CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002566
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
 AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59486.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59485.1; AAA59482.1; EAL24388.1; AAI13456.1; AAA59487.1 
Protein Name
 Laminin subunit beta-1 
Protein Synonyms/Alias
 Laminin B1 chain; Laminin-1 subunit beta; Laminin-10 subunit beta; Laminin-12 subunit beta; Laminin-2 subunit beta; Laminin-6 subunit beta; Laminin-8 subunit beta 
Gene Name
 LAMB1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
158ERSSDFGKTWGVYRYubiquitination[1]
215RALDPAFKIEDPYSPubiquitination[1, 2]
229PRIQNLLKITNLRIKubiquitination[1]
1244SPAAEPLKNIGNLFEubiquitination[1, 2]
1310AEQLEFIKNSDIRGAubiquitination[1]
Reference
 [1] 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]
 [2] 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] 
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 31 270 Laminin N-terminal.
 DOMAIN 271 334 Laminin EGF-like 1.
 DOMAIN 335 397 Laminin EGF-like 2.
 DOMAIN 398 457 Laminin EGF-like 3.
 DOMAIN 458 509 Laminin EGF-like 4.
 DOMAIN 510 540 Laminin EGF-like 5; truncated.
 DOMAIN 549 767 Laminin IV type B.
 DOMAIN 773 820 Laminin EGF-like 6.
 DOMAIN 821 866 Laminin EGF-like 7.
 DOMAIN 867 916 Laminin EGF-like 8.
 DOMAIN 917 975 Laminin EGF-like 9.
 DOMAIN 976 1027 Laminin EGF-like 10.
 DOMAIN 1028 1083 Laminin EGF-like 11.
 DOMAIN 1084 1131 Laminin EGF-like 12.
 DOMAIN 1132 1178 Laminin EGF-like 13.
 REGION 1179 1397 Domain II.
 REGION 1398 1430 Domain alpha.
 REGION 1431 1786 Domain I.
 CARBOHYD 120 120 N-linked (GlcNAc...) (Potential).
 CARBOHYD 356 356 N-linked (GlcNAc...) (Potential).
 CARBOHYD 519 519 N-linked (GlcNAc...) (Potential).
 CARBOHYD 677 677 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1041 1041 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1195 1195 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1279 1279 N-linked (GlcNAc...).
 CARBOHYD 1336 1336 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1343 1343 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1487 1487 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1542 1542 N-linked (GlcNAc...) (Potential).
 DISULFID 271 280 By similarity.
 DISULFID 273 298 By similarity.
 DISULFID 300 309 By similarity.
 DISULFID 312 332 By similarity.
 DISULFID 335 344 By similarity.
 DISULFID 337 362 By similarity.
 DISULFID 365 374 By similarity.
 DISULFID 377 395 By similarity.
 DISULFID 398 411 By similarity.
 DISULFID 400 426 By similarity.
 DISULFID 428 437 By similarity.
 DISULFID 440 455 By similarity.
 DISULFID 458 472 By similarity.
 DISULFID 460 479 By similarity.
 DISULFID 481 490 By similarity.
 DISULFID 493 507 By similarity.
 DISULFID 510 522 By similarity.
 DISULFID 512 529 By similarity.
 DISULFID 531 540 By similarity.
 DISULFID 773 785 By similarity.
 DISULFID 775 792 By similarity.
 DISULFID 794 803 By similarity.
 DISULFID 806 818 By similarity.
 DISULFID 821 833 By similarity.
 DISULFID 823 840 By similarity.
 DISULFID 842 851 By similarity.
 DISULFID 854 864 By similarity.
 DISULFID 867 876 By similarity.
 DISULFID 869 883 By similarity.
 DISULFID 886 895 By similarity.
 DISULFID 898 914 By similarity.
 DISULFID 917 933 By similarity.
 DISULFID 919 944 By similarity.
 DISULFID 946 955 By similarity.
 DISULFID 958 973 By similarity.
 DISULFID 976 990 By similarity.
 DISULFID 978 997 By similarity.
 DISULFID 1000 1009 By similarity.
 DISULFID 1012 1025 By similarity.
 DISULFID 1028 1040 By similarity.
 DISULFID 1030 1054 By similarity.
 DISULFID 1056 1065 By similarity.
 DISULFID 1068 1081 By similarity.
 DISULFID 1084 1096 By similarity.
 DISULFID 1086 1103 By similarity.
 DISULFID 1105 1114 By similarity.
 DISULFID 1117 1129 By similarity.
 DISULFID 1132 1144 By similarity.
 DISULFID 1134 1151 By similarity.
 DISULFID 1153 1162 By similarity.
 DISULFID 1165 1176 By similarity.
 DISULFID 1179 1179 Interchain (Probable).
 DISULFID 1182 1182 Interchain (Probable).
 DISULFID 1785 1785 Interchain (Probable).  
Keyword
 Basement membrane; Cell adhesion; Coiled coil; Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein; Laminin EGF-like domain; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1786 AA 
Protein Sequence
MGLLQLLAFS FLALCRARVR AQEPEFSYGC AEGSCYPATG DLLIGRAQKL SVTSTCGLHK 60
PEPYCIVSHL QEDKKCFICN SQDPYHETLN PDSHLIENVV TTFAPNRLKI WWQSENGVEN 120
VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI ERSSDFGKTW GVYRYFAYDC EASFPGISTG 180
PMKKVDDIIC DSRYSDIEPS TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL 240
HTLGDNLLDS RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGFNEEV EGMVHGHCMC 300
RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SISCHFDMAV YLATGNVSGG 360
VCDDCQHNTM GRNCEQCKPF YYQHPERDIR DPNFCERCTC DPAGSQNEGI CDSYTDFSTG 420
LIAGQCRCKL NVEGEHCDVC KEGFYDLSSE DPFGCKSCAC NPLGTIPGGN PCDSETGHCY 480
CKRLVTGQHC DQCLPEHWGL SNDLDGCRPC DCDLGGALNN SCFAESGQCS CRPHMIGRQC 540
NEVEPGYYFA TLDHYLYEAE EANLGPGVSI VERQYIQDRI PSWTGAGFVR VPEGAYLEFF 600
IDNIPYSMEY DILIRYEPQL PDHWEKAVIT VQRPGRIPTS SRCGNTIPDD DNQVVSLSPG 660
SRYVVLPRPV CFEKGTNYTV RLELPQYTSS DSDVESPYTL IDSLVLMPYC KSLDIFTVGG 720
SGDGVVTNSA WETFQRYRCL ENSRSVVKTP MTDVCRNIIF SISALLHQTG LACECDPQGS 780
LSSVCDPNGG QCQCRPNVVG RTCNRCAPGT FGFGPSGCKP CECHLQGSVN AFCNPVTGQC 840
HCFQGVYARQ CDRCLPGHWG FPSCQPCQCN GHADDCDPVT GECLNCQDYT MGHNCERCLA 900
GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY IGSRCDDCAS 960
GYFGNPSEVG GSCQPCQCHN NIDTTDPEAC DKETGRCLKC LYHTEGEHCQ FCRFGYYGDA 1020
LQQDCRKCVC NYLGTVQEHC NGSDCQCDKA TGQCLCLPNV IGQNCDRCAP NTWQLASGTG 1080
CDPCNCNAAH SFGPSCNEFT GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE 1140
TPQCDQSTGQ CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDVII AELTNRTHRF 1200
LEKAKALKIS GVIGPYRETV DSVERKVSEI KDILAQSPAA EPLKNIGNLF EEAEKLIKDV 1260
TEMMAQVEVK LSDTTSQSNS TAKELDSLQT EAESLDNTVK ELAEQLEFIK NSDIRGALDS 1320
ITKYFQMSLE AEERVNASTT EPNSTVEQSA LMRDRVEDVM MERESQFKEK QEEQARLLDE 1380
LAGKLQSLDL SAAAEMTCGT PPGASCSETE CGGPNCRTDE GERKCGGPGC GGLVTVAHNA 1440
WQKAMDLDQD VLSALAEVEQ LSKMVSEAKL RADEAKQSAE DILLKTNATK EKMDKSNEEL 1500
RNLIKQIRNF LTQDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER VESLSQVEVI 1560
LQHSAADIAR AEMLLEEAKR ASKSATDVKV TADMVKEALE EAEKAQVAAE KAIKQADEDI 1620
QGTQNLLTSI ESETAASEET LFNASQRISE LERNVEELKR KAAQNSGEAE YIEKVVYTVK 1680
QSAEDVKKTL DGELDEKYKK VENLIAKKTE ESADARRKAE MLQNEAKTLL AQANSKLQLL 1740
KDLERKYEDN QRYLEDKAQE LARLEGEVRS LLKDISQKVA VYSTCL 1786 
Gene Ontology
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0005606; C:laminin-1 complex; IDA:UniProtKB.
 GO:0043259; C:laminin-10 complex; IDA:UniProtKB.
 GO:0005607; C:laminin-2 complex; IDA:UniProtKB.
 GO:0043257; C:laminin-8 complex; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
 GO:0005201; F:extracellular matrix structural constituent; IDA:HGNC.
 GO:0043208; F:glycosphingolipid binding; IEA:Compara.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0016477; P:cell migration; IEA:Compara.
 GO:0007566; P:embryo implantation; IEA:Compara.
 GO:0007162; P:negative regulation of cell adhesion; IEA:Compara.
 GO:0042476; P:odontogenesis; IDA:UniProtKB.
 GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
 GO:0050679; P:positive regulation of epithelial cell proliferation; TAS:HGNC.
 GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:BHF-UCL. 
Interpro
 IPR002049; EGF_laminin.
 IPR013015; Laminin_IV.
 IPR008211; Laminin_N.
 IPR009053; Prefoldin. 
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