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O15230

- LAMA5_HUMAN

UniProt

O15230 - LAMA5_HUMAN

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Protein

Laminin subunit alpha-5

Gene
LAMA5, KIAA0533, KIAA1907
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. integrin binding Source: UniProtKB
  2. structural molecule activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. branching involved in salivary gland morphogenesis Source: Ensembl
  3. branching involved in ureteric bud morphogenesis Source: Ensembl
  4. cell differentiation Source: UniProtKB
  5. cell migration Source: UniProtKB
  6. cell proliferation Source: UniProtKB
  7. cell recognition Source: UniProtKB
  8. cilium assembly Source: Ensembl
  9. cytoskeleton organization Source: UniProtKB
  10. embryo development Source: UniProtKB
  11. endothelial cell differentiation Source: UniProtKB
  12. establishment of protein localization to plasma membrane Source: Ensembl
  13. extracellular matrix disassembly Source: Reactome
  14. extracellular matrix organization Source: Reactome
  15. focal adhesion assembly Source: UniProtKB
  16. hair follicle development Source: Ensembl
  17. integrin-mediated signaling pathway Source: UniProtKB
  18. lung development Source: Ensembl
  19. morphogenesis of a polarized epithelium Source: Ensembl
  20. morphogenesis of embryonic epithelium Source: Ensembl
  21. muscle organ development Source: Ensembl
  22. neural crest cell migration Source: Ensembl
  23. odontogenesis of dentin-containing tooth Source: Ensembl
  24. regulation of cell adhesion Source: InterPro
  25. regulation of cell migration Source: InterPro
  26. regulation of cell proliferation Source: Ensembl
  27. regulation of embryonic development Source: InterPro
  28. substrate adhesion-dependent cell spreading Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit alpha-5
Alternative name(s):
Laminin-10 subunit alpha
Laminin-11 subunit alpha
Laminin-15 subunit alpha
Gene namesi
Name:LAMA5
Synonyms:KIAA0533, KIAA1907
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:6485. LAMA5.

Subcellular locationi

GO - Cellular componenti

  1. basal lamina Source: UniProtKB
  2. basement membrane Source: UniProtKB
  3. extracellular region Source: Reactome
  4. extracellular space Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. laminin-10 complex Source: UniProtKB
  7. laminin-11 complex Source: BHF-UCL
  8. laminin-1 complex Source: InterPro
  9. laminin-5 complex Source: Ensembl
  10. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30274.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535 Reviewed predictionAdd
BLAST
Chaini36 – 36953660Laminin subunit alpha-5PRO_0000017062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi95 – 951N-linked (GlcNAc...) Reviewed prediction
Glycosylationi143 – 1431N-linked (GlcNAc...) Reviewed prediction
Glycosylationi243 – 2431N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi300 ↔ 309 By similarity
Disulfide bondi302 ↔ 322 By similarity
Disulfide bondi324 ↔ 333 By similarity
Disulfide bondi336 ↔ 356 By similarity
Disulfide bondi359 ↔ 368 By similarity
Disulfide bondi361 ↔ 393 By similarity
Disulfide bondi396 ↔ 405 By similarity
Disulfide bondi408 ↔ 426 By similarity
Disulfide bondi429 ↔ 440 By similarity
Disulfide bondi431 ↔ 447 By similarity
Disulfide bondi449 ↔ 458 By similarity
Glycosylationi452 – 4521N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi461 ↔ 471 By similarity
Glycosylationi479 – 4791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi494 ↔ 506 By similarity
Disulfide bondi496 ↔ 515 By similarity
Disulfide bondi517 ↔ 526 By similarity
Disulfide bondi529 ↔ 538 By similarity
Disulfide bondi541 ↔ 553 By similarity
Disulfide bondi543 ↔ 560 By similarity
Disulfide bondi562 ↔ 571 By similarity
Disulfide bondi574 ↔ 584 By similarity
Disulfide bondi587 ↔ 599 By similarity
Disulfide bondi589 ↔ 605 By similarity
Disulfide bondi607 ↔ 616 By similarity
Disulfide bondi619 ↔ 629 By similarity
Disulfide bondi632 ↔ 644 By similarity
Disulfide bondi634 ↔ 650 By similarity
Disulfide bondi652 ↔ 661 By similarity
Disulfide bondi664 ↔ 674 By similarity
Disulfide bondi677 ↔ 689 By similarity
Disulfide bondi679 ↔ 696 By similarity
Disulfide bondi698 ↔ 707 By similarity
Disulfide bondi710 ↔ 725 By similarity
Disulfide bondi746 ↔ 755 By similarity
Disulfide bondi758 ↔ 773 By similarity
Disulfide bondi776 ↔ 790 By similarity
Disulfide bondi778 ↔ 797 By similarity
Disulfide bondi799 ↔ 808 By similarity
Disulfide bondi811 ↔ 826 By similarity
Disulfide bondi829 ↔ 841 By similarity
Disulfide bondi831 ↔ 848 By similarity
Disulfide bondi850 ↔ 859 By similarity
Glycosylationi900 – 9001N-linked (GlcNAc...) Reviewed prediction
Glycosylationi921 – 9211N-linked (GlcNAc...) Reviewed prediction
Glycosylationi959 – 9591N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1330 – 13301N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1438 ↔ 1450 By similarity
Disulfide bondi1440 ↔ 1457 By similarity
Disulfide bondi1459 ↔ 1468 By similarity
Disulfide bondi1471 ↔ 1481 By similarity
Disulfide bondi1484 ↔ 1491 By similarity
Disulfide bondi1486 ↔ 1498 By similarity
Disulfide bondi1500 ↔ 1509 By similarity
Disulfide bondi1512 ↔ 1525 By similarity
Disulfide bondi1528 ↔ 1543 By similarity
Glycosylationi1529 – 15291N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1530 ↔ 1550 By similarity
Disulfide bondi1552 ↔ 1561 By similarity
Glycosylationi1555 – 15551N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1564 ↔ 1574 By similarity
Disulfide bondi1577 ↔ 1589 By similarity
Disulfide bondi1579 ↔ 1596 By similarity
Disulfide bondi1598 ↔ 1607 By similarity
Disulfide bondi1610 ↔ 1625 By similarity
Disulfide bondi1864 ↔ 1873 By similarity
Disulfide bondi1866 ↔ 1880 By similarity
Disulfide bondi1883 ↔ 1892 By similarity
Disulfide bondi1895 ↔ 1910 By similarity
Disulfide bondi1913 ↔ 1928 By similarity
Disulfide bondi1915 ↔ 1937 By similarity
Disulfide bondi1939 ↔ 1948 By similarity
Disulfide bondi1951 ↔ 1966 By similarity
Disulfide bondi1969 ↔ 1984 By similarity
Disulfide bondi1971 ↔ 1991 By similarity
Disulfide bondi1994 ↔ 2003 By similarity
Disulfide bondi2006 ↔ 2020 By similarity
Disulfide bondi2023 ↔ 2033 By similarity
Disulfide bondi2025 ↔ 2040 By similarity
Disulfide bondi2042 ↔ 2051 By similarity
Disulfide bondi2054 ↔ 2067 By similarity
Disulfide bondi2070 ↔ 2081 By similarity
Disulfide bondi2072 ↔ 2088 By similarity
Disulfide bondi2090 ↔ 2099 By similarity
Disulfide bondi2102 ↔ 2114 By similarity
Disulfide bondi2117 ↔ 2124 By similarity
Disulfide bondi2119 ↔ 2131 By similarity
Disulfide bondi2133 ↔ 2142 By similarity
Disulfide bondi2145 ↔ 2164 By similarity
Disulfide bondi2167 – 2167Interchain Inferred
Disulfide bondi2170 – 2170Interchain Inferred
Glycosylationi2196 – 21961N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2209 – 22091N-linked (GlcNAc...)1 Publication
Glycosylationi2303 – 23031N-linked (GlcNAc...)1 Publication
Glycosylationi2423 – 24231N-linked (GlcNAc...)1 Publication
Glycosylationi2501 – 25011N-linked (GlcNAc...)1 Publication
Glycosylationi2568 – 25681N-linked (GlcNAc...)1 Publication
Glycosylationi2707 – 27071N-linked (GlcNAc...)1 Publication
Disulfide bondi2899 ↔ 2929 By similarity
Disulfide bondi3090 ↔ 3115 By similarity
Glycosylationi3107 – 31071N-linked (GlcNAc...)1 Publication
Glycosylationi3209 – 32091N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3257 – 32571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3261 ↔ 3292 By similarity
Glycosylationi3287 – 32871N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3490 ↔ 3513 By similarity
Glycosylationi3626 – 36261N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3664 ↔ 3692 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO15230.
PaxDbiO15230.
PRIDEiO15230.

PTM databases

PhosphoSiteiO15230.

Expressioni

Tissue specificityi

Expressed in heart, lung, kidney, skeletal muscle, pancreas, retina and placenta. Little or no expression in brain and liver.

Gene expression databases

ArrayExpressiO15230.
BgeeiO15230.
CleanExiHS_LAMA5.
GenevestigatoriO15230.

Interactioni

Subunit structurei

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-5 is a subunit of laminin-10 (laminin-511), laminin-11 (laminin-521) and laminin-15 (laminin-523).

Protein-protein interaction databases

BioGridi110105. 13 interactions.
IntActiO15230. 11 interactions.
MINTiMINT-1183475.
STRINGi9606.ENSP00000252999.

Structurei

3D structure databases

ProteinModelPortaliO15230.
SMRiO15230. Positions 42-427.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 299259Laminin N-terminalAdd
BLAST
Domaini300 – 35859Laminin EGF-like 1Add
BLAST
Domaini359 – 42870Laminin EGF-like 2Add
BLAST
Domaini429 – 47446Laminin EGF-like 3Add
BLAST
Domaini494 – 54047Laminin EGF-like 4Add
BLAST
Domaini541 – 58646Laminin EGF-like 5Add
BLAST
Domaini587 – 63145Laminin EGF-like 6Add
BLAST
Domaini632 – 67645Laminin EGF-like 7Add
BLAST
Domaini677 – 72246Laminin EGF-like 8Add
BLAST
Domaini723 – 77553Laminin EGF-like 9Add
BLAST
Domaini776 – 82853Laminin EGF-like 10Add
BLAST
Domaini829 – 85022Laminin EGF-like 11; truncatedAdd
BLAST
Domaini1438 – 148346Laminin EGF-like 12Add
BLAST
Domaini1484 – 152744Laminin EGF-like 13Add
BLAST
Domaini1528 – 157649Laminin EGF-like 14Add
BLAST
Domaini1577 – 162751Laminin EGF-like 15Add
BLAST
Domaini1628 – 163710Laminin EGF-like 16; first part
Domaini1641 – 1830190Laminin IV type AAdd
BLAST
Domaini1831 – 186333Laminin EGF-like 16; second partAdd
BLAST
Domaini1864 – 191249Laminin EGF-like 17Add
BLAST
Domaini1913 – 196856Laminin EGF-like 18Add
BLAST
Domaini1969 – 202254Laminin EGF-like 19Add
BLAST
Domaini2023 – 206947Laminin EGF-like 20Add
BLAST
Domaini2070 – 211647Laminin EGF-like 21Add
BLAST
Domaini2117 – 216650Laminin EGF-like 22Add
BLAST
Domaini2736 – 2929194Laminin G-like 1Add
BLAST
Domaini2941 – 3115175Laminin G-like 2Add
BLAST
Domaini3124 – 3292169Laminin G-like 3Add
BLAST
Domaini3340 – 3513174Laminin G-like 4Add
BLAST
Domaini3520 – 3692173Laminin G-like 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni851 – 1437587Domain IV 1 (domain IV B)Add
BLAST
Regioni2167 – 2735569Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2203 – 222119 Reviewed predictionAdd
BLAST
Coiled coili2335 – 2466132 Reviewed predictionAdd
BLAST
Coiled coili2510 – 2670161 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1722 – 17243Cell attachment site Reviewed prediction
Motifi1838 – 18403Cell attachment site Reviewed prediction

Domaini

Domain G is globular and is part of the major cell-binding site located in the long arm of the laminin heterotrimer.

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG292643.
HOGENOMiHOG000231235.
HOVERGENiHBG052300.
InParanoidiO15230.
KOiK06240.
OMAiHTTGPRC.
PhylomeDBiO15230.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR008985. 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.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 19 hits.
PF02210. Laminin_G_2. 5 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 20 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
PROSITEiPS00022. EGF_1. 19 hits.
PS01186. EGF_2. 3 hits.
PS01248. EGF_LAM_1. 19 hits.
PS50027. EGF_LAM_2. 21 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O15230-1 [UniParc]FASTAAdd to Basket

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MAKRLCAGSA LCVRGPRGPA PLLLVGLALL GAARAREEAG GGFSLHPPYF     50
NLAEGARIAA SATCGEEAPA RGSPRPTEDL YCKLVGGPVA GGDPNQTIRG 100
QYCDICTAAN SNKAHPASNA IDGTERWWQS PPLSRGLEYN EVNVTLDLGQ 150
VFHVAYVLIK FANSPRPDLW VLERSMDFGR TYQPWQFFAS SKRDCLERFG 200
PQTLERITRD DAAICTTEYS RIVPLENGEI VVSLVNGRPG AMNFSYSPLL 250
REFTKATNVR LRFLRTNTLL GHLMGKALRD PTVTRRYYYS IKDISIGGRC 300
VCHGHADACD AKDPTDPFRL QCTCQHNTCG GTCDRCCPGF NQQPWKPATA 350
NSANECQSCN CYGHATDCYY DPEVDRRRAS QSLDGTYQGG GVCIDCQHHT 400
TGVNCERCLP GFYRSPNHPL DSPHVCRRCN CESDFTDGTC EDLTGRCYCR 450
PNFSGERCDV CAEGFTGFPS CYPTPSSSND TREQVLPAGQ IVNCDCSAAG 500
TQGNACRKDP RVGRCLCKPN FQGTHCELCA PGFYGPGCQP CQCSSPGVAD 550
DRCDPDTGQC RCRVGFEGAT CDRCAPGYFH FPLCQLCGCS PAGTLPEGCD 600
EAGRCLCQPE FAGPHCDRCR PGYHGFPNCQ ACTCDPRGAL DQLCGAGGLC 650
RCRPGYTGTA CQECSPGFHG FPSCVPCHCS AEGSLHAACD PRSGQCSCRP 700
RVTGLRCDTC VPGAYNFPYC EAGSCHPAGL APVDPALPEA QVPCMCRAHV 750
EGPSCDRCKP GFWGLSPSNP EGCTRCSCDL RGTLGGVAEC QPGTGQCFCK 800
PHVCGQACAS CKDGFFGLDQ ADYFGCRSCR CDIGGALGQS CEPRTGVCRC 850
RPNTQGPTCS EPARDHYLPD LHHLRLELEE AATPEGHAVR FGFNPLEFEN 900
FSWRGYAQMA PVQPRIVARL NLTSPDLFWL VFRYVNRGAM SVSGRVSVRE 950
EGRSATCANC TAQSQPVAFP PSTEPAFITV PQRGFGEPFV LNPGTWALRV 1000
EAEGVLLDYV VLLPSAYYEA ALLQLRVTEA CTYRPSAQQS GDNCLLYTHL 1050
PLDGFPSAAG LEALCRQDNS LPRPCPTEQL SPSHPPLITC TGSDVDVQLQ 1100
VAVPQPGRYA LVVEYANEDA RQEVGVAVHT PQRAPQQGLL SLHPCLYSTL 1150
CRGTARDTQD HLAVFHLDSE ASVRLTAEQA RFFLHGVTLV PIEEFSPEFV 1200
EPRVSCISSH GAFGPNSAAC LPSRFPKPPQ PIILRDCQVI PLPPGLPLTH 1250
AQDLTPAMSP AGPRPRPPTA VDPDAEPTLL REPQATVVFT THVPTLGRYA 1300
FLLHGYQPAH PTFPVEVLIN AGRVWQGHAN ASFCPHGYGC RTLVVCEGQA 1350
LLDVTHSELT VTVRVPKGRW LWLDYVLVVP ENVYSFGYLR EEPLDKSYDF 1400
ISHCAAQGYH ISPSSSSLFC RNAAASLSLF YNNGARPCGC HEVGATGPTC 1450
EPFGGQCPCH AHVIGRDCSR CATGYWGFPN CRPCDCGARL CDELTGQCIC 1500
PPRTIPPDCL LCQPQTFGCH PLVGCEECNC SGPGIQELTD PTCDTDSGQC 1550
KCRPNVTGRR CDTCSPGFHG YPRCRPCDCH EAGTAPGVCD PLTGQCYCKE 1600
NVQGPKCDQC SLGTFSLDAA NPKGCTRCFC FGATERCRSS SYTRQEFVDM 1650
EGWVLLSTDR QVVPHERQPG TEMLRADLRH VPEAVPEAFP ELYWQAPPSY 1700
LGDRVSSYGG TLRYELHSET QRGDVFVPME SRPDVVLQGN QMSITFLEPA 1750
YPTPGHVHRG QLQLVEGNFR HTETRNTVSR EELMMVLASL EQLQIRALFS 1800
QISSAVFLRR VALEVASPAG QGALASNVEL CLCPASYRGD SCQECAPGFY 1850
RDVKGLFLGR CVPCQCHGHS DRCLPGSGVC VDCQHNTEGA HCERCQAGFV 1900
SSRDDPSAPC VSCPCPLSVP SNNFAEGCVL RGGRTQCLCK PGYAGASCER 1950
CAPGFFGNPL VLGSSCQPCD CSGNGDPNLL FSDCDPLTGA CRGCLRHTTG 2000
PRCEICAPGF YGNALLPGNC TRCDCTPCGT EACDPHSGHC LCKAGVTGRR 2050
CDRCQEGHFG FDGCGGCRPC ACGPAAEGSE CHPQSGQCHC RPGTMGPQCR 2100
ECAPGYWGLP EQGCRRCQCP GGRCDPHTGR CNCPPGLSGE RCDTCSQQHQ 2150
VPVPGGPVGH SIHCEVCDHC VVLLLDDLER AGALLPAIHE QLRGINASSM 2200
AWARLHRLNA SIADLQSQLR SPLGPRHETA QQLEVLEQQS TSLGQDARRL 2250
GGQAVGTRDQ ASQLLAGTEA TLGHAKTLLA AIRAVDRTLS ELMSQTGHLG 2300
LANASAPSGE QLLRTLAEVE RLLWEMRARD LGAPQAAAEA ELAAAQRLLA 2350
RVQEQLSSLW EENQALATQT RDRLAQHEAG LMDLREALNR AVDATREAQE 2400
LNSRNQERLE EALQRKQELS RDNATLQATL HAARDTLASV FRLLHSLDQA 2450
KEELERLAAS LDGARTPLLQ RMQTFSPAGS KLRLVEAAEA HAQQLGQLAL 2500
NLSSIILDVN QDRLTQRAIE ASNAYSRILQ AVQAAEDAAG QALQQADHTW 2550
ATVVRQGLVD RAQQLLANST ALEEAMLQEQ QRLGLVWAAL QGARTQLRDV 2600
RAKKDQLEAH IQAAQAMLAM DTDETSKKIA HAKAVAAEAQ DTATRVQSQL 2650
QAMQENVERW QGQYEGLRGQ DLGQAVLDAG HSVSTLEKTL PQLLAKLSIL 2700
ENRGVHNASL ALSASIGRVR ELIAQARGAA SKVKVPMKFN GRSGVQLRTP 2750
RDLADLAAYT ALKFYLQGPE PEPGQGTEDR FVMYMGSRQA TGDYMGVSLR 2800
DKKVHWVYQL GEAGPAVLSI DEDIGEQFAA VSLDRTLQFG HMSVTVERQM 2850
IQETKGDTVA PGAEGLLNLR PDDFVFYVGG YPSTFTPPPL LRFPGYRGCI 2900
EMDTLNEEVV SLYNFERTFQ LDTAVDRPCA RSKSTGDPWL TDGSYLDGTG 2950
FARISFDSQI STTKRFEQEL RLVSYSGVLF FLKQQSQFLC LAVQEGSLVL 3000
LYDFGAGLKK AVPLQPPPPL TSASKAIQVF LLGGSRKRVL VRVERATVYS 3050
VEQDNDLELA DAYYLGGVPP DQLPPSLRRL FPTGGSVRGC VKGIKALGKY 3100
VDLKRLNTTG VSAGCTADLL VGRAMTFHGH GFLRLALSNV APLTGNVYSG 3150
FGFHSAQDSA LLYYRASPDG LCQVSLQQGR VSLQLLRTEV KTQAGFADGA 3200
PHYVAFYSNA TGVWLYVDDQ LQQMKPHRGP PPELQPQPEG PPRLLLGGLP 3250
ESGTIYNFSG CISNVFVQRL LGPQRVFDLQ QNLGSVNVST GCAPALQAQT 3300
PGLGPRGLQA TARKASRRSR QPARHPACML PPHLRTTRDS YQFGGSLSSH 3350
LEFVGILARH RNWPSLSMHV LPRSSRGLLL FTARLRPGSP SLALFLSNGH 3400
FVAQMEGLGT RLRAQSRQRS RPGRWHKVSV RWEKNRILLV TDGARAWSQE 3450
GPHRQHQGAE HPQPHTLFVG GLPASSHSSK LPVTVGFSGC VKRLRLHGRP 3500
LGAPTRMAGV TPCILGPLEA GLFFPGSGGV ITLDLPGATL PDVGLELEVR 3550
PLAVTGLIFH LGQARTPPYL QLQVTEKQVL LRADDGAGEF STSVTRPSVL 3600
CDGQWHRLAV MKSGNVLRLE VDAQSNHTVG PLLAAAAGAP APLYLGGLPE 3650
PMAVQPWPPA YCGCMRRLAV NRSPVAMTRS VEVHGAVGAS GCPAA 3695
Length:3,695
Mass (Da):399,737
Last modified:January 11, 2011 - v8
Checksum:iB13C479B55282E3C
GO

Sequence cautioni

The sequence CAC22310.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti401 – 4011T → A.1 Publication
Corresponds to variant rs4925229 [ dbSNP | Ensembl ].
VAR_047887
Natural varianti889 – 8891V → M.1 Publication
Corresponds to variant rs6062223 [ dbSNP | Ensembl ].
VAR_030847
Natural varianti1258 – 12581M → T.1 Publication
Corresponds to variant rs3810548 [ dbSNP | Ensembl ].
VAR_030848
Natural varianti1367 – 13671K → E.2 Publications
Corresponds to variant rs2427286 [ dbSNP | Ensembl ].
VAR_030849
Natural varianti1434 – 14341G → A.
Corresponds to variant rs17750870 [ dbSNP | Ensembl ].
VAR_030850
Natural varianti1667 – 16671R → W.
Corresponds to variant rs13039398 [ dbSNP | Ensembl ].
VAR_030851
Natural varianti1671 – 16711T → M.
Corresponds to variant rs944893 [ dbSNP | Ensembl ].
VAR_047888
Natural varianti1717 – 17171H → Y.
Corresponds to variant rs875379 [ dbSNP | Ensembl ].
VAR_030852
Natural varianti1807 – 18071F → S.2 Publications
Corresponds to variant rs2427284 [ dbSNP | Ensembl ].
VAR_030853
Natural varianti1900 – 19001V → M.1 Publication
Corresponds to variant rs2427283 [ dbSNP | Ensembl ].
VAR_030854
Natural varianti1908 – 19081A → T.
Corresponds to variant rs11698080 [ dbSNP | Ensembl ].
VAR_030855
Natural varianti2036 – 20361H → R.
Corresponds to variant rs6143021 [ dbSNP | Ensembl ].
VAR_030856
Natural varianti2053 – 20531R → H.
Corresponds to variant rs3737137 [ dbSNP | Ensembl ].
VAR_030857
Natural varianti2062 – 20621D → N.2 Publications
Corresponds to variant rs2274934 [ dbSNP | Ensembl ].
VAR_030858
Natural varianti2226 – 22261R → H.
Corresponds to variant rs2297587 [ dbSNP | Ensembl ].
VAR_030859
Natural varianti3079 – 30791R → W.3 Publications
Corresponds to variant rs944895 [ dbSNP | Ensembl ].
VAR_030860

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti956 – 9561T → A in AAM12527. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF443072 mRNA. Translation: AAM12527.1.
AL354836 Genomic DNA. Translation: CAC22310.1. Sequence problems.
AB067494 mRNA. Translation: BAB67800.1.
AB011105 mRNA. Translation: BAA25459.1.
Z95636 mRNA. Translation: CAB09137.1.
CCDSiCCDS33502.1.
RefSeqiNP_005551.3. NM_005560.4.
UniGeneiHs.473256.

Genome annotation databases

EnsembliENST00000252999; ENSP00000252999; ENSG00000130702.
GeneIDi3911.
KEGGihsa:3911.
UCSCiuc002ycq.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF443072 mRNA. Translation: AAM12527.1 .
AL354836 Genomic DNA. Translation: CAC22310.1 . Sequence problems.
AB067494 mRNA. Translation: BAB67800.1 .
AB011105 mRNA. Translation: BAA25459.1 .
Z95636 mRNA. Translation: CAB09137.1 .
CCDSi CCDS33502.1.
RefSeqi NP_005551.3. NM_005560.4.
UniGenei Hs.473256.

3D structure databases

ProteinModelPortali O15230.
SMRi O15230. Positions 42-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110105. 13 interactions.
IntActi O15230. 11 interactions.
MINTi MINT-1183475.
STRINGi 9606.ENSP00000252999.

Chemistry

ChEMBLi CHEMBL2364187.
DrugBanki DB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSitei O15230.

Proteomic databases

MaxQBi O15230.
PaxDbi O15230.
PRIDEi O15230.

Protocols and materials databases

DNASUi 3911.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252999 ; ENSP00000252999 ; ENSG00000130702 .
GeneIDi 3911.
KEGGi hsa:3911.
UCSCi uc002ycq.3. human.

Organism-specific databases

CTDi 3911.
GeneCardsi GC20M060883.
H-InvDB HIX0015978.
HGNCi HGNC:6485. LAMA5.
MIMi 601033. gene.
neXtProti NX_O15230.
PharmGKBi PA30274.
HUGEi Search...
Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292643.
HOGENOMi HOG000231235.
HOVERGENi HBG052300.
InParanoidi O15230.
KOi K06240.
OMAi HTTGPRC.
PhylomeDBi O15230.
TreeFami TF335359.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.

Miscellaneous databases

ChiTaRSi LAMA5. human.
GeneWikii Laminin,_alpha_5.
GenomeRNAii 3911.
NextBioi 15363.
PROi O15230.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15230.
Bgeei O15230.
CleanExi HS_LAMA5.
Genevestigatori O15230.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
InterProi 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.
[Graphical view ]
Pfami PF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 19 hits.
PF02210. Laminin_G_2. 5 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 20 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 5 hits.
PROSITEi PS00022. EGF_1. 19 hits.
PS01186. EGF_2. 3 hits.
PS01248. EGF_LAM_1. 19 hits.
PS50027. EGF_LAM_2. 21 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Recombinant human laminin-10 (alpha5beta1gamma1). Production, purification, and migration-promoting activity on vascular endothelial cells."
    Doi M., Thyboll J., Kortesmaa J., Jansson K., Iivanainen A., Parvardeh M., Timpl R., Hedin U., Swedenborg J., Tryggvason K.
    J. Biol. Chem. 277:12741-12748(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-401; THR-1258; GLU-1367; SER-1807; MET-1900; ASN-2062 AND TRP-3079.
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1934, VARIANTS MET-889; GLU-1367 AND SER-1807.
    Tissue: Brain.
  4. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2051-3695, VARIANTS ASN-2062 AND TRP-3079.
    Tissue: Brain.
  5. "Tissue-specific expression of the human laminin alpha5-chain, and mapping of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome 2 near the locus for the ragged (Ra) mutation."
    Durkin M.E., Loechel F., Mattei M.-G., Gilpin B.J., Albrechtsen R., Wewer U.M.
    FEBS Lett. 411:296-300(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2743-3695, VARIANT TRP-3079.
    Tissue: Placenta.
  6. "Laminin expression in adult and developing retinae: evidence of two novel CNS laminins."
    Libby R.T., Champliaud M.-F., Claudepierre T., Xu Y., Gibbons E.P., Koch M., Burgeson R.E., Hunter D.D., Brunken W.J.
    J. Neurosci. 20:6517-6528(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: EXPRESSION IN RETINA.
  7. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2209; ASN-2303; ASN-2423; ASN-2501; ASN-2568; ASN-2707 AND ASN-3107.
    Tissue: Liver.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLAMA5_HUMAN
AccessioniPrimary (citable) accession number: O15230
Secondary accession number(s): Q8TDF8, Q8WZA7, Q9H1P1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 151 of the entry and version 8 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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