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Protein

Laminin subunit beta-4

Gene

LAMB4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit beta-4
Alternative name(s):
Laminin beta-1-related protein
Gene namesi
Name:LAMB4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:6491. LAMB4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30279.

Chemistry

ChEMBLiCHEMBL2364187.

Polymorphism and mutation databases

BioMutaiLAMB4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 17611742Laminin subunit beta-4PRO_0000312857Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence analysis
Glycosylationi229 – 2291N-linked (GlcNAc...)Sequence analysis
Glycosylationi246 – 2461N-linked (GlcNAc...)Sequence analysis
Disulfide bondi265 ↔ ?274PROSITE-ProRule annotation
Disulfide bondi267 ↔ 295PROSITE-ProRule annotation
Disulfide bondi297 ↔ 306PROSITE-ProRule annotation
Disulfide bondi309 ↔ 329PROSITE-ProRule annotation
Disulfide bondi332 ↔ 341PROSITE-ProRule annotation
Disulfide bondi334 ↔ 359PROSITE-ProRule annotation
Disulfide bondi362 ↔ 371PROSITE-ProRule annotation
Disulfide bondi374 ↔ 392PROSITE-ProRule annotation
Disulfide bondi395 ↔ 408PROSITE-ProRule annotation
Disulfide bondi397 ↔ 423PROSITE-ProRule annotation
Disulfide bondi425 ↔ 434PROSITE-ProRule annotation
Disulfide bondi437 ↔ 452PROSITE-ProRule annotation
Disulfide bondi455 ↔ 468PROSITE-ProRule annotation
Disulfide bondi457 ↔ 475PROSITE-ProRule annotation
Disulfide bondi477 ↔ 486PROSITE-ProRule annotation
Disulfide bondi489 ↔ 503PROSITE-ProRule annotation
Disulfide bondi506 ↔ 518PROSITE-ProRule annotation
Disulfide bondi508 ↔ 525PROSITE-ProRule annotation
Disulfide bondi527 ↔ 536PROSITE-ProRule annotation
Disulfide bondi769 ↔ 781PROSITE-ProRule annotation
Disulfide bondi771 ↔ 788PROSITE-ProRule annotation
Disulfide bondi790 ↔ 799PROSITE-ProRule annotation
Disulfide bondi802 ↔ 814PROSITE-ProRule annotation
Disulfide bondi817 ↔ 829PROSITE-ProRule annotation
Disulfide bondi819 ↔ 836PROSITE-ProRule annotation
Disulfide bondi838 ↔ 847PROSITE-ProRule annotation
Disulfide bondi850 ↔ 860PROSITE-ProRule annotation
Disulfide bondi863 ↔ 872PROSITE-ProRule annotation
Disulfide bondi865 ↔ 879PROSITE-ProRule annotation
Disulfide bondi882 ↔ 891PROSITE-ProRule annotation
Disulfide bondi894 ↔ 908PROSITE-ProRule annotation
Disulfide bondi913 ↔ 938PROSITE-ProRule annotation
Disulfide bondi940 ↔ 949PROSITE-ProRule annotation
Disulfide bondi952 ↔ 967PROSITE-ProRule annotation
Disulfide bondi970 ↔ 984PROSITE-ProRule annotation
Disulfide bondi972 ↔ 991PROSITE-ProRule annotation
Disulfide bondi994 ↔ 1003PROSITE-ProRule annotation
Disulfide bondi1006 ↔ 1019PROSITE-ProRule annotation
Glycosylationi1016 – 10161N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1022 ↔ 1043PROSITE-ProRule annotation
Disulfide bondi1024 ↔ 1050PROSITE-ProRule annotation
Disulfide bondi1052 ↔ 1061PROSITE-ProRule annotation
Glycosylationi1055 – 10551N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1064 ↔ 1077PROSITE-ProRule annotation
Disulfide bondi1080 ↔ 1092PROSITE-ProRule annotation
Disulfide bondi1082 ↔ 1099PROSITE-ProRule annotation
Disulfide bondi1101 ↔ 1110PROSITE-ProRule annotation
Disulfide bondi1113 ↔ 1125PROSITE-ProRule annotation
Disulfide bondi1128 ↔ 1140PROSITE-ProRule annotation
Disulfide bondi1130 ↔ 1147PROSITE-ProRule annotation
Disulfide bondi1149 ↔ 1158PROSITE-ProRule annotation
Disulfide bondi1161 ↔ 1172PROSITE-ProRule annotation
Disulfide bondi1175 – 1175InterchainCurated
Disulfide bondi1178 – 1178InterchainCurated
Glycosylationi1223 – 12231N-linked (GlcNAc...)Sequence analysis
Glycosylationi1301 – 13011N-linked (GlcNAc...)Sequence analysis
Glycosylationi1326 – 13261N-linked (GlcNAc...)Sequence analysis
Glycosylationi1333 – 13331N-linked (GlcNAc...)Sequence analysis
Glycosylationi1354 – 13541N-linked (GlcNAc...)Sequence analysis
Glycosylationi1469 – 14691N-linked (GlcNAc...)Sequence analysis
Glycosylationi1517 – 15171N-linked (GlcNAc...)Sequence analysis
Glycosylationi1587 – 15871N-linked (GlcNAc...)Sequence analysis
Glycosylationi1596 – 15961N-linked (GlcNAc...)Sequence analysis
Glycosylationi1609 – 16091N-linked (GlcNAc...)Sequence analysis
Glycosylationi1725 – 17251N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1759 – 1759InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiA4D0S4.
PeptideAtlasiA4D0S4.
PRIDEiA4D0S4.

PTM databases

iPTMnetiA4D0S4.
PhosphoSiteiA4D0S4.

Expressioni

Gene expression databases

BgeeiA4D0S4.
CleanExiHS_LAMB4.
ExpressionAtlasiA4D0S4. baseline and differential.
GenevisibleiA4D0S4. HS.

Organism-specific databases

HPAiHPA020242.
HPA024247.

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.

Protein-protein interaction databases

BioGridi116479. 2 interactions.
IntActiA4D0S4. 1 interaction.
STRINGi9606.ENSP00000205386.

Structurei

3D structure databases

ProteinModelPortaliA4D0S4.
SMRiA4D0S4. Positions 23-543, 780-1174.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 264241Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini265 – 33167Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini332 – 39463Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini395 – 45460Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini455 – 50551Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini506 – 55247Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini545 – 763219Laminin IV type BPROSITE-ProRule annotationAdd
BLAST
Domaini769 – 81648Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini817 – 86246Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini863 – 91048Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini911 – 96959Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini970 – 102152Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini1022 – 107958Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini1080 – 112748Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1128 – 117447Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1175 – 1375201Domain IIAdd
BLAST
Regioni1376 – 140833Domain alphaAdd
BLAST
Regioni1409 – 1761353Domain IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1243 – 130159Sequence analysisAdd
BLAST
Coiled coili1416 – 148065Sequence analysisAdd
BLAST
Coiled coili1525 – 1759235Sequence analysisAdd
BLAST

Domaini

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains VI and IV are globular.

Sequence similaritiesi

Contains 13 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type B 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

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
GeneTreeiENSGT00780000121851.
HOVERGENiHBG052301.
InParanoidiA4D0S4.
KOiK06245.
OMAiHVSIRLD.
OrthoDBiEOG75XGK0.
PhylomeDBiA4D0S4.
TreeFamiTF312903.

Family and domain databases

InterProiIPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 12 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 10 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.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: A4D0S4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQFQLTLFLH LGWLSYSKAQ DDCNRGACHP TTGDLLVGRN TQLMASSTCG
60 70 80 90 100
LSRAQKYCIL SYLEGEQKCF ICDSRFPYDP YDQPNSHTIE NVIVSFEPDR
110 120 130 140 150
EKKWWQSENG LDHVSIRLDL EALFRFSHLI LTFKTFRPAA MLVERSTDYG
160 170 180 190 200
HNWKVFKYFA KDCATSFPNI TSGQAQGVGD IVCDSKYSDI EPSTGGEVVL
210 220 230 240 250
KVLDPSFEIE NPYSPYIQDL VTLTNLRINF TKLHTLGDAL LGRRQNDSLD
260 270 280 290 300
KYYYALYEMI VRGSCFCNGH ASECRPMQKM RGDVFSPPGM VHGQCVCQHN
310 320 330 340 350
TDGPNCERCK DFFQDAPWRP AADLQDNACR SCSCNSHSSR CHFDMTTYLA
360 370 380 390 400
SGGLSGGVCE DCQHNTEGQH CDRCRPLFYR DPLKTISDPY ACIPCECDPD
410 420 430 440 450
GTISGGICVS HSDPALGSVA GQCLCKENVE GAKCDQCKPN HYGLSATDPL
460 470 480 490 500
GCQPCDCNPL GSLPFLTCDV DTGQCLCLSY VTGAHCEECT VGYWGLGNHL
510 520 530 540 550
HGCSPCDCDI GGAYSNVCSP KNGQCECRPH VTGRSCSEPA PGYFFAPLNF
560 570 580 590 600
YLYEAEEATT LQGLAPLGSE TFGQSPAVHV VLGEPVPGNP VTWTGPGFAR
610 620 630 640 650
VLPGAGLRFA VNNIPFPVDF TIAIHYETQS AADWTVQIVV NPPGGSEHCI
660 670 680 690 700
PKTLQSKPQS FALPAATRIM LLPTPICLEP DVQYSIDVYF SQPLQGESHA
710 720 730 740 750
HSHVLVDSLG LIPQINSLEN FCSKQDLDEY QLHNCVEIAS AMGPQVLPGA
760 770 780 790 800
CERLIISMSA KLHDGAVACK CHPQGSVGSS CSRLGGQCQC KPLVVGRCCD
810 820 830 840 850
RCSTGSYDLG HHGCHPCHCH PQGSKDTVCD QVTGQCPCHG EVSGRRCDRC
860 870 880 890 900
LAGYFGFPSC HPCPCNRFAE LCDPETGSCF NCGGFTTGRN CERCIDGYYG
910 920 930 940 950
NPSSGQPCRP CLCPDDPSSN QYFAHSCYQN LWSSDVICNC LQGYTGTQCG
960 970 980 990 1000
ECSTGFYGNP RISGAPCQPC ACNNNIDVTD PESCSRVTGE CLRCLHNTQG
1010 1020 1030 1040 1050
ANCQLCKPGH YGSALNQTCR RCSCHASGVS PMECPPGGGA CLCDPVTGAC
1060 1070 1080 1090 1100
PCLPNVTGLA CDRCADGYWN LVPGRGCQSC DCDPRTSQSS HCDQLTGQCP
1110 1120 1130 1140 1150
CKLGYGGKRC SECQENYYGD PPGRCIPCDC NRAGTQKPIC DPDTGMCRCR
1160 1170 1180 1190 1200
EGVSGQRCDR CARGHSQEFP TCLQCHLCFD QWDHTISSLS KAVQGLMRLA
1210 1220 1230 1240 1250
ANMEDKRETL PVCEADFKDL RGNVSEIERI LKHPVFPSGK FLKVKDYHDS
1260 1270 1280 1290 1300
VRRQIMQLNE QLKAVYEFQD LKDTIERAKN EADLLLEDLQ EEIDLQSSVL
1310 1320 1330 1340 1350
NASIADSSEN IKKYYHISSS AEKKINETSS TINTSANTRN DLLTILDTLT
1360 1370 1380 1390 1400
SKGNLSLERL KQIKIPDIQI LNEKVCGDPG NVPCVPLPCG GALCTGRKGH
1410 1420 1430 1440 1450
RKCRGPGCHG SLTLSTNALQ KAQEAKSIIR NLDKQVRGLK NQIESISEQA
1460 1470 1480 1490 1500
EVSKNNALQL REKLGNIRNQ SDSEEENINL FIKKVKNFLL EENVPPEDIE
1510 1520 1530 1540 1550
KVANGVLDIH LPIPSQNLTD ELVKIQKHMQ LCEDYRTDEN RLNEEADGAQ
1560 1570 1580 1590 1600
KLLVKAKAAE KAANILLNLD KTLNQLQQAQ ITQGRANSTI TQLTANITKI
1610 1620 1630 1640 1650
KKNVLQAENQ TREMKSELEL AKQRSGLEDG LSLLQTKLQR HQDHAVNAKV
1660 1670 1680 1690 1700
QAESAQHQAG SLEKEFVELK KQYAILQRKT STTGLTKETL GKVKQLKDAA
1710 1720 1730 1740 1750
EKLAGDTEAK IRRITDLERK IQDLNLSRQA KADQLRILED QVVAIKNEIV
1760
EQEKKYARCY S
Length:1,761
Mass (Da):193,540
Last modified:April 3, 2007 - v1
Checksum:i57A740F079CE1FB2
GO
Isoform 2 (identifier: A4D0S4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     709-772: LGLIPQINSL...HDGAVACKCH → AAVQWHNLGS...PGWSRTPDLR
     773-1761: Missing.

Show »
Length:772
Mass (Da):85,105
Checksum:iB74332DD472E0C6B
GO
Isoform 3 (identifier: A4D0S4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1716-1723: DLERKIQD → GCFQNSAR
     1724-1761: Missing.

Show »
Length:1,723
Mass (Da):188,959
Checksum:iEF23F9CBED1266A7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701F → S in AAC95123 (Ref. 1) Curated
Sequence conflicti93 – 931I → T in AAC95123 (Ref. 1) Curated
Sequence conflicti1542 – 15421L → S in AAC95123 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441M → T.
Corresponds to variant rs35644375 [ dbSNP | Ensembl ].
VAR_037588
Natural varianti234 – 2341H → Y.
Corresponds to variant rs2074749 [ dbSNP | Ensembl ].
VAR_037589
Natural varianti591 – 5911V → F.
Corresponds to variant rs9690688 [ dbSNP | Ensembl ].
VAR_037590
Natural varianti866 – 8661N → S.
Corresponds to variant rs2240445 [ dbSNP | Ensembl ].
VAR_037591
Natural varianti1028 – 10281G → C.1 Publication
VAR_074174
Natural varianti1350 – 13501T → N.
Corresponds to variant rs10260756 [ dbSNP | Ensembl ].
VAR_037592
Natural varianti1510 – 15101H → Y.
Corresponds to variant rs1627354 [ dbSNP | Ensembl ].
VAR_037593
Natural varianti1612 – 16121R → S.
Corresponds to variant rs2528693 [ dbSNP | Ensembl ].
VAR_037594

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei709 – 77264LGLIP…ACKCH → AAVQWHNLGSLQPPPPECKQ FSCFSFPSSWDYRHPPPHLA SFCIFSRDGVSPHWPGWSRT PDLR in isoform 2. 1 PublicationVSP_029913Add
BLAST
Alternative sequencei773 – 1761989Missing in isoform 2. 1 PublicationVSP_029914Add
BLAST
Alternative sequencei1716 – 17238DLERKIQD → GCFQNSAR in isoform 3. 1 PublicationVSP_029915
Alternative sequencei1724 – 176138Missing in isoform 3. 1 PublicationVSP_029916Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF028816 mRNA. Translation: AAC95123.1.
AC005048 Genomic DNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24387.1.
BC045172 mRNA. Translation: AAH45172.2.
BC140804 mRNA. Translation: AAI40805.1.
BC142619 mRNA. Translation: AAI42620.1.
AK075165 mRNA. No translation available.
CCDSiCCDS34732.1. [A4D0S4-1]
RefSeqiNP_001304975.1. NM_001318046.1. [A4D0S4-1]
NP_001304977.1. NM_001318048.1.
NP_031382.2. NM_007356.2. [A4D0S4-1]
XP_011514280.1. XM_011515978.1. [A4D0S4-3]
UniGeneiHs.62022.

Genome annotation databases

EnsembliENST00000205386; ENSP00000205386; ENSG00000091128. [A4D0S4-1]
ENST00000388781; ENSP00000373433; ENSG00000091128. [A4D0S4-1]
GeneIDi22798.
KEGGihsa:22798.
UCSCiuc003vey.3. human. [A4D0S4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF028816 mRNA. Translation: AAC95123.1.
AC005048 Genomic DNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24387.1.
BC045172 mRNA. Translation: AAH45172.2.
BC140804 mRNA. Translation: AAI40805.1.
BC142619 mRNA. Translation: AAI42620.1.
AK075165 mRNA. No translation available.
CCDSiCCDS34732.1. [A4D0S4-1]
RefSeqiNP_001304975.1. NM_001318046.1. [A4D0S4-1]
NP_001304977.1. NM_001318048.1.
NP_031382.2. NM_007356.2. [A4D0S4-1]
XP_011514280.1. XM_011515978.1. [A4D0S4-3]
UniGeneiHs.62022.

3D structure databases

ProteinModelPortaliA4D0S4.
SMRiA4D0S4. Positions 23-543, 780-1174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116479. 2 interactions.
IntActiA4D0S4. 1 interaction.
STRINGi9606.ENSP00000205386.

Chemistry

ChEMBLiCHEMBL2364187.

PTM databases

iPTMnetiA4D0S4.
PhosphoSiteiA4D0S4.

Polymorphism and mutation databases

BioMutaiLAMB4.

Proteomic databases

PaxDbiA4D0S4.
PeptideAtlasiA4D0S4.
PRIDEiA4D0S4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000205386; ENSP00000205386; ENSG00000091128. [A4D0S4-1]
ENST00000388781; ENSP00000373433; ENSG00000091128. [A4D0S4-1]
GeneIDi22798.
KEGGihsa:22798.
UCSCiuc003vey.3. human. [A4D0S4-1]

Organism-specific databases

CTDi22798.
GeneCardsiLAMB4.
HGNCiHGNC:6491. LAMB4.
HPAiHPA020242.
HPA024247.
MIMi616380. gene.
neXtProtiNX_A4D0S4.
PharmGKBiPA30279.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
GeneTreeiENSGT00780000121851.
HOVERGENiHBG052301.
InParanoidiA4D0S4.
KOiK06245.
OMAiHVSIRLD.
OrthoDBiEOG75XGK0.
PhylomeDBiA4D0S4.
TreeFamiTF312903.

Miscellaneous databases

ChiTaRSiLAMB4. human.
GenomeRNAii22798.
PROiA4D0S4.
SOURCEiSearch...

Gene expression databases

BgeeiA4D0S4.
CleanExiHS_LAMB4.
ExpressionAtlasiA4D0S4. baseline and differential.
GenevisibleiA4D0S4. HS.

Family and domain databases

InterProiIPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 12 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 10 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the human laminin beta-4 chain."
    Olson P.F., Koch M., Champliaud M.F., Rowland K., Jin W., Burgeson R.E.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 975-1761 (ISOFORM 3).
    Tissue: Testis.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1528-1761 (ISOFORM 1).
    Tissue: Placenta.
  6. Cited for: VARIANT CYS-1028.

Entry informationi

Entry nameiLAMB4_HUMAN
AccessioniPrimary (citable) accession number: A4D0S4
Secondary accession number(s): A5PKU6
, B2RTT3, B5MEB9, Q86TP7, Q86XN2, Q8NBX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: April 3, 2007
Last modified: July 6, 2016
This is version 82 of the entry and version 1 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 7
    Human chromosome 7: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.