CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008977
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Laminin subunit beta-2 
Protein Synonyms/Alias
 Laminin B1s chain; Laminin-11 subunit beta; Laminin-14 subunit beta; Laminin-15 subunit beta; Laminin-3 subunit beta; Laminin-4 subunit beta; Laminin-7 subunit beta; Laminin-9 subunit beta; S-laminin subunit beta; S-LAM beta 
Gene Name
 LAMB2 
Gene Synonyms/Alias
 LAMS 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
241SRIQNLLKITNLRVNubiquitination[1]
1322DQHLDLLKHSNFLGAubiquitination[1]
1671DALLEALKLKRAGNSubiquitination[1, 2]
1714GDQYQTVKALAERKAubiquitination[1, 3]
1748LLQAAQDKLQRLQELubiquitination[1]
1769NERALESKAAQLDGLubiquitination[1, 3]
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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] 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 43 282 Laminin N-terminal.
 DOMAIN 283 346 Laminin EGF-like 1.
 DOMAIN 347 409 Laminin EGF-like 2.
 DOMAIN 410 469 Laminin EGF-like 3.
 DOMAIN 470 521 Laminin EGF-like 4.
 DOMAIN 522 552 Laminin EGF-like 5; truncated.
 DOMAIN 561 777 Laminin IV type B.
 DOMAIN 783 830 Laminin EGF-like 6.
 DOMAIN 831 876 Laminin EGF-like 7.
 DOMAIN 877 926 Laminin EGF-like 8.
 DOMAIN 927 985 Laminin EGF-like 9.
 DOMAIN 986 1037 Laminin EGF-like 10.
 DOMAIN 1038 1094 Laminin EGF-like 11.
 DOMAIN 1095 1142 Laminin EGF-like 12.
 DOMAIN 1143 1189 Laminin EGF-like 13.
 REGION 1190 1409 Domain II.
 REGION 1410 1442 Domain alpha.
 REGION 1443 1798 Domain I.
 CARBOHYD 248 248 N-linked (GlcNAc...) (Potential).
 CARBOHYD 368 368 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1085 1085 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1249 1249 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1308 1308 N-linked (GlcNAc...).
 CARBOHYD 1348 1348 N-linked (GlcNAc...).
 CARBOHYD 1499 1499 N-linked (GlcNAc...).
 DISULFID 283 292 By similarity.
 DISULFID 285 310 By similarity.
 DISULFID 312 321 By similarity.
 DISULFID 324 344 By similarity.
 DISULFID 347 356 By similarity.
 DISULFID 349 374 By similarity.
 DISULFID 377 386 By similarity.
 DISULFID 389 407 By similarity.
 DISULFID 410 423 By similarity.
 DISULFID 412 438 By similarity.
 DISULFID 440 449 By similarity.
 DISULFID 452 467 By similarity.
 DISULFID 470 484 By similarity.
 DISULFID 472 491 By similarity.
 DISULFID 493 502 By similarity.
 DISULFID 505 519 By similarity.
 DISULFID 522 534 By similarity.
 DISULFID 524 541 By similarity.
 DISULFID 543 552 By similarity.
 DISULFID 783 795 By similarity.
 DISULFID 785 802 By similarity.
 DISULFID 804 813 By similarity.
 DISULFID 816 828 By similarity.
 DISULFID 831 843 By similarity.
 DISULFID 833 850 By similarity.
 DISULFID 852 861 By similarity.
 DISULFID 864 874 By similarity.
 DISULFID 877 886 By similarity.
 DISULFID 879 893 By similarity.
 DISULFID 896 905 By similarity.
 DISULFID 908 924 By similarity.
 DISULFID 927 943 By similarity.
 DISULFID 929 954 By similarity.
 DISULFID 956 965 By similarity.
 DISULFID 968 983 By similarity.
 DISULFID 986 1000 By similarity.
 DISULFID 988 1007 By similarity.
 DISULFID 1010 1019 By similarity.
 DISULFID 1022 1035 By similarity.
 DISULFID 1038 1058 By similarity.
 DISULFID 1040 1065 By similarity.
 DISULFID 1067 1076 By similarity.
 DISULFID 1079 1092 By similarity.
 DISULFID 1095 1107 By similarity.
 DISULFID 1097 1114 By similarity.
 DISULFID 1116 1125 By similarity.
 DISULFID 1128 1140 By similarity.
 DISULFID 1143 1155 By similarity.
 DISULFID 1145 1162 By similarity.
 DISULFID 1164 1173 By similarity.
 DISULFID 1176 1187 By similarity.
 DISULFID 1190 1190 Interchain (Probable).
 DISULFID 1193 1193 Interchain (Probable).
 DISULFID 1797 1797 Interchain (Probable).  
Keyword
 Basement membrane; Cell adhesion; Coiled coil; Complete proteome; 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
 1798 AA 
Protein Sequence
MELTSRERGR GQPLPWELRL GLLLSVLAAT LAQAPAPDVP GCSRGSCYPA TGDLLVGRAD 60
RLTASSTCGL NGPQPYCIVS HLQDEKKCFL CDSRRPFSAR DNPHSHRIQN VVTSFAPQRR 120
AAWWQSENGI PAVTIQLDLE AEFHFTHLIM TFKTFRPAAM LVERSADFGR TWHVYRYFSY 180
DCGADFPGVP LAPPRHWDDV VCESRYSEIE PSTEGEVIYR VLDPAIPIPD PYSSRIQNLL 240
KITNLRVNLT RLHTLGDNLL DPRREIREKY YYALYELVVR GNCFCYGHAS ECAPAPGAPA 300
HAEGMVHGAC ICKHNTRGLN CEQCQDFYRD LPWRPAEDGH SHACRKCECH GHTHSCHFDM 360
AVYLASGNVS GGVCDGCQHN TAGRHCELCR PFFYRDPTKD LRDPAVCRSC DCDPMGSQDG 420
GRCDSHDDPA LGLVSGQCRC KEHVVGTRCQ QCRDGFFGLS ISDRLGCRRC QCNARGTVPG 480
STPCDPNSGS CYCKRLVTGR GCDRCLPGHW GLSHDLLGCR PCDCDVGGAL DPQCDEGTGQ 540
CHCRQHMVGR RCEQVQPGYF RPFLDHLIWE AEDTRGQVLD VVERLVTPGE TPSWTGSGFV 600
RLQEGQTLEF LVASVPKAMD YDLLLRLEPQ VPEQWAELEL IVQRPGPVPA HSLCGHLVPK 660
DDRIQGTLQP HARYLIFPNP VCLEPGISYK LHLKLVRTGG SAQPETPYSG PGLLIDSLVL 720
LPRVLVLEMF SGGDAAALER QATFERYQCH EEGLVPSKTS PSEACAPLLI SLSTLIYNGA 780
LPCQCNPQGS LSSECNPHGG QCLCKPGVVG RRCDLCAPGY YGFGPTGCQA CQCSHEGALS 840
SLCEKTSGQC LCRTGAFGLR CDRCQRGQWG FPSCRPCVCN GHADECNTHT GACLGCRDHT 900
GGEHCERCIA GFHGDPRLPY GGQCRPCPCP EGPGSQRHFA TSCHQDEYSQ QIVCHCRAGY 960
TGLRCEACAP GHFGDPSRPG GRCQLCECSG NIDPMDPDAC DPHTGQCLRC LHHTEGPHCA 1020
HCKPGFHGQA ARQSCHRCTC NLLGTNPQQC PSPDQCHCDP SSGQCPCLPN VQGPSCDRCA 1080
PNFWNLTSGH GCQPCACHPS RARGPTCNEF TGQCHCRAGF GGRTCSECQE LHWGDPGLQC 1140
HACDCDSRGI DTPQCHRFTG HCSCRPGVSG VRCDQCARGF SGIFPACHPC HACFGDWDRV 1200
VQDLAARTQR LEQRAQELQQ TGVLGAFESS FWHMQEKLGI VQGIVGARNT SAASTAQLVE 1260
ATEELRREIG EATEHLTQLE ADLTDVQDEN FNANHALSGL ERDRLALNLT LRQLDQHLDL 1320
LKHSNFLGAY DSIRHAHSQS AEAERRANTS ALAVPSPVSN SASARHRTEA LMDAQKEDFN 1380
SKHMANQRAL GKLSAHTHTL SLTDINELVC GAPGDAPCAT SPCGGAGCRD EDGQPRCGGL 1440
SCNGAAATAD LALGRARHTQ AELQRALAEG GSILSRVAET RRQASEAQQR AQAALDKANA 1500
SRGQVEQANQ ELQELIQSVK DFLNQEGADP DSIEMVATRV LELSIPASAE QIQHLAGAIA 1560
ERVRSLADVD AILARTVGDV RRAEQLLQDA RRARSWAEDE KQKAETVQAA LEEAQRAQGI 1620
AQGAIRGAVA DTRDTEQTLY QVQERMAGAE RALSSAGERA RQLDALLEAL KLKRAGNSLA 1680
ASTAEETAGS AQGRAQEAEQ LLRGPLGDQY QTVKALAERK AQGVLAAQAR AEQLRDEARD 1740
LLQAAQDKLQ RLQELEGTYE ENERALESKA AQLDGLEARM RSVLQAINLQ VQIYNTCQ 1798 
Gene Ontology
 GO:0043260; C:laminin-11 complex; TAS:BHF-UCL.
 GO:0005608; C:laminin-3 complex; IPI:UniProtKB.
 GO:0045202; C:synapse; IEA:Compara.
 GO:0005198; F:structural molecule activity; NAS:ProtInc.
 GO:0014002; P:astrocyte development; IEA:Compara.
 GO:0048677; P:axon extension involved in regeneration; IEA:Compara.
 GO:0007411; P:axon guidance; IEA:Compara.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0072274; P:metanephric glomerular basement membrane development; IEA:Compara.
 GO:0072249; P:metanephric glomerular visceral epithelial cell development; IEA:Compara.
 GO:0007528; P:neuromuscular junction development; IEA:Compara.
 GO:0060041; P:retina development in camera-type eye; IEA:Compara.
 GO:0014044; P:Schwann cell development; IEA:Compara.
 GO:0007601; P:visual perception; IEA:Compara. 
Interpro
 IPR013032; EGF-like_CS.
 IPR002049; EGF_laminin.
 IPR013015; Laminin_IV.
 IPR008211; Laminin_N. 
Pfam
 PF00053; Laminin_EGF
 PF00055; Laminin_N 
SMART
 SM00180; EGF_Lam
 SM00136; LamNT 
PROSITE
 PS00022; EGF_1
 PS01186; EGF_2
 PS01248; EGF_LAM_1
 PS50027; EGF_LAM_2
 PS51116; LAMININ_IVB
 PS51117; LAMININ_NTER 
PRINTS