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O15230

- LAMA5_HUMAN

UniProt

O15230 - LAMA5_HUMAN

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Protein

Laminin subunit alpha-5

Gene

LAMA5

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 matrix Source: UniProtKB
  4. extracellular region Source: Reactome
  5. extracellular space Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProtKB
  7. laminin-10 complex Source: UniProtKB
  8. laminin-11 complex Source: BHF-UCL
  9. laminin-1 complex Source: InterPro
  10. laminin-5 complex Source: Ensembl
  11. 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 – 3535Sequence AnalysisAdd
BLAST
Chaini36 – 36953660Laminin subunit alpha-5PRO_0000017062Add
BLAST

Amino acid modifications

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

BgeeiO15230.
CleanExiHS_LAMA5.
ExpressionAtlasiO15230. baseline and differential.
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. 16 interactions.
IntActiO15230. 14 interactions.
MINTiMINT-1183475.
STRINGi9606.ENSP00000252999.

Structurei

3D structure databases

ProteinModelPortaliO15230.
SMRiO15230. Positions 42-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 299259Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini300 – 35859Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini359 – 42870Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini429 – 47446Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini494 – 54047Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini541 – 58646Laminin EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini587 – 63145Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini632 – 67645Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini677 – 72246Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini723 – 77553Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini776 – 82853Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini829 – 85022Laminin EGF-like 11; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini1438 – 148346Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1484 – 152744Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini1528 – 157649Laminin EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini1577 – 162751Laminin EGF-like 15PROSITE-ProRule annotationAdd
BLAST
Domaini1628 – 163710Laminin EGF-like 16; first partPROSITE-ProRule annotation
Domaini1641 – 1830190Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini1831 – 186333Laminin EGF-like 16; second partPROSITE-ProRule annotationAdd
BLAST
Domaini1864 – 191249Laminin EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini1913 – 196856Laminin EGF-like 18PROSITE-ProRule annotationAdd
BLAST
Domaini1969 – 202254Laminin EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini2023 – 206947Laminin EGF-like 20PROSITE-ProRule annotationAdd
BLAST
Domaini2070 – 211647Laminin EGF-like 21PROSITE-ProRule annotationAdd
BLAST
Domaini2117 – 216650Laminin EGF-like 22PROSITE-ProRule annotationAdd
BLAST
Domaini2736 – 2929194Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini2941 – 3115175Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini3124 – 3292169Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini3340 – 3513174Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini3520 – 3692173Laminin G-like 5PROSITE-ProRule annotationAdd
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 – 222119Sequence AnalysisAdd
BLAST
Coiled coili2335 – 2466132Sequence AnalysisAdd
BLAST
Coiled coili2510 – 2670161Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1722 – 17243Cell attachment siteSequence Analysis
Motifi1838 – 18403Cell attachment siteSequence Analysis

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

Contains 22 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 5 laminin G-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG292643.
GeneTreeiENSGT00760000118860.
HOGENOMiHOG000231235.
HOVERGENiHBG052300.
InParanoidiO15230.
KOiK06240.
OMAiHTTGPRC.
PhylomeDBiO15230.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
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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        10         20         30         40         50
MAKRLCAGSA LCVRGPRGPA PLLLVGLALL GAARAREEAG GGFSLHPPYF
60 70 80 90 100
NLAEGARIAA SATCGEEAPA RGSPRPTEDL YCKLVGGPVA GGDPNQTIRG
110 120 130 140 150
QYCDICTAAN SNKAHPASNA IDGTERWWQS PPLSRGLEYN EVNVTLDLGQ
160 170 180 190 200
VFHVAYVLIK FANSPRPDLW VLERSMDFGR TYQPWQFFAS SKRDCLERFG
210 220 230 240 250
PQTLERITRD DAAICTTEYS RIVPLENGEI VVSLVNGRPG AMNFSYSPLL
260 270 280 290 300
REFTKATNVR LRFLRTNTLL GHLMGKALRD PTVTRRYYYS IKDISIGGRC
310 320 330 340 350
VCHGHADACD AKDPTDPFRL QCTCQHNTCG GTCDRCCPGF NQQPWKPATA
360 370 380 390 400
NSANECQSCN CYGHATDCYY DPEVDRRRAS QSLDGTYQGG GVCIDCQHHT
410 420 430 440 450
TGVNCERCLP GFYRSPNHPL DSPHVCRRCN CESDFTDGTC EDLTGRCYCR
460 470 480 490 500
PNFSGERCDV CAEGFTGFPS CYPTPSSSND TREQVLPAGQ IVNCDCSAAG
510 520 530 540 550
TQGNACRKDP RVGRCLCKPN FQGTHCELCA PGFYGPGCQP CQCSSPGVAD
560 570 580 590 600
DRCDPDTGQC RCRVGFEGAT CDRCAPGYFH FPLCQLCGCS PAGTLPEGCD
610 620 630 640 650
EAGRCLCQPE FAGPHCDRCR PGYHGFPNCQ ACTCDPRGAL DQLCGAGGLC
660 670 680 690 700
RCRPGYTGTA CQECSPGFHG FPSCVPCHCS AEGSLHAACD PRSGQCSCRP
710 720 730 740 750
RVTGLRCDTC VPGAYNFPYC EAGSCHPAGL APVDPALPEA QVPCMCRAHV
760 770 780 790 800
EGPSCDRCKP GFWGLSPSNP EGCTRCSCDL RGTLGGVAEC QPGTGQCFCK
810 820 830 840 850
PHVCGQACAS CKDGFFGLDQ ADYFGCRSCR CDIGGALGQS CEPRTGVCRC
860 870 880 890 900
RPNTQGPTCS EPARDHYLPD LHHLRLELEE AATPEGHAVR FGFNPLEFEN
910 920 930 940 950
FSWRGYAQMA PVQPRIVARL NLTSPDLFWL VFRYVNRGAM SVSGRVSVRE
960 970 980 990 1000
EGRSATCANC TAQSQPVAFP PSTEPAFITV PQRGFGEPFV LNPGTWALRV
1010 1020 1030 1040 1050
EAEGVLLDYV VLLPSAYYEA ALLQLRVTEA CTYRPSAQQS GDNCLLYTHL
1060 1070 1080 1090 1100
PLDGFPSAAG LEALCRQDNS LPRPCPTEQL SPSHPPLITC TGSDVDVQLQ
1110 1120 1130 1140 1150
VAVPQPGRYA LVVEYANEDA RQEVGVAVHT PQRAPQQGLL SLHPCLYSTL
1160 1170 1180 1190 1200
CRGTARDTQD HLAVFHLDSE ASVRLTAEQA RFFLHGVTLV PIEEFSPEFV
1210 1220 1230 1240 1250
EPRVSCISSH GAFGPNSAAC LPSRFPKPPQ PIILRDCQVI PLPPGLPLTH
1260 1270 1280 1290 1300
AQDLTPAMSP AGPRPRPPTA VDPDAEPTLL REPQATVVFT THVPTLGRYA
1310 1320 1330 1340 1350
FLLHGYQPAH PTFPVEVLIN AGRVWQGHAN ASFCPHGYGC RTLVVCEGQA
1360 1370 1380 1390 1400
LLDVTHSELT VTVRVPKGRW LWLDYVLVVP ENVYSFGYLR EEPLDKSYDF
1410 1420 1430 1440 1450
ISHCAAQGYH ISPSSSSLFC RNAAASLSLF YNNGARPCGC HEVGATGPTC
1460 1470 1480 1490 1500
EPFGGQCPCH AHVIGRDCSR CATGYWGFPN CRPCDCGARL CDELTGQCIC
1510 1520 1530 1540 1550
PPRTIPPDCL LCQPQTFGCH PLVGCEECNC SGPGIQELTD PTCDTDSGQC
1560 1570 1580 1590 1600
KCRPNVTGRR CDTCSPGFHG YPRCRPCDCH EAGTAPGVCD PLTGQCYCKE
1610 1620 1630 1640 1650
NVQGPKCDQC SLGTFSLDAA NPKGCTRCFC FGATERCRSS SYTRQEFVDM
1660 1670 1680 1690 1700
EGWVLLSTDR QVVPHERQPG TEMLRADLRH VPEAVPEAFP ELYWQAPPSY
1710 1720 1730 1740 1750
LGDRVSSYGG TLRYELHSET QRGDVFVPME SRPDVVLQGN QMSITFLEPA
1760 1770 1780 1790 1800
YPTPGHVHRG QLQLVEGNFR HTETRNTVSR EELMMVLASL EQLQIRALFS
1810 1820 1830 1840 1850
QISSAVFLRR VALEVASPAG QGALASNVEL CLCPASYRGD SCQECAPGFY
1860 1870 1880 1890 1900
RDVKGLFLGR CVPCQCHGHS DRCLPGSGVC VDCQHNTEGA HCERCQAGFV
1910 1920 1930 1940 1950
SSRDDPSAPC VSCPCPLSVP SNNFAEGCVL RGGRTQCLCK PGYAGASCER
1960 1970 1980 1990 2000
CAPGFFGNPL VLGSSCQPCD CSGNGDPNLL FSDCDPLTGA CRGCLRHTTG
2010 2020 2030 2040 2050
PRCEICAPGF YGNALLPGNC TRCDCTPCGT EACDPHSGHC LCKAGVTGRR
2060 2070 2080 2090 2100
CDRCQEGHFG FDGCGGCRPC ACGPAAEGSE CHPQSGQCHC RPGTMGPQCR
2110 2120 2130 2140 2150
ECAPGYWGLP EQGCRRCQCP GGRCDPHTGR CNCPPGLSGE RCDTCSQQHQ
2160 2170 2180 2190 2200
VPVPGGPVGH SIHCEVCDHC VVLLLDDLER AGALLPAIHE QLRGINASSM
2210 2220 2230 2240 2250
AWARLHRLNA SIADLQSQLR SPLGPRHETA QQLEVLEQQS TSLGQDARRL
2260 2270 2280 2290 2300
GGQAVGTRDQ ASQLLAGTEA TLGHAKTLLA AIRAVDRTLS ELMSQTGHLG
2310 2320 2330 2340 2350
LANASAPSGE QLLRTLAEVE RLLWEMRARD LGAPQAAAEA ELAAAQRLLA
2360 2370 2380 2390 2400
RVQEQLSSLW EENQALATQT RDRLAQHEAG LMDLREALNR AVDATREAQE
2410 2420 2430 2440 2450
LNSRNQERLE EALQRKQELS RDNATLQATL HAARDTLASV FRLLHSLDQA
2460 2470 2480 2490 2500
KEELERLAAS LDGARTPLLQ RMQTFSPAGS KLRLVEAAEA HAQQLGQLAL
2510 2520 2530 2540 2550
NLSSIILDVN QDRLTQRAIE ASNAYSRILQ AVQAAEDAAG QALQQADHTW
2560 2570 2580 2590 2600
ATVVRQGLVD RAQQLLANST ALEEAMLQEQ QRLGLVWAAL QGARTQLRDV
2610 2620 2630 2640 2650
RAKKDQLEAH IQAAQAMLAM DTDETSKKIA HAKAVAAEAQ DTATRVQSQL
2660 2670 2680 2690 2700
QAMQENVERW QGQYEGLRGQ DLGQAVLDAG HSVSTLEKTL PQLLAKLSIL
2710 2720 2730 2740 2750
ENRGVHNASL ALSASIGRVR ELIAQARGAA SKVKVPMKFN GRSGVQLRTP
2760 2770 2780 2790 2800
RDLADLAAYT ALKFYLQGPE PEPGQGTEDR FVMYMGSRQA TGDYMGVSLR
2810 2820 2830 2840 2850
DKKVHWVYQL GEAGPAVLSI DEDIGEQFAA VSLDRTLQFG HMSVTVERQM
2860 2870 2880 2890 2900
IQETKGDTVA PGAEGLLNLR PDDFVFYVGG YPSTFTPPPL LRFPGYRGCI
2910 2920 2930 2940 2950
EMDTLNEEVV SLYNFERTFQ LDTAVDRPCA RSKSTGDPWL TDGSYLDGTG
2960 2970 2980 2990 3000
FARISFDSQI STTKRFEQEL RLVSYSGVLF FLKQQSQFLC LAVQEGSLVL
3010 3020 3030 3040 3050
LYDFGAGLKK AVPLQPPPPL TSASKAIQVF LLGGSRKRVL VRVERATVYS
3060 3070 3080 3090 3100
VEQDNDLELA DAYYLGGVPP DQLPPSLRRL FPTGGSVRGC VKGIKALGKY
3110 3120 3130 3140 3150
VDLKRLNTTG VSAGCTADLL VGRAMTFHGH GFLRLALSNV APLTGNVYSG
3160 3170 3180 3190 3200
FGFHSAQDSA LLYYRASPDG LCQVSLQQGR VSLQLLRTEV KTQAGFADGA
3210 3220 3230 3240 3250
PHYVAFYSNA TGVWLYVDDQ LQQMKPHRGP PPELQPQPEG PPRLLLGGLP
3260 3270 3280 3290 3300
ESGTIYNFSG CISNVFVQRL LGPQRVFDLQ QNLGSVNVST GCAPALQAQT
3310 3320 3330 3340 3350
PGLGPRGLQA TARKASRRSR QPARHPACML PPHLRTTRDS YQFGGSLSSH
3360 3370 3380 3390 3400
LEFVGILARH RNWPSLSMHV LPRSSRGLLL FTARLRPGSP SLALFLSNGH
3410 3420 3430 3440 3450
FVAQMEGLGT RLRAQSRQRS RPGRWHKVSV RWEKNRILLV TDGARAWSQE
3460 3470 3480 3490 3500
GPHRQHQGAE HPQPHTLFVG GLPASSHSSK LPVTVGFSGC VKRLRLHGRP
3510 3520 3530 3540 3550
LGAPTRMAGV TPCILGPLEA GLFFPGSGGV ITLDLPGATL PDVGLELEVR
3560 3570 3580 3590 3600
PLAVTGLIFH LGQARTPPYL QLQVTEKQVL LRADDGAGEF STSVTRPSVL
3610 3620 3630 3640 3650
CDGQWHRLAV MKSGNVLRLE VDAQSNHTVG PLLAAAAGAP APLYLGGLPE
3660 3670 3680 3690
PMAVQPWPPA YCGCMRRLAV NRSPVAMTRS VEVHGAVGAS GCPAA
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. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti956 – 9561T → A in AAM12527. (PubMed:11821406)Curated

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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 16 interactions.
IntActi O15230. 14 interactions.
MINTi MINT-1183475.
STRINGi 9606.ENSP00000252999.

Chemistry

ChEMBLi CHEMBL2364187.

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.
GeneTreei ENSGT00760000118860.
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

Bgeei O15230.
CleanExi HS_LAMA5.
ExpressionAtlasi O15230. baseline and differential.
Genevestigatori O15230.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
InterProi IPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
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: November 26, 2014
This is version 154 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