CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012195
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Laminin subunit beta-3 
Protein Synonyms/Alias
 Epiligrin subunit bata; Kalinin B1 chain; Kalinin subunit beta; Laminin B1k chain; Laminin-5 subunit beta; Nicein subunit beta 
Gene Name
 LAMB3 
Gene Synonyms/Alias
 LAMNB1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
51SSTCGLTKPETYCTQubiquitination[1]
65QYGEWQMKCCKCDSRubiquitination[1]
141ERSSDFGKTWRVYQYubiquitination[1, 2, 3]
188NARLNGGKVQLNLMDubiquitination[1, 2, 3]
207IPATQSQKIQEVGEIubiquitination[1, 2, 3]
402VTGQCVCKEHVQGERubiquitination[1]
414GERCDLCKPGFTGLTubiquitination[1]
705RKREQFEKISSADPSubiquitination[1, 2, 3]
766GGGTGSPKLVALRLEubiquitination[1, 2, 3]
786DLTPTFNKLCGNSRQubiquitination[1]
953DLVLSQTKQDIARARubiquitination[1, 2, 3, 4]
1027QVLRPAEKLVTSMTKubiquitination[1, 3]
1034KLVTSMTKQLGDFWTubiquitination[3]
1152ADLTGLEKRVEQIRDubiquitination[2, 3]
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]
 [3] 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]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572
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 22 249 Laminin N-terminal.
 DOMAIN 250 315 Laminin EGF-like 1.
 DOMAIN 316 378 Laminin EGF-like 2.
 DOMAIN 379 430 Laminin EGF-like 3.
 DOMAIN 431 480 Laminin EGF-like 4.
 DOMAIN 481 533 Laminin EGF-like 5.
 DOMAIN 534 580 Laminin EGF-like 6.
 REGION 579 785 Domain II.
 REGION 786 816 Domain alpha.
 REGION 817 1170 Domain I.
 CARBOHYD 220 220 N-linked (GlcNAc...) (Potential).
 CARBOHYD 604 604 N-linked (GlcNAc...) (Potential).
 CARBOHYD 810 810 N-linked (GlcNAc...) (Potential).
 DISULFID 250 259 By similarity.
 DISULFID 252 279 By similarity.
 DISULFID 281 290 By similarity.
 DISULFID 293 313 By similarity.
 DISULFID 316 325 By similarity.
 DISULFID 318 343 By similarity.
 DISULFID 346 355 By similarity.
 DISULFID 358 376 By similarity.
 DISULFID 379 392 By similarity.
 DISULFID 381 399 By similarity.
 DISULFID 401 410 By similarity.
 DISULFID 413 428 By similarity.
 DISULFID 431 444 By similarity.
 DISULFID 433 451 By similarity.
 DISULFID 453 462 By similarity.
 DISULFID 465 478 By similarity.
 DISULFID 481 493 By similarity.
 DISULFID 483 500 By similarity.
 DISULFID 502 511 By similarity.
 DISULFID 519 531 By similarity.
 DISULFID 534 546 By similarity.
 DISULFID 536 553 By similarity.
 DISULFID 555 564 By similarity.
 DISULFID 567 578 By similarity.
 DISULFID 581 581 Interchain (Probable).
 DISULFID 584 584 Interchain (Probable).
 DISULFID 1171 1171 Interchain (Probable).  
Keyword
 Basement membrane; Cell adhesion; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Epidermolysis bullosa; Extracellular matrix; Glycoprotein; Laminin EGF-like domain; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1172 AA 
Protein Sequence
MRPFFLLCFA LPGLLHAQQA CSRGACYPPV GDLLVGRTRF LRASSTCGLT KPETYCTQYG 60
EWQMKCCKCD SRQPHNYYSH RVENVASSSG PMRWWQSQND VNPVSLQLDL DRRFQLQEVM 120
MEFQGPMPAG MLIERSSDFG KTWRVYQYLA ADCTSTFPRV RQGRPQSWQD VRCQSLPQRP 180
NARLNGGKVQ LNLMDLVSGI PATQSQKIQE VGEITNLRVN FTRLAPVPQR GYHPPSAYYA 240
VSQLRLQGSC FCHGHADRCA PKPGASAGPS TAVQVHDVCV CQHNTAGPNC ERCAPFYNNR 300
PWRPAEGQDA HECQRCDCNG HSETCHFDPA VFAASQGAYG GVCDNCRDHT EGKNCERCQL 360
HYFRNRRPGA SIQETCISCE CDPDGAVPGA PCDPVTGQCV CKEHVQGERC DLCKPGFTGL 420
TYANPQGCHR CDCNILGSRR DMPCDEESGR CLCLPNVVGP KCDQCAPYHW KLASGQGCEP 480
CACDPHNSLS PQCNQFTGQC PCREGFGGLM CSAAAIRQCP DRTYGDVATG CRACDCDFRG 540
TEGPGCDKAS GRCLCRPGLT GPRCDQCQRG YCNRYPVCVA CHPCFQTYDA DLREQALRFG 600
RLRNATASLW SGPGLEDRGL ASRILDAKSK IEQIRAVLSS PAVTEQEVAQ VASAILSLRR 660
TLQGLQLDLP LEEETLSLPR DLESLDRSFN GLLTMYQRKR EQFEKISSAD PSGAFRMLST 720
AYEQSAQAAQ QVSDSSRLLD QLRDSRREAE RLVRQAGGGG GTGSPKLVAL RLEMSSLPDL 780
TPTFNKLCGN SRQMACTPIS CPGELCPQDN GTACGSRCRG VLPRAGGAFL MAGQVAEQLR 840
GFNAQLQRTR QMIRAAEESA SQIQSSAQRL ETQVSASRSQ MEEDVRRTRL LIQQVRDFLT 900
DPDTDAATIQ EVSEAVLALW LPTDSATVLQ KMNEIQAIAA RLPNVDLVLS QTKQDIARAR 960
RLQAEAEEAR SRAHAVEGQV EDVVGNLRQG TVALQEAQDT MQGTSRSLRL IQDRVAEVQQ 1020
VLRPAEKLVT SMTKQLGDFW TRMEELRHQA RQQGAEAVQA QQLAEGASEQ ALSAQEGFER 1080
IKQKYAELKD RLGQSSMLGE QGARIQSVKT EAEELFGETM EMMDRMKDME LELLRGSQAI 1140
MLRSADLTGL EKRVEQIRDH INGRVLYYAT CK 1172 
Gene Ontology
 GO:0005576; C:extracellular region; TAS:Reactome.
 GO:0005610; C:laminin-5 complex; IEA:Compara.
 GO:0005198; F:structural molecule activity; NAS:ProtInc.
 GO:0050873; P:brown fat cell differentiation; IEA:Compara.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0008544; P:epidermis development; TAS:ProtInc.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0031581; P:hemidesmosome assembly; TAS:Reactome. 
Interpro
 IPR013032; EGF-like_CS.
 IPR002049; EGF_laminin.
 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
 PS51117; LAMININ_NTER 
PRINTS