CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000407
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Laminin subunit alpha-5 
Protein Synonyms/Alias
 Laminin-10 subunit alpha; Laminin-11 subunit alpha; Laminin-15 subunit alpha 
Gene Name
 LAMA5 
Gene Synonyms/Alias
 KIAA0533; KIAA1907 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
192WQFFASSKRDCLERFubiquitination[1, 2]
292RRYYYSIKDISIGGRubiquitination[2]
1854PGFYRDVKGLFLGRCubiquitination[2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [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 41 299 Laminin N-terminal.
 DOMAIN 300 358 Laminin EGF-like 1.
 DOMAIN 359 428 Laminin EGF-like 2.
 DOMAIN 429 474 Laminin EGF-like 3.
 DOMAIN 494 540 Laminin EGF-like 4.
 DOMAIN 541 586 Laminin EGF-like 5.
 DOMAIN 587 631 Laminin EGF-like 6.
 DOMAIN 632 676 Laminin EGF-like 7.
 DOMAIN 677 722 Laminin EGF-like 8.
 DOMAIN 723 775 Laminin EGF-like 9.
 DOMAIN 776 828 Laminin EGF-like 10.
 DOMAIN 829 850 Laminin EGF-like 11; truncated.
 DOMAIN 1438 1483 Laminin EGF-like 12.
 DOMAIN 1484 1527 Laminin EGF-like 13.
 DOMAIN 1528 1576 Laminin EGF-like 14.
 DOMAIN 1577 1627 Laminin EGF-like 15.
 DOMAIN 1628 1637 Laminin EGF-like 16; first part.
 DOMAIN 1641 1830 Laminin IV type A.
 DOMAIN 1831 1863 Laminin EGF-like 16; second part.
 DOMAIN 1864 1912 Laminin EGF-like 17.
 DOMAIN 1913 1968 Laminin EGF-like 18.
 DOMAIN 1969 2022 Laminin EGF-like 19.
 DOMAIN 2023 2069 Laminin EGF-like 20.
 DOMAIN 2070 2116 Laminin EGF-like 21.
 DOMAIN 2117 2166 Laminin EGF-like 22.
 DOMAIN 2736 2929 Laminin G-like 1.
 DOMAIN 2941 3115 Laminin G-like 2.
 DOMAIN 3124 3292 Laminin G-like 3.
 DOMAIN 3340 3513 Laminin G-like 4.
 DOMAIN 3520 3692 Laminin G-like 5.
 REGION 851 1437 Domain IV 1 (domain IV B).
 REGION 2167 2735 Domain II and I.
 MOTIF 1722 1724 Cell attachment site (Potential).
 MOTIF 1838 1840 Cell attachment site (Potential).
 CARBOHYD 95 95 N-linked (GlcNAc...) (Potential).
 CARBOHYD 143 143 N-linked (GlcNAc...) (Potential).
 CARBOHYD 243 243 N-linked (GlcNAc...) (Potential).
 CARBOHYD 452 452 N-linked (GlcNAc...) (Potential).
 CARBOHYD 479 479 N-linked (GlcNAc...) (Potential).
 CARBOHYD 900 900 N-linked (GlcNAc...) (Potential).
 CARBOHYD 921 921 N-linked (GlcNAc...) (Potential).
 CARBOHYD 959 959 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1330 1330 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1529 1529 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1555 1555 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2196 2196 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2209 2209 N-linked (GlcNAc...).
 CARBOHYD 2303 2303 N-linked (GlcNAc...).
 CARBOHYD 2423 2423 N-linked (GlcNAc...).
 CARBOHYD 2501 2501 N-linked (GlcNAc...).
 CARBOHYD 2568 2568 N-linked (GlcNAc...).
 CARBOHYD 2707 2707 N-linked (GlcNAc...).
 CARBOHYD 3107 3107 N-linked (GlcNAc...).
 CARBOHYD 3209 3209 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3257 3257 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3287 3287 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3626 3626 N-linked (GlcNAc...) (Potential).
 DISULFID 300 309 By similarity.
 DISULFID 302 322 By similarity.
 DISULFID 324 333 By similarity.
 DISULFID 336 356 By similarity.
 DISULFID 359 368 By similarity.
 DISULFID 361 393 By similarity.
 DISULFID 396 405 By similarity.
 DISULFID 408 426 By similarity.
 DISULFID 429 440 By similarity.
 DISULFID 431 447 By similarity.
 DISULFID 449 458 By similarity.
 DISULFID 461 471 By similarity.
 DISULFID 494 506 By similarity.
 DISULFID 496 515 By similarity.
 DISULFID 517 526 By similarity.
 DISULFID 529 538 By similarity.
 DISULFID 541 553 By similarity.
 DISULFID 543 560 By similarity.
 DISULFID 562 571 By similarity.
 DISULFID 574 584 By similarity.
 DISULFID 587 599 By similarity.
 DISULFID 589 605 By similarity.
 DISULFID 607 616 By similarity.
 DISULFID 619 629 By similarity.
 DISULFID 632 644 By similarity.
 DISULFID 634 650 By similarity.
 DISULFID 652 661 By similarity.
 DISULFID 664 674 By similarity.
 DISULFID 677 689 By similarity.
 DISULFID 679 696 By similarity.
 DISULFID 698 707 By similarity.
 DISULFID 710 725 By similarity.
 DISULFID 746 755 By similarity.
 DISULFID 758 773 By similarity.
 DISULFID 776 790 By similarity.
 DISULFID 778 797 By similarity.
 DISULFID 799 808 By similarity.
 DISULFID 811 826 By similarity.
 DISULFID 829 841 By similarity.
 DISULFID 831 848 By similarity.
 DISULFID 850 859 By similarity.
 DISULFID 1438 1450 By similarity.
 DISULFID 1440 1457 By similarity.
 DISULFID 1459 1468 By similarity.
 DISULFID 1471 1481 By similarity.
 DISULFID 1484 1491 By similarity.
 DISULFID 1486 1498 By similarity.
 DISULFID 1500 1509 By similarity.
 DISULFID 1512 1525 By similarity.
 DISULFID 1528 1543 By similarity.
 DISULFID 1530 1550 By similarity.
 DISULFID 1552 1561 By similarity.
 DISULFID 1564 1574 By similarity.
 DISULFID 1577 1589 By similarity.
 DISULFID 1579 1596 By similarity.
 DISULFID 1598 1607 By similarity.
 DISULFID 1610 1625 By similarity.
 DISULFID 1864 1873 By similarity.
 DISULFID 1866 1880 By similarity.
 DISULFID 1883 1892 By similarity.
 DISULFID 1895 1910 By similarity.
 DISULFID 1913 1928 By similarity.
 DISULFID 1915 1937 By similarity.
 DISULFID 1939 1948 By similarity.
 DISULFID 1951 1966 By similarity.
 DISULFID 1969 1984 By similarity.
 DISULFID 1971 1991 By similarity.
 DISULFID 1994 2003 By similarity.
 DISULFID 2006 2020 By similarity.
 DISULFID 2023 2033 By similarity.
 DISULFID 2025 2040 By similarity.
 DISULFID 2042 2051 By similarity.
 DISULFID 2054 2067 By similarity.
 DISULFID 2070 2081 By similarity.
 DISULFID 2072 2088 By similarity.
 DISULFID 2090 2099 By similarity.
 DISULFID 2102 2114 By similarity.
 DISULFID 2117 2124 By similarity.
 DISULFID 2119 2131 By similarity.
 DISULFID 2133 2142 By similarity.
 DISULFID 2145 2164 By similarity.
 DISULFID 2167 2167 Interchain (Probable).
 DISULFID 2170 2170 Interchain (Probable).
 DISULFID 2899 2929 By similarity.
 DISULFID 3090 3115 By similarity.
 DISULFID 3261 3292 By similarity.
 DISULFID 3490 3513 By similarity.
 DISULFID 3664 3692 By similarity.  
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
 3695 AA 
Protein Sequence
MAKRLCAGSA LCVRGPRGPA PLLLVGLALL GAARAREEAG GGFSLHPPYF NLAEGARIAA 60
SATCGEEAPA RGSPRPTEDL YCKLVGGPVA GGDPNQTIRG QYCDICTAAN SNKAHPASNA 120
IDGTERWWQS PPLSRGLEYN EVNVTLDLGQ VFHVAYVLIK FANSPRPDLW VLERSMDFGR 180
TYQPWQFFAS SKRDCLERFG PQTLERITRD DAAICTTEYS RIVPLENGEI VVSLVNGRPG 240
AMNFSYSPLL REFTKATNVR LRFLRTNTLL GHLMGKALRD PTVTRRYYYS IKDISIGGRC 300
VCHGHADACD AKDPTDPFRL QCTCQHNTCG GTCDRCCPGF NQQPWKPATA NSANECQSCN 360
CYGHATDCYY DPEVDRRRAS QSLDGTYQGG GVCIDCQHHT TGVNCERCLP GFYRSPNHPL 420
DSPHVCRRCN CESDFTDGTC EDLTGRCYCR PNFSGERCDV CAEGFTGFPS CYPTPSSSND 480
TREQVLPAGQ IVNCDCSAAG TQGNACRKDP RVGRCLCKPN FQGTHCELCA PGFYGPGCQP 540
CQCSSPGVAD DRCDPDTGQC RCRVGFEGAT CDRCAPGYFH FPLCQLCGCS PAGTLPEGCD 600
EAGRCLCQPE FAGPHCDRCR PGYHGFPNCQ ACTCDPRGAL DQLCGAGGLC RCRPGYTGTA 660
CQECSPGFHG FPSCVPCHCS AEGSLHAACD PRSGQCSCRP RVTGLRCDTC VPGAYNFPYC 720
EAGSCHPAGL APVDPALPEA QVPCMCRAHV EGPSCDRCKP GFWGLSPSNP EGCTRCSCDL 780
RGTLGGVAEC QPGTGQCFCK PHVCGQACAS CKDGFFGLDQ ADYFGCRSCR CDIGGALGQS 840
CEPRTGVCRC RPNTQGPTCS EPARDHYLPD LHHLRLELEE AATPEGHAVR FGFNPLEFEN 900
FSWRGYAQMA PVQPRIVARL NLTSPDLFWL VFRYVNRGAM SVSGRVSVRE EGRSATCANC 960
TAQSQPVAFP PSTEPAFITV PQRGFGEPFV LNPGTWALRV EAEGVLLDYV VLLPSAYYEA 1020
ALLQLRVTEA CTYRPSAQQS GDNCLLYTHL PLDGFPSAAG LEALCRQDNS LPRPCPTEQL 1080
SPSHPPLITC TGSDVDVQLQ VAVPQPGRYA LVVEYANEDA RQEVGVAVHT PQRAPQQGLL 1140
SLHPCLYSTL CRGTARDTQD HLAVFHLDSE ASVRLTAEQA RFFLHGVTLV PIEEFSPEFV 1200
EPRVSCISSH GAFGPNSAAC LPSRFPKPPQ PIILRDCQVI PLPPGLPLTH AQDLTPAMSP 1260
AGPRPRPPTA VDPDAEPTLL REPQATVVFT THVPTLGRYA FLLHGYQPAH PTFPVEVLIN 1320
AGRVWQGHAN ASFCPHGYGC RTLVVCEGQA LLDVTHSELT VTVRVPKGRW LWLDYVLVVP 1380
ENVYSFGYLR EEPLDKSYDF ISHCAAQGYH ISPSSSSLFC RNAAASLSLF YNNGARPCGC 1440
HEVGATGPTC EPFGGQCPCH AHVIGRDCSR CATGYWGFPN CRPCDCGARL CDELTGQCIC 1500
PPRTIPPDCL LCQPQTFGCH PLVGCEECNC SGPGIQELTD PTCDTDSGQC KCRPNVTGRR 1560
CDTCSPGFHG YPRCRPCDCH EAGTAPGVCD PLTGQCYCKE NVQGPKCDQC SLGTFSLDAA 1620
NPKGCTRCFC FGATERCRSS SYTRQEFVDM EGWVLLSTDR QVVPHERQPG TEMLRADLRH 1680
VPEAVPEAFP ELYWQAPPSY LGDRVSSYGG TLRYELHSET QRGDVFVPME SRPDVVLQGN 1740
QMSITFLEPA YPTPGHVHRG QLQLVEGNFR HTETRNTVSR EELMMVLASL EQLQIRALFS 1800
QISSAVFLRR VALEVASPAG QGALASNVEL CLCPASYRGD SCQECAPGFY RDVKGLFLGR 1860
CVPCQCHGHS DRCLPGSGVC VDCQHNTEGA HCERCQAGFV SSRDDPSAPC VSCPCPLSVP 1920
SNNFAEGCVL RGGRTQCLCK PGYAGASCER CAPGFFGNPL VLGSSCQPCD CSGNGDPNLL 1980
FSDCDPLTGA CRGCLRHTTG PRCEICAPGF YGNALLPGNC TRCDCTPCGT EACDPHSGHC 2040
LCKAGVTGRR CDRCQEGHFG FDGCGGCRPC ACGPAAEGSE CHPQSGQCHC RPGTMGPQCR 2100
ECAPGYWGLP EQGCRRCQCP GGRCDPHTGR CNCPPGLSGE RCDTCSQQHQ VPVPGGPVGH 2160
SIHCEVCDHC VVLLLDDLER AGALLPAIHE QLRGINASSM AWARLHRLNA SIADLQSQLR 2220
SPLGPRHETA QQLEVLEQQS TSLGQDARRL GGQAVGTRDQ ASQLLAGTEA TLGHAKTLLA 2280
AIRAVDRTLS ELMSQTGHLG LANASAPSGE QLLRTLAEVE RLLWEMRARD LGAPQAAAEA 2340
ELAAAQRLLA RVQEQLSSLW EENQALATQT RDRLAQHEAG LMDLREALNR AVDATREAQE 2400
LNSRNQERLE EALQRKQELS RDNATLQATL HAARDTLASV FRLLHSLDQA KEELERLAAS 2460
LDGARTPLLQ RMQTFSPAGS KLRLVEAAEA HAQQLGQLAL NLSSIILDVN QDRLTQRAIE 2520
ASNAYSRILQ AVQAAEDAAG QALQQADHTW ATVVRQGLVD RAQQLLANST ALEEAMLQEQ 2580
QRLGLVWAAL QGARTQLRDV RAKKDQLEAH IQAAQAMLAM DTDETSKKIA HAKAVAAEAQ 2640
DTATRVQSQL QAMQENVERW QGQYEGLRGQ DLGQAVLDAG HSVSTLEKTL PQLLAKLSIL 2700
ENRGVHNASL ALSASIGRVR ELIAQARGAA SKVKVPMKFN GRSGVQLRTP RDLADLAAYT 2760
ALKFYLQGPE PEPGQGTEDR FVMYMGSRQA TGDYMGVSLR DKKVHWVYQL GEAGPAVLSI 2820
DEDIGEQFAA VSLDRTLQFG HMSVTVERQM IQETKGDTVA PGAEGLLNLR PDDFVFYVGG 2880
YPSTFTPPPL LRFPGYRGCI EMDTLNEEVV SLYNFERTFQ LDTAVDRPCA RSKSTGDPWL 2940
TDGSYLDGTG FARISFDSQI STTKRFEQEL RLVSYSGVLF FLKQQSQFLC LAVQEGSLVL 3000
LYDFGAGLKK AVPLQPPPPL TSASKAIQVF LLGGSRKRVL VRVERATVYS VEQDNDLELA 3060
DAYYLGGVPP DQLPPSLRRL FPTGGSVRGC VKGIKALGKY VDLKRLNTTG VSAGCTADLL 3120
VGRAMTFHGH GFLRLALSNV APLTGNVYSG FGFHSAQDSA LLYYRASPDG LCQVSLQQGR 3180
VSLQLLRTEV KTQAGFADGA PHYVAFYSNA TGVWLYVDDQ LQQMKPHRGP PPELQPQPEG 3240
PPRLLLGGLP ESGTIYNFSG CISNVFVQRL LGPQRVFDLQ QNLGSVNVST GCAPALQAQT 3300
PGLGPRGLQA TARKASRRSR QPARHPACML PPHLRTTRDS YQFGGSLSSH LEFVGILARH 3360
RNWPSLSMHV LPRSSRGLLL FTARLRPGSP SLALFLSNGH FVAQMEGLGT RLRAQSRQRS 3420
RPGRWHKVSV RWEKNRILLV TDGARAWSQE GPHRQHQGAE HPQPHTLFVG GLPASSHSSK 3480
LPVTVGFSGC VKRLRLHGRP LGAPTRMAGV TPCILGPLEA GLFFPGSGGV ITLDLPGATL 3540
PDVGLELEVR PLAVTGLIFH LGQARTPPYL QLQVTEKQVL LRADDGAGEF STSVTRPSVL 3600
CDGQWHRLAV MKSGNVLRLE VDAQSNHTVG PLLAAAAGAP APLYLGGLPE PMAVQPWPPA 3660
YCGCMRRLAV NRSPVAMTRS VEVHGAVGAS GCPAA 3695 
Gene Ontology
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0005606; C:laminin-1 complex; IEA:InterPro.
 GO:0043259; C:laminin-10 complex; IDA:UniProtKB.
 GO:0043260; C:laminin-11 complex; TAS:BHF-UCL.
 GO:0005178; F:integrin binding; IDA:UniProtKB.
 GO:0005198; F:structural molecule activity; IC:UniProtKB.
 GO:0001525; P:angiogenesis; NAS:UniProtKB.
 GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Compara.
 GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Compara.
 GO:0016477; P:cell migration; IDA:UniProtKB.
 GO:0008283; P:cell proliferation; NAS:UniProtKB.
 GO:0008037; P:cell recognition; NAS:UniProtKB.
 GO:0042384; P:cilium assembly; IEA:Compara.
 GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
 GO:0009790; P:embryo development; NAS:UniProtKB.
 GO:0045446; P:endothelial cell differentiation; NAS:UniProtKB.
 GO:0090002; P:establishment of protein localization to plasma membrane; IEA:Compara.
 GO:0048041; P:focal adhesion assembly; NAS:UniProtKB.
 GO:0001942; P:hair follicle development; IEA:Compara.
 GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
 GO:0030324; P:lung development; IEA:Compara.
 GO:0001738; P:morphogenesis of a polarized epithelium; IEA:Compara.
 GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Compara.
 GO:0007517; P:muscle organ development; IEA:Compara.
 GO:0001755; P:neural crest cell migration; IEA:Compara.
 GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Compara.
 GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
 GO:0030334; P:regulation of cell migration; IEA:InterPro.
 GO:0042127; P:regulation of cell proliferation; IEA:Compara.
 GO:0045995; P:regulation of embryonic development; IEA:InterPro.
 GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:BHF-UCL. 
Interpro
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR013032; EGF-like_CS.
 IPR002049; EGF_laminin.
 IPR018031; Laminin_B_subgr.
 IPR000034; Laminin_B_type_IV.
 IPR001791; Laminin_G.
 IPR009254; Laminin_I.
 IPR010307; Laminin_II.
 IPR008211; Laminin_N.
 IPR001368; TNFR/NGFR_Cys_rich_reg. 
Pfam
 PF00052; Laminin_B
 PF00053; Laminin_EGF
 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