LAMA2_MOUSE - dbPTM
LAMA2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAMA2_MOUSE
UniProt AC Q60675
Protein Name Laminin subunit alpha-2
Gene Name Lama2
Organism Mus musculus (Mouse).
Sequence Length 3118
Subcellular Localization Secreted, extracellular space, extracellular matrix, basement membrane. Major component.
Protein Description Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components..
Protein Sequence MPAATAGILLLLLLGTLEGSQTQRRQSQAHQQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQPVRNPQCRICNQNSSNPYQRHPITNAIDGKNTWWQSPSIKNGVEYHYVTITLDLQQVFQIAYVIVKAANSPRPGNWILERSLDDVEYKPWQYHAVTDTECLTLYNIYPRTGPPSYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDPSPELLEFTSARYIRLRFQRIRTLNADLMMFAHKDPREIDPIVTRRYYYSVKDISVGGMCICYGHARACPLDPATNKSRCECEHNTCGESCDRCCPGFHQKPWRAGTFLTKSECEACNCHGKAEECYYDETVASRNLSLNIHGKYIGGGVCINCTHNTAGINCETCVDGFFRPKGVSPNYPRPCQPCHCDPTGSLSEVCVKDEKYAQRGLKPGSCHCKTGFGGVNCDRCVRGYHGYPDCQPCNCSGLGSTNEDPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQKGCEECFCSGVSNRCQSSYWTYGNIQDMRGWYLTDLSGRIRMAPQLDNPDSPQQISISNSEARKSLLDGYYWSAPPPYLGNRLPAVGGQLSFTISYDLEEEEDDTEKILQLMIIFEGNDLRISTAYKEVYLEPSEEHIEEVSLKEEAFTIHGTNLPVTRKDFMIVLTNLERVLMQITYNLGMDAIFRLSSVNLESAVPYPTDRRIATDVEVCQCPPGYSGSSCETCWPRHRRVNGTIFGGICEPCQCFAHAEACDDITGECLNCKDHTGGPYCNECLPGFYGDPTRGSPEDCQPCACPLNIPSNNFSPTCHLDRSLGLICDECPIGYTGPRCERCAEGYFGQPSIPGGSCQPCQCNDNLDYSIPGSCDSLSGSCLICKPGTTGRYCELCADGYFGDAVNAKNCQPCRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQLGRGCLPCNCNSFGSKSFDCEASGQCWCQPGVAGKKCDRCAHGYFNFQEGGCIACDCSHLGNNCDPKTGQCICPPNTTGEKCSECLPNTWGHSIVTGCKVCNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPLCTLCDCFLPGTDATTCDLETRKCSCSDQTGQCSCKVNVEGVHCDRCRPGKFGLDAKNPLGCSSCYCFGVTSQCSEAKGLIRTWVTLSDEQTILPLVDEALQHTTTKGIAFQKPEIVAKMDEVRQELHLEPFYWKLPQQFEGKKLMAYGGKLKYAIYFEARDETGFATYKPQVIIRGGTPTHARIITRHMAAPLIGQLTRHEIEMTEKEWKYYGDDPRISRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEPGHVLAGSPPAHLIERCDCPPGYSGLSCETCAPGFYRLRSEPGGRTPGPTLGTCVPCQCNGHSSQCDPETSVCQNCQHHTAGDFCERCALGYYGIVRGLPNDCQPCACPLISPSNNFSPSCVLEGLEDYRCTACPRGYEGQYCERCAPGYTGSPSSPGGSCQECECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWHAREGAECVFCGDECTGLLLGDLARLEQMTMNINLTGPLPAPYKILYGLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKIIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDCVRTYRPEIKKGSYNNIVVHVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGSISVRALDGPKASMVPSTYHSVSPPGYTILDVDANAMLFVGGLTGKIKKADAVRVITFTGCMGETYFDNKPIGLWNFREKEGDCKGCTVSPQVEDSEGTIQFDGEGYALVSRPIRWYPNISTVMFKFRTFSSSALLMYLATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNHNDGKWKAFTLSRIQKQANISIVDIDSNQEENVATSSSGNNFGLDLKADDKIYFGGLPTLRNLSMKARPEVNVKKYSGCLKDIEISRTPYNILSSPDYVGVTKGCSLENVYTVSFPKPGFVELAAVSIDVGTEINLSFSTRNESGIILLGSGGTLTPPRRKRRQTTQAYYAIFLNKGRLEVHLSSGTRTMRKIVIKPEPNLFHDGREHSVHVERTRGIFTVQIDEDRRHMQNLTEEQPIEVKKLFVGGAPPEFQPSPLRNIPAFQGCVWNLVINSIPMDFAQPIAFKNADIGRCTYQKPREDESEAVPAEVIVQPQPVPTPAFPFPAPTMVHGPCVAESEPALLTGSKQFGLSRNSHIAIAFDDTKVKNRLTIELEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTSTMIPTKINDGQWHKIKIVRVKQEGILYVDDASSQTISPKKADILDVVGILYVGGLPINYTTRRIGPVTYSLDGCVRNLHMEQAPVDLDQPTSSFHVGTCFANAESGTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTRPTGVLLGVSSQKMDGMGIEMIDEKLMFHVDNGAGRFTAIYDAGIPGHMCNGQWHKVTAKKIKNRLELVVDGNQVDAQSPNSASTSADTNDPVFVGGFPGGLNQFGLTTNIRFRGCIRSLKLTKGTGKPLEVNFAKALELRGVQPVSCPTT
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
51N-linked_GlycosylationSNALITTNATCGEKG
HCCEEECCCCCCCCC
25.30-
85N-linked_GlycosylationQCRICNQNSSNPYQR
CCCCCCCCCCCCCCC
33.15-
246PhosphorylationLRFQRIRTLNADLMM
HHHHHHHHCCCCEEH
23.22-
299N-linked_GlycosylationCPLDPATNKSRCECE
CCCCCCCCHHHCCCC
42.27-
359N-linked_GlycosylationDETVASRNLSLNIHG
CCCHHCCCEEEEEEC
31.33-
376N-linked_GlycosylationIGGGVCINCTHNTAG
ECCCEEEECCCCCCC
21.36-
395DimethylationTCVDGFFRPKGVSPN
CEECCCCCCCCCCCC
29.74-
395MethylationTCVDGFFRPKGVSPN
CEECCCCCCCCCCCC
29.7454540705
466N-linked_GlycosylationYPDCQPCNCSGLGST
CCCCCCCCCCCCCCC
29.67-
742N-linked_GlycosylationWPRHRRVNGTIFGGI
CCCCCCCCCEEECCC
39.83-
919N-linked_GlycosylationQPCRCNINGSFSEIC
CCCCCCCCCCHHHHE
27.14-
1031N-linked_GlycosylationGQCICPPNTTGEKCS
CCCCCCCCCCCCCHH
35.10-
1057N-linked_GlycosylationVTGCKVCNCSTVGSL
CCCCCCCCCCCHHHH
26.26-
1232AcetylationHLEPFYWKLPQQFEG
CCCHHCCCCCHHHCC
38.626567405
1245PhosphorylationEGKKLMAYGGKLKYA
CCEEEEEECCEEEEE
16.6727180971
1593N-linked_GlycosylationEQMTMNINLTGPLPA
HHCCCCCCCCCCCCC
26.92-
1610N-linked_GlycosylationKILYGLENTTQELKH
EEEEECCCHHHHHHH
54.17-
1651PhosphorylationNELLTRATKVTADGE
HHHHHHHEEECCCCH
23.8230635358
1654PhosphorylationLTRATKVTADGEQTG
HHHHEEECCCCHHCC
22.1630635358
1669PhosphorylationQDAERTNSRAESLEE
CCHHHHHHHHHHHHH
32.0521183079
1673PhosphorylationRTNSRAESLEEFIKG
HHHHHHHHHHHHHHH
39.8419060867
1696N-linked_GlycosylationNEKAVQLNETLGNQD
HHHHHHHHHHHCCCH
34.19-
1806N-linked_GlycosylationLSAANQKNMTILETK
HHHHHHHCCCHHHHH
24.06-
1897N-linked_GlycosylationESHAAQLNDSSAVLD
HHHHHHCCCCHHHHH
34.73-
1912N-linked_GlycosylationGILDEAKNISFNATA
HHHHHHHHCCCCHHH
42.03-
1916N-linked_GlycosylationEAKNISFNATAAFRA
HHHHCCCCHHHHHHH
29.59-
2013N-linked_GlycosylationSGLLGALNDTMDKLS
HHHHHHHHHHHHHHH
42.02-
2024N-linked_GlycosylationDKLSAITNDTAAKLQ
HHHHHHCCHHHHHHH
38.22-
2041N-linked_GlycosylationKEKAREANDTAKAVL
HHHHHHCHHHHHHHH
42.27-
2084AcetylationAVVKDPSKNKIIADA
CEECCCCCCEEEECC
68.5922902405
2084AcetylationAVVKDPSKNKIIADA
CEECCCCCCEEEECC
68.59-
2122N-linked_GlycosylationLEDNLKKNISEIKEL
HHHHHHHCHHHHHHH
41.24-
2236N-linked_GlycosylationEASRTGRNGSISVRA
EECCCCCCCCEEEEE
50.32-
2356N-linked_GlycosylationRPIRWYPNISTVMFK
CCEEECCCCCEEEEE
25.75-
2366PhosphorylationTVMFKFRTFSSSALL
EEEEEEECCCHHHHH
30.8821183079
2368PhosphorylationMFKFRTFSSSALLMY
EEEEECCCHHHHHHH
23.8330635358
2369PhosphorylationFKFRTFSSSALLMYL
EEEECCCHHHHHHHH
18.5530635358
2370PhosphorylationKFRTFSSSALLMYLA
EEECCCHHHHHHHHH
23.0330635358
2375PhosphorylationSSSALLMYLATRDLK
CHHHHHHHHHHCCHH
7.9921183079
2378PhosphorylationALLMYLATRDLKDFM
HHHHHHHHCCHHHHC
23.3230635358
2431N-linked_GlycosylationSRIQKQANISIVDID
HHHHHHCCEEEEECC
26.50-
2474N-linked_GlycosylationGGLPTLRNLSMKARP
CCHHHHCCCCCCCCC
39.31-
2547N-linked_GlycosylationIDVGTEINLSFSTRN
EECCCEEEEEEECCC
24.33-
2554N-linked_GlycosylationNLSFSTRNESGIILL
EEEEECCCCCCEEEE
48.12-
2556PhosphorylationSFSTRNESGIILLGS
EEECCCCCCEEEECC
38.5526026062
2563PhosphorylationSGIILLGSGGTLTPP
CCEEEECCCCCCCCC
33.7426026062
2566PhosphorylationILLGSGGTLTPPRRK
EEECCCCCCCCCCHH
30.8626026062
2568PhosphorylationLGSGGTLTPPRRKRR
ECCCCCCCCCCHHCC
30.9627149854
2608AcetylationTMRKIVIKPEPNLFH
EEEEEEECCCCCCCC
32.2222902405
2608AcetylationTMRKIVIKPEPNLFH
EEEEEEECCCCCCCC
32.22-
2644N-linked_GlycosylationEDRRHMQNLTEEQPI
CCHHHHHCCCCCCCC
48.61-
2845AcetylationINDGQWHKIKIVRVK
CCCCCCEEEEEEEEE
42.61-
2845AcetylationINDGQWHKIKIVRVK
CCCCCCEEEEEEEEE
42.6122902405
2863PhosphorylationILYVDDASSQTISPK
EEEEECCCCCCCCCC
29.9421454597
2864PhosphorylationLYVDDASSQTISPKK
EEEECCCCCCCCCCC
32.8221454597
2868PhosphorylationDASSQTISPKKADIL
CCCCCCCCCCCCCCC
33.7721454597
2889N-linked_GlycosylationYVGGLPINYTTRRIG
EECCCCCCCCCCCCC
26.59-
2947AcetylationFDGTGFAKAVGGFKV
ECCCCCHHCCCCEEE
37.32-
2947AcetylationFDGTGFAKAVGGFKV
ECCCCCHHCCCCEEE
37.3222902405
3023AcetylationMCNGQWHKVTAKKIK
CCCCCEEEEEHHHHC
30.10-
3023AcetylationMCNGQWHKVTAKKIK
CCCCCEEEEEHHHHC
30.1022902405
3095AcetylationKLTKGTGKPLEVNFA
EECCCCCCCEEEEEH
43.83-
3095AcetylationKLTKGTGKPLEVNFA
EECCCCCCCEEEEEH
43.8322902405
3103AcetylationPLEVNFAKALELRGV
CEEEEEHHHHHHCCC
45.48-
3103AcetylationPLEVNFAKALELRGV
CEEEEEHHHHHHCCC
45.4822902405

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 LAMA2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAMA2_MOUSE !!

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 LAMA2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LAMA2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAMA2_MOUSE

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Related Literatures of Post-Translational Modification

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