UniProtKB - P02469 (LAMB1_MOUSE)
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Protein
Laminin subunit beta-1
Gene
Lamb1
Organism
Mus musculus (Mouse)
Status
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. Involved in the organization of the laminar architecture of the cerebral cortex (By similarity). It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons (By similarity). Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface (By similarity).By similarity
GO - Molecular functioni
- enzyme binding Source: MGI
- extracellular matrix structural constituent Source: HGNC
- glycosphingolipid binding Source: MGI
- integrin binding Source: MGI
GO - Biological processi
- cell migration Source: MGI
- embryo implantation Source: MGI
- learning or memory Source: UniProtKB
- negative regulation of cell adhesion Source: UniProtKB
- neuronal-glial interaction involved in cerebral cortex radial glia guided migration Source: MGI
- neuron projection development Source: MGI
- odontogenesis Source: HGNC
- positive regulation of cell migration Source: HGNC
- substrate adhesion-dependent cell spreading Source: MGI
Keywordsi
Biological process | Cell adhesion |
Enzyme and pathway databases
Reactomei | R-MMU-3000157 Laminin interactions R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-MMU-8874081 MET activates PTK2 signaling R-MMU-8957275 Post-translational protein phosphorylation |
Names & Taxonomyi
Protein namesi | Recommended name: Laminin subunit beta-1Alternative name(s): 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 namesi | Name:Lamb1 Synonyms:Lamb-1, Lamb1-1 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:96743 Lamb1 |
Subcellular locationi
Keywords - Cellular componenti
Basement membrane, Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 21 | Add BLAST | 21 | |
ChainiPRO_0000017066 | 22 – 1786 | Laminin subunit beta-1Add BLAST | 1765 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 120 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 250 | PhosphoserineCombined sources | 1 | |
Disulfide bondi | 271 ↔ 280 | PROSITE-ProRule annotation | ||
Disulfide bondi | 273 ↔ 298 | PROSITE-ProRule annotation | ||
Disulfide bondi | 300 ↔ 309 | PROSITE-ProRule annotation | ||
Disulfide bondi | 312 ↔ 332 | PROSITE-ProRule annotation | ||
Disulfide bondi | 335 ↔ 344 | PROSITE-ProRule annotation | ||
Disulfide bondi | 337 ↔ 362 | PROSITE-ProRule annotation | ||
Glycosylationi | 356 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 365 ↔ 374 | PROSITE-ProRule annotation | ||
Disulfide bondi | 377 ↔ 395 | PROSITE-ProRule annotation | ||
Disulfide bondi | 398 ↔ 411 | PROSITE-ProRule annotation | ||
Disulfide bondi | 400 ↔ 426 | PROSITE-ProRule annotation | ||
Disulfide bondi | 428 ↔ 437 | PROSITE-ProRule annotation | ||
Disulfide bondi | 440 ↔ 455 | PROSITE-ProRule annotation | ||
Disulfide bondi | 458 ↔ 472 | PROSITE-ProRule annotation | ||
Disulfide bondi | 460 ↔ 479 | PROSITE-ProRule annotation | ||
Disulfide bondi | 481 ↔ 490 | PROSITE-ProRule annotation | ||
Disulfide bondi | 493 ↔ 507 | PROSITE-ProRule annotation | ||
Disulfide bondi | 510 ↔ 522 | PROSITE-ProRule annotation | ||
Disulfide bondi | 512 ↔ 529 | PROSITE-ProRule annotation | ||
Glycosylationi | 519 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 531 ↔ 540 | PROSITE-ProRule annotation | ||
Glycosylationi | 677 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 773 ↔ 785 | PROSITE-ProRule annotation | ||
Disulfide bondi | 775 ↔ 792 | PROSITE-ProRule annotation | ||
Disulfide bondi | 794 ↔ 803 | PROSITE-ProRule annotation | ||
Disulfide bondi | 806 ↔ 818 | PROSITE-ProRule annotation | ||
Disulfide bondi | 821 ↔ 833 | PROSITE-ProRule annotation | ||
Disulfide bondi | 823 ↔ 840 | PROSITE-ProRule annotation | ||
Disulfide bondi | 842 ↔ 851 | PROSITE-ProRule annotation | ||
Disulfide bondi | 854 ↔ 864 | PROSITE-ProRule annotation | ||
Disulfide bondi | 867 ↔ 876 | PROSITE-ProRule annotation | ||
Disulfide bondi | 869 ↔ 883 | PROSITE-ProRule annotation | ||
Disulfide bondi | 886 ↔ 895 | PROSITE-ProRule annotation | ||
Disulfide bondi | 898 ↔ 914 | PROSITE-ProRule annotation | ||
Disulfide bondi | 917 ↔ 933 | PROSITE-ProRule annotation | ||
Disulfide bondi | 919 ↔ 944 | PROSITE-ProRule annotation | ||
Disulfide bondi | 946 ↔ 955 | PROSITE-ProRule annotation | ||
Disulfide bondi | 958 ↔ 973 | PROSITE-ProRule annotation | ||
Disulfide bondi | 976 ↔ 990 | PROSITE-ProRule annotation | ||
Disulfide bondi | 978 ↔ 997 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1000 ↔ 1009 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1012 ↔ 1025 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1028 ↔ 1040 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1030 ↔ 1054 | PROSITE-ProRule annotation | ||
Glycosylationi | 1041 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1056 ↔ 1065 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1068 ↔ 1081 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1084 ↔ 1096 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1086 ↔ 1103 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1105 ↔ 1114 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1117 ↔ 1129 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1132 ↔ 1144 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1134 ↔ 1151 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1153 ↔ 1162 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1165 ↔ 1176 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1179 | InterchainCurated | ||
Disulfide bondi | 1182 | InterchainCurated | ||
Glycosylationi | 1195 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1279 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 1336 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 1343 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 1487 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 1496 | PhosphoserineBy similarity | 1 | |
Glycosylationi | 1542 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1643 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 1666 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 1785 | InterchainCurated |
Keywords - PTMi
Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
MaxQBi | P02469 |
PaxDbi | P02469 |
PeptideAtlasi | P02469 |
PRIDEi | P02469 |
PTM databases
iPTMneti | P02469 |
PhosphoSitePlusi | P02469 |
Expressioni
Tissue specificityi
Widely expressed in the embryo. High levels are detected in the cerebellar basement membrane, at postnatal day 7.1 Publication
Gene expression databases
Bgeei | ENSMUSG00000002900 |
CleanExi | MM_LAMB1-1 |
ExpressionAtlasi | P02469 baseline and differential |
Genevisiblei | P02469 MM |
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. Beta-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213).
Binary interactionsi
GO - Molecular functioni
- enzyme binding Source: MGI
- integrin binding Source: MGI
Protein-protein interaction databases
BioGridi | 2011014 interactors. |
IntActi | P02469 7 interactors. |
MINTi | P02469 |
STRINGi | 10090.ENSMUSP00000002979 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Helixi | 30 – 32 | Combined sources | 3 | |
Beta strandi | 40 – 43 | Combined sources | 4 | |
Helixi | 47 – 49 | Combined sources | 3 | |
Beta strandi | 58 – 60 | Combined sources | 3 | |
Beta strandi | 62 – 67 | Combined sources | 6 | |
Beta strandi | 69 – 72 | Combined sources | 4 | |
Beta strandi | 74 – 79 | Combined sources | 6 | |
Turni | 87 – 89 | Combined sources | 3 | |
Helixi | 96 – 98 | Combined sources | 3 | |
Beta strandi | 122 – 142 | Combined sources | 21 | |
Beta strandi | 146 – 155 | Combined sources | 10 | |
Beta strandi | 161 – 169 | Combined sources | 9 | |
Turni | 170 – 172 | Combined sources | 3 | |
Beta strandi | 173 – 177 | Combined sources | 5 | |
Turni | 200 – 202 | Combined sources | 3 | |
Beta strandi | 204 – 210 | Combined sources | 7 | |
Beta strandi | 212 – 214 | Combined sources | 3 | |
Helixi | 222 – 228 | Combined sources | 7 | |
Beta strandi | 229 – 239 | Combined sources | 11 | |
Helixi | 252 – 255 | Combined sources | 4 | |
Beta strandi | 261 – 270 | Combined sources | 10 | |
Beta strandi | 304 – 309 | Combined sources | 6 | |
Beta strandi | 342 – 346 | Combined sources | 5 | |
Helixi | 348 – 353 | Combined sources | 6 | |
Beta strandi | 360 – 364 | Combined sources | 5 | |
Beta strandi | 369 – 371 | Combined sources | 3 | |
Beta strandi | 381 – 383 | Combined sources | 3 | |
Beta strandi | 385 – 387 | Combined sources | 3 | |
Beta strandi | 395 – 397 | Combined sources | 3 | |
Turni | 402 – 404 | Combined sources | 3 | |
Helixi | 407 – 409 | Combined sources | 3 | |
Helixi | 417 – 419 | Combined sources | 3 | |
Turni | 434 – 437 | Combined sources | 4 | |
Beta strandi | 454 – 457 | Combined sources | 4 | |
Turni | 462 – 464 | Combined sources | 3 | |
Turni | 474 – 476 | Combined sources | 3 | |
Turni | 488 – 490 | Combined sources | 3 | |
Helixi | 1739 – 1784 | Combined sources | 46 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4AQS | X-ray | 3.11 | A | 22-542 | [»] | |
5MC9 | X-ray | 2.13 | B | 1735-1786 | [»] | |
ProteinModelPortali | P02469 | |||||
SMRi | P02469 | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 31 – 270 | Laminin N-terminalPROSITE-ProRule annotationAdd BLAST | 240 | |
Domaini | 271 – 334 | Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST | 64 | |
Domaini | 335 – 397 | Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST | 63 | |
Domaini | 398 – 457 | Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST | 60 | |
Domaini | 458 – 509 | Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST | 52 | |
Domaini | 510 – 540 | Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd BLAST | 31 | |
Domaini | 549 – 767 | Laminin IV type BPROSITE-ProRule annotationAdd BLAST | 219 | |
Domaini | 773 – 820 | Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST | 48 | |
Domaini | 821 – 866 | Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST | 46 | |
Domaini | 867 – 916 | Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST | 50 | |
Domaini | 917 – 975 | Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST | 59 | |
Domaini | 976 – 1027 | Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST | 52 | |
Domaini | 1028 – 1083 | Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST | 56 | |
Domaini | 1084 – 1131 | Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST | 48 | |
Domaini | 1132 – 1178 | Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST | 47 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1179 – 1397 | Domain IIAdd BLAST | 219 | |
Regioni | 1398 – 1430 | Domain alphaAdd BLAST | 33 | |
Regioni | 1431 – 1786 | Domain IAdd BLAST | 356 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 1216 – 1315 | Sequence analysisAdd BLAST | 100 | |
Coiled coili | 1368 – 1388 | Sequence analysisAdd BLAST | 21 | |
Coiled coili | 1448 – 1778 | Sequence analysisAdd BLAST | 331 |
Keywords - Domaini
Coiled coil, Laminin EGF-like domain, Repeat, SignalPhylogenomic databases
eggNOGi | KOG0994 Eukaryota ENOG410XPEG LUCA |
GeneTreei | ENSGT00780000121851 |
HOVERGENi | HBG052301 |
InParanoidi | P02469 |
Family and domain databases
Gene3Di | 2.60.120.14901 hit |
InterProi | View protein in InterPro IPR000742 EGF-like_dom IPR002049 Laminin_EGF IPR013015 Laminin_IV_B IPR008211 Laminin_N IPR038684 Laminin_N_sf |
Pfami | View protein in Pfam PF00053 Laminin_EGF, 13 hits PF00055 Laminin_N, 1 hit |
SMARTi | View protein in SMART SM00181 EGF, 10 hits SM00180 EGF_Lam, 13 hits SM00136 LamNT, 1 hit |
PROSITEi | View protein in PROSITE PS00022 EGF_1, 9 hits PS01186 EGF_2, 2 hits PS01248 EGF_LAM_1, 11 hits PS50027 EGF_LAM_2, 13 hits PS51116 LAMININ_IVB, 1 hit PS51117 LAMININ_NTER, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P02469-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGLLQVFAFG VLALWGTRVC AQEPEFSYGC AEGSCYPATG DLLIGRAQKL
60 70 80 90 100
SVTSTCGLHK PEPYCIVSHL QEDKKCFICD SRDPYHETLN PDSHLIENVV
110 120 130 140 150
TTFAPNRLKI WWQSENGVEN VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI
160 170 180 190 200
ERSSDFGKAW GVYRYFAYDC ESSFPGISTG PMKKVDDIIC DSRYSDIEPS
210 220 230 240 250
TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL HTLGDNLLDS
260 270 280 290 300
RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGVNEEV EGMVHGHCMC
310 320 330 340 350
RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SSSCHFDMAV
360 370 380 390 400
FLATGNVSGG VCDNCQHNTM GRNCEQCKPF YFQHPERDIR DPNLCEPCTC
410 420 430 440 450
DPAGSENGGI CDGYTDFSVG LIAGQCRCKL HVEGERCDVC KEGFYDLSAE
460 470 480 490 500
DPYGCKSCAC NPLGTIPGGN PCDSETGYCY CKRLVTGQRC DQCLPQHWGL
510 520 530 540 550
SNDLDGCRPC DCDLGGALNN SCSEDSGQCS CLPHMIGRQC NEVESGYYFT
560 570 580 590 600
TLDHYIYEAE EANLGPGVIV VERQYIQDRI PSWTGPGFVR VPEGAYLEFF
610 620 630 640 650
IDNIPYSMEY EILIRYEPQL PDHWEKAVIT VQRPGKIPAS SRCGNTVPDD
660 670 680 690 700
DNQVVSLSPG SRYVVLPRPV CFEKGMNYTV RLELPQYTAS GSDVESPYTF
710 720 730 740 750
IDSLVLMPYC KSLDIFTVGG SGDGEVTNSA WETFQRYRCL ENSRSVVKTP
760 770 780 790 800
MTDVCRNIIF SISALIHQTG LACECDPQGS LSSVCDPNGG QCQCRPNVVG
810 820 830 840 850
RTCNRCAPGT FGFGPNGCKP CDCHLQGSAS AFCDAITGQC HCFQGIYARQ
860 870 880 890 900
CDRCLPGYWG FPSCQPCQCN GHALDCDTVT GECLSCQDYT TGHNCERCLA
910 920 930 940 950
GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY
960 970 980 990 1000
IGSRCDDCAS GFFGNPSDFG GSCQPCQCHH NIDTTDPEAC DKETGRCLKC
1010 1020 1030 1040 1050
LYHTEGDHCQ LCQYGYYGDA LRQDCRKCVC NYLGTVKEHC NGSDCHCDKA
1060 1070 1080 1090 1100
TGQCSCLPNV IGQNCDRCAP NTWQLASGTG CGPCNCNAAH SFGPSCNEFT
1110 1120 1130 1140 1150
GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE TPQCDQSTGQ
1160 1170 1180 1190 1200
CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDAII GELTNRTHKF
1210 1220 1230 1240 1250
LEKAKALKIS GVIGPYRETV DSVEKKVNEI KDILAQSPAA EPLKNIGILF
1260 1270 1280 1290 1300
EEAEKLTKDV TEKMAQVEVK LTDTASQSNS TAGELGALQA EAESLDKTVK
1310 1320 1330 1340 1350
ELAEQLEFIK NSDIQGALDS ITKYFQMSLE AEKRVNASTT DPNSTVEQSA
1360 1370 1380 1390 1400
LTRDRVEDLM LERESPFKEQ QEEQARLLDE LAGKLQSLDL SAVAQMTCGT
1410 1420 1430 1440 1450
PPGADCSESE CGGPNCRTDE GEKKCGGPGC GGLVTVAHSA WQKAMDFDRD
1460 1470 1480 1490 1500
VLSALAEVEQ LSKMVSEAKV RADEAKQNAQ DVLLKTNATK EKVDKSNEDL
1510 1520 1530 1540 1550
RNLIKQIRNF LTEDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER
1560 1570 1580 1590 1600
VETLSQVEVI LQQSAADIAR AELLLEEAKR ASKSATDVKV TADMVKEALE
1610 1620 1630 1640 1650
EAEKAQVAAE KAIKQADEDI QGTQNLLTSI ESETAASEET LTNASQRISK
1660 1670 1680 1690 1700
LERNVEELKR KAAQNSGEAE YIEKVVYSVK QNADDVKKTL DGELDEKYKK
1710 1720 1730 1740 1750
VESLIAQKTE ESADARRKAE LLQNEAKTLL AQANSKLQLL EDLERKYEDN
1760 1770 1780
QKYLEDKAQE LVRLEGEVRS LLKDISEKVA VYSTCL
Sequence cautioni
The sequence AAA39407 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 159 | A → T in AAA39407 (PubMed:3493487).Curated | 1 | |
Sequence conflicti | 569 | I → V in AAA39407 (PubMed:3493487).Curated | 1 | |
Sequence conflicti | 993 | E → D in AAA39407 (PubMed:3493487).Curated | 1 | |
Sequence conflicti | 1393 | V → A in AAA39407 (PubMed:3493487).Curated | 1 | |
Sequence conflicti | 1393 | V → A in CAA28839 (PubMed:6209134).Curated | 1 | |
Sequence conflicti | 1531 – 1534 | MEMP → SGNA in AAA39407 (PubMed:3493487).Curated | 4 | |
Sequence conflicti | 1692 | G → C in CAA28839 (PubMed:6209134).Curated | 1 | |
Sequence conflicti | 1749 | D → N in CAA28839 (PubMed:6209134).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M15525 mRNA Translation: AAA39407.1 Different initiation. CR974423 Genomic DNA No translation available. CT571245 Genomic DNA No translation available. X05212 mRNA Translation: CAA28839.1 |
PIRi | A26413 MMMSB1 |
RefSeqi | XP_006515055.2, XM_006514992.3 XP_006515056.1, XM_006514993.1 |
UniGenei | Mm.172674 |
Genome annotation databases
Ensembli | ENSMUST00000169088; ENSMUSP00000132778; ENSMUSG00000002900 |
GeneIDi | 16777 |
Similar proteinsi
Entry informationi
Entry namei | LAMB1_MOUSE | |
Accessioni | P02469Primary (citable) accession number: P02469 Secondary accession number(s): E9PXZ9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | July 27, 2011 | |
Last modified: | April 25, 2018 | |
This is version 173 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |