CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003872
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Laminin subunit gamma-1 
Protein Synonyms/Alias
 Laminin B2 chain; Laminin-1 subunit gamma; Laminin-10 subunit gamma; Laminin-11 subunit gamma; Laminin-2 subunit gamma; Laminin-3 subunit gamma; Laminin-4 subunit gamma; Laminin-6 subunit gamma; Laminin-7 subunit gamma; Laminin-8 subunit gamma; Laminin-9 subunit gamma; S-laminin subunit gamma; S-LAM gamma 
Gene Name
 LAMC1 
Gene Synonyms/Alias
 LAMB2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
188SCENTYSKANRGFIRubiquitination[1]
564RYFIAPAKFLGKQVLubiquitination[1]
622YPSETTVKYVFRLHEubiquitination[2]
1093LREAQDVKDVDQNLMubiquitination[2]
1303LEQLIDQKLKDYEDLubiquitination[2]
1371NDILNNLKDFDRRVNubiquitination[2]
1423AADATEAKNKAHEAEubiquitination[2]
1557KVSDLDRKVSDLENEubiquitination[2]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional 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. 
Sequence Annotation
 DOMAIN 46 285 Laminin N-terminal.
 DOMAIN 286 341 Laminin EGF-like 1.
 DOMAIN 342 397 Laminin EGF-like 2.
 DOMAIN 398 444 Laminin EGF-like 3.
 DOMAIN 445 494 Laminin EGF-like 4.
 DOMAIN 495 504 Laminin EGF-like 5; first part.
 DOMAIN 514 689 Laminin IV type A.
 DOMAIN 690 723 Laminin EGF-like 5; second part.
 DOMAIN 724 772 Laminin EGF-like 6.
 DOMAIN 773 827 Laminin EGF-like 7.
 DOMAIN 828 883 Laminin EGF-like 8.
 DOMAIN 884 934 Laminin EGF-like 9.
 DOMAIN 935 982 Laminin EGF-like 10.
 DOMAIN 983 1030 Laminin EGF-like 11.
 REGION 1030 1609 Domain II and I.
 MOD_RES 1493 1493 Phosphoserine.
 CARBOHYD 60 60 N-linked (GlcNAc...) (Potential).
 CARBOHYD 134 134 N-linked (GlcNAc...) (Potential).
 CARBOHYD 576 576 N-linked (GlcNAc...) (Potential).
 CARBOHYD 650 650 N-linked (GlcNAc...).
 CARBOHYD 1022 1022 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1107 1107 N-linked (GlcNAc...).
 CARBOHYD 1161 1161 N-linked (GlcNAc...).
 CARBOHYD 1175 1175 N-linked (GlcNAc...).
 CARBOHYD 1205 1205 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1223 1223 N-linked (GlcNAc...).
 CARBOHYD 1241 1241 N-linked (GlcNAc...).
 CARBOHYD 1380 1380 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1395 1395 N-linked (GlcNAc...).
 CARBOHYD 1439 1439 N-linked (GlcNAc...) (Potential).
 DISULFID 286 295 By similarity.
 DISULFID 288 305 By similarity.
 DISULFID 307 316 By similarity.
 DISULFID 319 339 By similarity.
 DISULFID 342 351 By similarity.
 DISULFID 344 367 By similarity.
 DISULFID 370 379 By similarity.
 DISULFID 382 395 By similarity.
 DISULFID 398 410 By similarity.
 DISULFID 400 416 By similarity.
 DISULFID 418 427 By similarity.
 DISULFID 430 442 By similarity.
 DISULFID 445 456 By similarity.
 DISULFID 447 463 By similarity.
 DISULFID 465 474 By similarity.
 DISULFID 477 492 By similarity.
 DISULFID 724 733 By similarity.
 DISULFID 726 740 By similarity.
 DISULFID 742 751 By similarity.
 DISULFID 754 770 By similarity.
 DISULFID 773 781 By similarity.
 DISULFID 775 792 By similarity.
 DISULFID 795 804 By similarity.
 DISULFID 807 825 By similarity.
 DISULFID 828 842 By similarity.
 DISULFID 830 849 By similarity.
 DISULFID 852 861 By similarity.
 DISULFID 864 881 By similarity.
 DISULFID 884 898 By similarity.
 DISULFID 886 905 By similarity.
 DISULFID 907 916 By similarity.
 DISULFID 919 932 By similarity.
 DISULFID 935 947 By similarity.
 DISULFID 937 954 By similarity.
 DISULFID 956 965 By similarity.
 DISULFID 968 980 By similarity.
 DISULFID 983 995 By similarity.
 DISULFID 985 1001 By similarity.
 DISULFID 1003 1012 By similarity.
 DISULFID 1015 1028 By similarity.
 DISULFID 1031 1031 Interchain (Probable).
 DISULFID 1034 1034 Interchain (Probable).
 DISULFID 1600 1600 Interchain (Probable).  
Keyword
 Basement membrane; Cell adhesion; Coiled coil; Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein; Laminin EGF-like domain; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1609 AA 
Protein Sequence
MRGSHRAAPA LRPRGRLWPV LAVLAAAAAA GCAQAAMDEC TDEGGRPQRC MPEFVNAAFN 60
VTVVATNTCG TPPEEYCVQT GVTGVTKSCH LCDAGQPHLQ HGAAFLTDYN NQADTTWWQS 120
QTMLAGVQYP SSINLTLHLG KAFDITYVRL KFHTSRPESF AIYKRTREDG PWIPYQYYSG 180
SCENTYSKAN RGFIRTGGDE QQALCTDEFS DISPLTGGNV AFSTLEGRPS AYNFDNSPVL 240
QEWVTATDIR VTLNRLNTFG DEVFNDPKVL KSYYYAISDF AVGGRCKCNG HASECMKNEF 300
DKLVCNCKHN TYGVDCEKCL PFFNDRPWRR ATAESASECL PCDCNGRSQE CYFDPELYRS 360
TGHGGHCTNC QDNTDGAHCE RCRENFFRLG NNEACSSCHC SPVGSLSTQC DSYGRCSCKP 420
GVMGDKCDRC QPGFHSLTEA GCRPCSCDPS GSIDECNIET GRCVCKDNVE GFNCERCKPG 480
FFNLESSNPR GCTPCFCFGH SSVCTNAVGY SVYSISSTFQ IDEDGWRAEQ RDGSEASLEW 540
SSERQDIAVI SDSYFPRYFI APAKFLGKQV LSYGQNLSFS FRVDRRDTRL SAEDLVLEGA 600
GLRVSVPLIA QGNSYPSETT VKYVFRLHEA TDYPWRPALT PFEFQKLLNN LTSIKIRGTY 660
SERSAGYLDD VTLASARPGP GVPATWVESC TCPVGYGGQF CEMCLSGYRR ETPNLGPYSP 720
CVLCACNGHS ETCDPETGVC NCRDNTAGPH CEKCSDGYYG DSTAGTSSDC QPCPCPGGSS 780
CAVVPKTKEV VCTNCPTGTT GKRCELCDDG YFGDPLGRNG PVRLCRLCQC SDNIDPNAVG 840
NCNRLTGECL KCIYNTAGFY CDRCKDGFFG NPLAPNPADK CKACNCNLYG TMKQQSSCNP 900
VTGQCECLPH VTGQDCGACD PGFYNLQSGQ GCERCDCHAL GSTNGQCDIR TGQCECQPGI 960
TGQHCERCEV NHFGFGPEGC KPCDCHPEGS LSLQCKDDGR CECREGFVGN RCDQCEENYF 1020
YNRSWPGCQE CPACYRLVKD KVADHRVKLQ ELESLIANLG TGDEMVTDQA FEDRLKEAER 1080
EVMDLLREAQ DVKDVDQNLM DRLQRVNNTL SSQISRLQNI RNTIEETGNL AEQARAHVEN 1140
TERLIEIASR ELEKAKVAAA NVSVTQPEST GDPNNMTLLA EEARKLAERH KQEADDIVRV 1200
AKTANDTSTE AYNLLLRTLA GENQTAFEIE ELNRKYEQAK NISQDLEKQA ARVHEEAKRA 1260
GDKAVEIYAS VAQLSPLDSE TLENEANNIK MEAENLEQLI DQKLKDYEDL REDMRGKELE 1320
VKNLLEKGKT EQQTADQLLA RADAAKALAE EAAKKGRDTL QEANDILNNL KDFDRRVNDN 1380
KTAAEEALRK IPAINQTITE ANEKTREAQQ ALGSAAADAT EAKNKAHEAE RIASAVQKNA 1440
TSTKAEAERT FAEVTDLDNE VNNMLKQLQE AEKELKRKQD DADQDMMMAG MASQAAQEAE 1500
INARKAKNSV TSLLSIINDL LEQLGQLDTV DLNKLNEIEG TLNKAKDEMK VSDLDRKVSD 1560
LENEAKKQEA AIMDYNRDIE EIMKDIRNLE DIRKTLPSGC FNTPSIEKP 1609 
Gene Ontology
 GO:0005615; C:extracellular space; NAS:UniProtKB.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0005606; C:laminin-1 complex; NAS:UniProtKB.
 GO:0043259; C:laminin-10 complex; TAS:BHF-UCL.
 GO:0043260; C:laminin-11 complex; TAS:BHF-UCL.
 GO:0005201; F:extracellular matrix structural constituent; IMP:HGNC.
 GO:0043208; F:glycosphingolipid binding; IEA:Compara.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0016477; P:cell migration; IMP:HGNC.
 GO:0007492; P:endoderm development; TAS:ProtInc.
 GO:0022617; P:extracellular matrix disassembly; IMP:HGNC.
 GO:0031581; P:hemidesmosome assembly; IMP:HGNC.
 GO:0050679; P:positive regulation of epithelial cell proliferation; TAS:HGNC.
 GO:0006461; P:protein complex assembly; IDA:HGNC.
 GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:BHF-UCL. 
Interpro
 IPR013032; EGF-like_CS.
 IPR002049; EGF_laminin.
 IPR008979; Galactose-bd-like.
 IPR018031; Laminin_B_subgr.
 IPR000034; Laminin_B_type_IV.
 IPR008211; Laminin_N. 
Pfam
 PF00052; Laminin_B
 PF00053; Laminin_EGF
 PF00055; Laminin_N 
SMART
 SM00180; EGF_Lam
 SM00281; LamB
 SM00136; LamNT 
PROSITE
 PS00022; EGF_1
 PS01186; EGF_2
 PS01248; EGF_LAM_1
 PS50027; EGF_LAM_2
 PS51115; LAMININ_IVA
 PS51117; LAMININ_NTER 
PRINTS