CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005265
UniProt Accession
Genbank Protein ID
 Z26653; U66796; U66733; U66734; U66735; U66736; U66737; U66738; U66739; U66740; U66741; U66742; U66743; U66745; U66746; U66747; U66748; U66749; U66750; U66751; U66752; U66753; U66754; U66755; U66756; U66757; U66758; U66759; U66760; U66761; U66762; U66763; U66764; U66765; U66766; U66768; U66769; U66770; U66771; U66772; U66773; U66774; U66775; U66776; U66777; U66778; U66779; U66780; U66781; U66782; U66783; U66784; U66785; U66786; U66787; U66788; U66789; U66790; U66791; U66792; U66793; U66794; U66795; AL583853; AL356124; AL445439; AL513527; AL590613; AL669984; AL590613; AL356124; AL445439; AL513527; AL583853; AL669984; AL445439; AL356124; AL513527; AL583853; AL590613; AL669984; AL513527; AL356124; AL445439; AL583853; AL590613; AL669984; AL669984; AL356124; AL445439; AL513527; AL583853; AL590613; AL356124; AL445439; AL513527; AL583853; AL590613; AL669984; AL589927; M59832 
Genbank Nucleotide ID
 CAA81394.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; AAB18388.1; CAH70492.1; CAH70492.1; CAH70492.1; CAH70492.1; CAH70492.1; CAH70492.1; CAH70771.1; CAH70771.1; CAH70771.1; CAH70771.1; CAH70771.1; CAH70771.1; CAH72952.1; CAH72952.1; CAH72952.1; CAH72952.1; CAH72952.1; CAH72952.1; CAI15185.1; CAI15185.1; CAI15185.1; CAI15185.1; CAI15185.1; CAI15185.1; CAI16682.1; CAI16682.1; CAI16682.1; CAI16682.1; CAI16682.1; CAI16682.1; CAI22470.1; CAI22470.1; CAI22470.1; CAI22470.1; CAI22470.1; CAI22470.1; AAA63215.1 
Protein Name
 Laminin subunit alpha-2 
Protein Synonyms/Alias
 Laminin M chain; Laminin-12 subunit alpha; Laminin-2 subunit alpha; Laminin-4 subunit alpha; Merosin heavy chain 
Gene Name
 LAMA2 
Gene Synonyms/Alias
 LAMM 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
428SLNEVCVKDEKHARRubiquitination[1]
1943DEAEKVAKEAKDLAHmethylation[2]
2038AAKLQAVKDKARQANubiquitination[3]
2040KLQAVKDKARQANDTubiquitination[3]
2658VEQPIEVKKLFVGGAubiquitination[4]
2856KIKIMRSKQEGILYVubiquitination[1, 4]
2951FDGTGFAKAVGGFKVubiquitination[1]
3107PLEVNFAKALELRGVubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] 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 35 286 Laminin N-terminal.
 DOMAIN 287 343 Laminin EGF-like 1.
 DOMAIN 344 413 Laminin EGF-like 2.
 DOMAIN 414 468 Laminin EGF-like 3.
 DOMAIN 469 517 Laminin EGF-like 4.
 DOMAIN 518 527 Laminin EGF-like 5; first part.
 DOMAIN 531 723 Laminin IV type A 1.
 DOMAIN 724 756 Laminin EGF-like 5; second part.
 DOMAIN 757 806 Laminin EGF-like 6.
 DOMAIN 807 864 Laminin EGF-like 7.
 DOMAIN 865 917 Laminin EGF-like 8.
 DOMAIN 918 966 Laminin EGF-like 9.
 DOMAIN 967 1013 Laminin EGF-like 10.
 DOMAIN 1014 1059 Laminin EGF-like 11.
 DOMAIN 1060 1105 Laminin EGF-like 12.
 DOMAIN 1106 1165 Laminin EGF-like 13.
 DOMAIN 1166 1175 Laminin EGF-like 14; first part.
 DOMAIN 1176 1379 Laminin IV type A 2.
 DOMAIN 1380 1419 Laminin EGF-like 14; second part.
 DOMAIN 1420 1468 Laminin EGF-like 15.
 DOMAIN 1469 1526 Laminin EGF-like 16.
 DOMAIN 1527 1573 Laminin EGF-like 17.
 DOMAIN 2145 2328 Laminin G-like 1.
 DOMAIN 2340 2521 Laminin G-like 2.
 DOMAIN 2526 2710 Laminin G-like 3.
 DOMAIN 2763 2934 Laminin G-like 4.
 DOMAIN 2939 3110 Laminin G-like 5.
 REGION 1574 2144 Domain II and I.
 CARBOHYD 55 55 N-linked (GlcNAc...) (Potential).
 CARBOHYD 89 89 N-linked (GlcNAc...) (Potential).
 CARBOHYD 303 303 N-linked (GlcNAc...) (Potential).
 CARBOHYD 363 363 N-linked (GlcNAc...).
 CARBOHYD 380 380 N-linked (GlcNAc...) (Potential).
 CARBOHYD 470 470 N-linked (GlcNAc...) (Potential).
 CARBOHYD 746 746 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1061 1061 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1597 1597 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1614 1614 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1700 1700 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1810 1810 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1901 1901 N-linked (GlcNAc...).
 CARBOHYD 1916 1916 N-linked (GlcNAc...).
 CARBOHYD 1920 1920 N-linked (GlcNAc...).
 CARBOHYD 2017 2017 N-linked (GlcNAc...).
 CARBOHYD 2028 2028 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2045 2045 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2126 2126 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2240 2240 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2360 2360 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2435 2435 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2478 2478 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2551 2551 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2558 2558 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2648 2648 N-linked (GlcNAc...).
 CARBOHYD 2868 2868 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2893 2893 N-linked (GlcNAc...) (Potential).
 DISULFID 287 296 By similarity.
 DISULFID 289 307 By similarity.
 DISULFID 309 318 By similarity.
 DISULFID 321 341 By similarity.
 DISULFID 344 353 By similarity.
 DISULFID 346 378 By similarity.
 DISULFID 381 390 By similarity.
 DISULFID 393 411 By similarity.
 DISULFID 414 426 By similarity.
 DISULFID 416 442 By similarity.
 DISULFID 444 453 By similarity.
 DISULFID 456 466 By similarity.
 DISULFID 469 482 By similarity.
 DISULFID 471 486 By similarity.
 DISULFID 488 497 By similarity.
 DISULFID 500 515 By similarity.
 DISULFID 757 766 By similarity.
 DISULFID 759 773 By similarity.
 DISULFID 776 785 By similarity.
 DISULFID 788 804 By similarity.
 DISULFID 807 822 By similarity.
 DISULFID 809 832 By similarity.
 DISULFID 835 844 By similarity.
 DISULFID 847 862 By similarity.
 DISULFID 865 879 By similarity.
 DISULFID 867 886 By similarity.
 DISULFID 889 898 By similarity.
 DISULFID 901 915 By similarity.
 DISULFID 918 930 By similarity.
 DISULFID 920 937 By similarity.
 DISULFID 939 948 By similarity.
 DISULFID 951 964 By similarity.
 DISULFID 967 979 By similarity.
 DISULFID 969 985 By similarity.
 DISULFID 987 996 By similarity.
 DISULFID 999 1011 By similarity.
 DISULFID 1014 1023 By similarity.
 DISULFID 1016 1030 By similarity.
 DISULFID 1032 1041 By similarity.
 DISULFID 1044 1057 By similarity.
 DISULFID 1060 1072 By similarity.
 DISULFID 1062 1079 By similarity.
 DISULFID 1081 1090 By similarity.
 DISULFID 1093 1103 By similarity.
 DISULFID 1106 1118 By similarity.
 DISULFID 1108 1134 By similarity.
 DISULFID 1136 1145 By similarity.
 DISULFID 1148 1163 By similarity.
 DISULFID 1420 1429 By similarity.
 DISULFID 1422 1436 By similarity.
 DISULFID 1439 1448 By similarity.
 DISULFID 1451 1466 By similarity.
 DISULFID 1469 1484 By similarity.
 DISULFID 1471 1494 By similarity.
 DISULFID 1497 1506 By similarity.
 DISULFID 1509 1524 By similarity.
 DISULFID 1527 1539 By similarity.
 DISULFID 1529 1546 By similarity.
 DISULFID 1548 1557 By similarity.
 DISULFID 1560 1571 By similarity.
 DISULFID 1574 1574 Interchain (Probable).
 DISULFID 1578 1578 Interchain (Probable).
 DISULFID 2302 2328 By similarity.
 DISULFID 2495 2521 By similarity.
 DISULFID 2683 2710 By similarity.
 DISULFID 2909 2934 By similarity.  
Keyword
 Basement membrane; Cell adhesion; Coiled coil; Complete proteome; Congenital muscular dystrophy; Direct protein sequencing; Disease mutation; Disulfide bond; Extracellular matrix; Glycoprotein; Laminin EGF-like domain; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3122 AA 
Protein Sequence
MPGAAGVLLL LLLSGGLGGV QAQRPQQQRQ SQAHQQRGLF PAVLNLASNA LITTNATCGE 60
KGPEMYCKLV EHVPGQPVRN PQCRICNQNS SNPNQRHPIT NAIDGKNTWW QSPSIKNGIE 120
YHYVTITLDL QQVFQIAYVI VKAANSPRPG NWILERSLDD VEYKPWQYHA VTDTECLTLY 180
NIYPRTGPPS YAKDDEVICT SFYSKIHPLE NGEIHISLIN GRPSADDPSP ELLEFTSARY 240
IRLRFQRIRT LNADLMMFAH KDPREIDPIV TRRYYYSVKD ISVGGMCICY GHARACPLDP 300
ATNKSRCECE HNTCGDSCDQ CCPGFHQKPW RAGTFLTKTE CEACNCHGKA EECYYDENVA 360
RRNLSLNIRG KYIGGGVCIN CTQNTAGINC ETCTDGFFRP KGVSPNYPRP CQPCHCDPIG 420
SLNEVCVKDE KHARRGLAPG SCHCKTGFGG VSCDRCARGY TGYPDCKACN CSGLGSKNED 480
PCFGPCICKE NVEGGDCSRC KSGFFNLQED NWKGCDECFC SGVSNRCQSS YWTYGKIQDM 540
SGWYLTDLPG RIRVAPQQDD LDSPQQISIS NAEARQALPH SYYWSAPAPY LGNKLPAVGG 600
QLTFTISYDL EEEEEDTERV LQLMIILEGN DLSISTAQDE VYLHPSEEHT NVLLLKEESF 660
TIHGTHFPVR RKEFMTVLAN LKRVLLQITY SFGMDAIFRL SSVNLESAVS YPTDGSIAAA 720
VEVCQCPPGY TGSSCESCWP RHRRVNGTIF GGICEPCQCF GHAESCDDVT GECLNCKDHT 780
GGPYCDKCLP GFYGEPTKGT SEDCQPCACP LNIPSNNFSP TCHLDRSLGL ICDGCPVGYT 840
GPRCERCAEG YFGQPSVPGG SCQPCQCNDN LDFSIPGSCD SLSGSCLICK PGTTGRYCEL 900
CADGYFGDAV DAKNCQPCRC NAGGSFSEVC HSQTGQCECR ANVQGQRCDK CKAGTFGLQS 960
ARGCVPCNCN SFGSKSFDCE ESGQCWCQPG VTGKKCDRCA HGYFNFQEGG CTACECSHLG 1020
NNCDPKTGRC ICPPNTIGEK CSKCAPNTWG HSITTGCKAC NCSTVGSLDF QCNVNTGQCN 1080
CHPKFSGAKC TECSRGHWNY PRCNLCDCFL PGTDATTCDS ETKKCSCSDQ TGQCTCKVNV 1140
EGIHCDRCRP GKFGLDAKNP LGCSSCYCFG TTTQCSEAKG LIRTWVTLKA EQTILPLVDE 1200
ALQHTTTKGI VFQHPEIVAH MDLMREDLHL EPFYWKLPEQ FEGKKLMAYG GKLKYAIYFE 1260
AREETGFSTY NPQVIIRGGT PTHARIIVRH MAAPLIGQLT RHEIEMTEKE WKYYGDDPRV 1320
HRTVTREDFL DILYDIHYIL IKATYGNFMR QSRISEISME VAEQGRGTTM TPPADLIEKC 1380
DCPLGYSGLS CEACLPGFYR LRSQPGGRTP GPTLGTCVPC QCNGHSSLCD PETSICQNCQ 1440
HHTAGDFCER CALGYYGIVK GLPNDCQQCA CPLISSSNNF SPSCVAEGLD DYRCTACPRG 1500
YEGQYCERCA PGYTGSPGNP GGSCQECECD PYGSLPVPCD PVTGFCTCRP GATGRKCDGC 1560
KHWHAREGWE CVFCGDECTG LLLGDLARLE QMVMSINLTG PLPAPYKMLY GLENMTQELK 1620
HLLSPQRAPE RLIQLAEGNL NTLVTEMNEL LTRATKVTAD GEQTGQDAER TNTRAKSLGE 1680
FIKELARDAE AVNEKAIKLN ETLGTRDEAF ERNLEGLQKE IDQMIKELRR KNLETQKEIA 1740
EDELVAAEAL LKKVKKLFGE SRGENEEMEK DLREKLADYK NKVDDAWDLL REATDKIREA 1800
NRLFAVNQKN MTALEKKKEA VESGKRQIEN TLKEGNDILD EANRLADEIN SIIDYVEDIQ 1860
TKLPPMSEEL NDKIDDLSQE IKDRKLAEKV SQAESHAAQL NDSSAVLDGI LDEAKNISFN 1920
ATAAFKAYSN IKDYIDEAEK VAKEAKDLAH EATKLATGPR GLLKEDAKGC LQKSFRILNE 1980
AKKLANDVKE NEDHLNGLKT RIENADARNG DLLRTLNDTL GKLSAIPNDT AAKLQAVKDK 2040
ARQANDTAKD VLAQITELHQ NLDGLKKNYN KLADSVAKTN AVVKDPSKNK IIADADATVK 2100
NLEQEADRLI DKLKPIKELE DNLKKNISEI KELINQARKQ ANSIKVSVSS GGDCIRTYKP 2160
EIKKGSYNNI VVNVKTAVAD NLLFYLGSAK FIDFLAIEMR KGKVSFLWDV GSGVGRVEYP 2220
DLTIDDSYWY RIVASRTGRN GTISVRALDG PKASIVPSTH HSTSPPGYTI LDVDANAMLF 2280
VGGLTGKLKK ADAVRVITFT GCMGETYFDN KPIGLWNFRE KEGDCKGCTV SPQVEDSEGT 2340
IQFDGEGYAL VSRPIRWYPN ISTVMFKFRT FSSSALLMYL ATRDLRDFMS VELTDGHIKV 2400
SYDLGSGMAS VVSNQNHNDG KWKSFTLSRI QKQANISIVD IDTNQEENIA TSSSGNNFGL 2460
DLKADDKIYF GGLPTLRNLS MKARPEVNLK KYSGCLKDIE ISRTPYNILS SPDYVGVTKG 2520
CSLENVYTVS FPKPGFVELS PVPIDVGTEI NLSFSTKNES GIILLGSGGT PAPPRRKRRQ 2580
TGQAYYAILL NRGRLEVHLS TGARTMRKIV IRPEPNLFHD GREHSVHVER TRGIFTVQVD 2640
ENRRYMQNLT VEQPIEVKKL FVGGAPPEFQ PSPLRNIPPF EGCIWNLVIN SVPMDFARPV 2700
SFKNADIGRC AHQKLREDED GAAPAEIVIQ PEPVPTPAFP TPTPVLTHGP CAAESEPALL 2760
IGSKQFGLSR NSHIAIAFDD TKVKNRLTIE LEVRTEAESG LLFYMARINH ADFATVQLRN 2820
GLPYFSYDLG SGDTHTMIPT KINDGQWHKI KIMRSKQEGI LYVDGASNRT ISPKKADILD 2880
VVGMLYVGGL PINYTTRRIG PVTYSIDGCV RNLHMAEAPA DLEQPTSSFH VGTCFANAQR 2940
GTYFDGTGFA KAVGGFKVGL DLLVEFEFRT TTTTGVLLGI SSQKMDGMGI EMIDEKLMFH 3000
VDNGAGRFTA VYDAGVPGHL CDGQWHKVTA NKIKHRIELT VDGNQVEAQS PNPASTSADT 3060
NDPVFVGGFP DDLKQFGLTT SIPFRGCIRS LKLTKGTGKP LEVNFAKALE LRGVQPVSCP 3120
AN 3122 
Gene Ontology
 GO:0005604; C:basement membrane; IDA:UniProtKB.
 GO:0005606; C:laminin-1 complex; IEA:InterPro.
 GO:0042383; C:sarcolemma; IEA:Compara.
 GO:0005198; F:structural molecule activity; TAS:ProtInc.
 GO:0007411; P:axon guidance; IEA:Compara.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0007517; P:muscle organ development; TAS:ProtInc.
 GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IEA:Compara.
 GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
 GO:0030334; P:regulation of cell migration; IEA:InterPro.
 GO:0045995; P:regulation of embryonic development; IEA:InterPro. 
Interpro
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR002049; EGF_laminin.
 IPR008979; Galactose-bd-like.
 IPR018031; Laminin_B_subgr.
 IPR000034; Laminin_B_type_IV.
 IPR001791; Laminin_G.
 IPR009254; Laminin_I.
 IPR010307; Laminin_II.
 IPR008211; Laminin_N. 
Pfam
 PF00052; Laminin_B
 PF00053; Laminin_EGF
 PF00054; Laminin_G_1
 PF02210; Laminin_G_2
 PF06008; Laminin_I
 PF06009; Laminin_II
 PF00055; Laminin_N 
SMART
 SM00180; EGF_Lam
 SM00281; LamB
 SM00282; LamG
 SM00136; LamNT 
PROSITE
 PS00022; EGF_1
 PS01186; EGF_2
 PS01248; EGF_LAM_1
 PS50027; EGF_LAM_2
 PS50025; LAM_G_DOMAIN
 PS51115; LAMININ_IVA
 PS51117; LAMININ_NTER 
PRINTS