHHHHHC		40.7216263699
816N-linked_GlycosylationIPRDEKLNQSNFQKM
CCCCHHHCHHHHHHH		55.0617660510
828N-linked_GlycosylationQKMYQMFNETTSQVR
HHHHHHHHHHHHHHH		40.1216263699
837PhosphorylationTTSQVRKYQQNMSHL
HHHHHHHHHHHHHHH		12.5529632367
840N-linked_GlycosylationQVRKYQQNMSHLEEK
HHHHHHHHHHHHHHH		20.5616263699
842PhosphorylationRKYQQNMSHLEEKLL
HHHHHHHHHHHHHHH		32.2526552605
851PhosphorylationLEEKLLLTTKISKNF
HHHHHHHHHHHHCCH		26.4729396449
852PhosphorylationEEKLLLTTKISKNFE
HHHHHHHHHHHCCHH		26.7529396449
860PhosphorylationKISKNFETRLQDIES
HHHCCHHHHHHHHHH		32.32-
870PhosphorylationQDIESKVTQTLIPYY
HHHHHHHHHHHHCEE		21.4123607784
872PhosphorylationIESKVTQTLIPYYIS
HHHHHHHHHHCEEEE		19.7923607784
876PhosphorylationVTQTLIPYYISVKKG
HHHHHHCEEEEEECC		13.3623607784
877PhosphorylationTQTLIPYYISVKKGS
HHHHHCEEEEEECCC		4.9523607784
879PhosphorylationTLIPYYISVKKGSVV
HHHCEEEEEECCCEE		16.2623607784
884PhosphorylationYISVKKGSVVTNERD
EEEEECCCEECCCHH		23.4623607784
887PhosphorylationVKKGSVVTNERDQAL
EECCCEECCCHHHHH		29.2523607784
901PhosphorylationLQLQVLNSRFKALEA
HHHHHHHHHHHHHHH		34.63-
910PhosphorylationFKALEAKSIHLSINF
HHHHHHHEEEEEEEE		23.4529083192
914PhosphorylationEAKSIHLSINFFSLN
HHHEEEEEEEEHHHC		11.0029083192
921N-linked_GlycosylationSINFFSLNKTLHEVL
EEEEHHHCCHHHHHH		33.78UniProtKB CARBOHYD
933N-linked_GlycosylationEVLTMCHNASTSVSE
HHHHHHHCCCCCHHH		30.56UniProtKB CARBOHYD
942N-linked_GlycosylationSTSVSELNATIPKWI
CCCHHHHHCCCCHHH		30.8716263699
944PhosphorylationSVSELNATIPKWIKH
CHHHHHCCCCHHHHH		36.42-
981N-linked_GlycosylationKTQAALSNLTCCIDR
CHHHHHHCCEEEECC		39.9717660510
989PhosphorylationLTCCIDRSLPGSLAN
CEEEECCCCCCHHHH		34.8622210691
993PhosphorylationIDRSLPGSLANVVKS
ECCCCCCHHHHHHHC		23.5122210691
1018PhosphorylationINALKKPTVNLTTVL
HHHCCCCCCCCEEEE		30.7927135362
1020N-linked_GlycosylationALKKPTVNLTTVLIG
HCCCCCCCCEEEEEC		33.8616263699
1022PhosphorylationKKPTVNLTTVLIGRT
CCCCCCCEEEEECCC		15.0627135362
1023PhosphorylationKPTVNLTTVLIGRTQ
CCCCCCEEEEECCCC		19.2427135362
1075N-linked_GlycosylationRHPFTGDNCTIKLVE
CCCCCCCCCEEEEEE		26.61UniProtKB CARBOHYD
1218PhosphorylationPAKFPPVTTFSGYLL
CCCCCCCEEEEEEEE		28.09-
1219PhosphorylationAKFPPVTTFSGYLLY
CCCCCCEEEEEEEEE		18.94-
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 MMRN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MMRN1_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 MMRN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CYTM_HUMANCST6physical
26186194
RNAS7_HUMANRNASE7physical
26186194
FA5_HUMANF5physical
26186194
PPAP_HUMANACPPphysical
26186194
CATH_HUMANCTSHphysical
26186194
CDSN_HUMANCDSNphysical
26186194
S10A7_HUMANS100A7physical
26186194
ECM1_HUMANECM1physical
26186194
CATL2_HUMANCTSVphysical
26186194
APOE_HUMANAPOEphysical
26186194
KPRP_HUMANKPRPphysical
26186194
FA5_HUMANF5physical
28514442
APOE_HUMANAPOEphysical
28514442
PPAP_HUMANACPPphysical
28514442
ECM1_HUMANECM1physical
28514442
RNAS7_HUMANRNASE7physical
28514442
CATH_HUMANCTSHphysical
28514442
IGSF8_HUMANIGSF8physical
28514442
CATL2_HUMANCTSVphysical
28514442
CYTM_HUMANCST6physical
28514442
KPRP_HUMANKPRPphysical
28514442
CDSN_HUMANCDSNphysical
28514442
SPB4_HUMANSERPINB4physical
28514442
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 MMRN1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344; ASN-729; ASN-942 ANDASN-1020, AND MASS SPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-114, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-114; ASN-120; ASN-136;ASN-618 AND ASN-729, AND MASS SPECTROMETRY.

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