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P02469

- LAMB1_MOUSE

UniProt

P02469 - LAMB1_MOUSE

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Protein
Laminin subunit beta-1
Gene
Lamb1, Lamb-1, Lamb1-1
Organism
Mus musculus (Mouse)
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. 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.

GO - Molecular functioni

  1. enzyme binding Source: MGI
  2. extracellular matrix structural constituent Source: HGNC
  3. glycosphingolipid binding Source: MGI
  4. integrin binding Source: MGI
  5. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. cell migration Source: MGI
  3. embryo implantation Source: MGI
  4. learning or memory Source: UniProtKB
  5. negative regulation of cell adhesion Source: UniProtKB
  6. neuron projection development Source: HGNC
  7. odontogenesis Source: HGNC
  8. positive regulation of cell migration Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.
REACT_219680. L1CAM interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit beta-1
Alternative 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:96743. Lamb1.

Subcellular locationi

GO - Cellular componenti

  1. basal lamina Source: MGI
  2. basement membrane Source: UniProtKB
  3. extracellular region Source: Reactome
  4. laminin complex Source: MGI
  5. laminin-1 complex Source: HGNC
  6. laminin-10 complex Source: HGNC
  7. laminin-2 complex Source: HGNC
  8. laminin-8 complex Source: HGNC
  9. perinuclear region of cytoplasm Source: UniProtKB
  10. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121
Add
BLAST
Chaini22 – 17861765Laminin subunit beta-1
PRO_0000017066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi120 – 1201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi271 ↔ 280 By similarity
Disulfide bondi273 ↔ 298 By similarity
Disulfide bondi300 ↔ 309 By similarity
Disulfide bondi312 ↔ 332 By similarity
Disulfide bondi335 ↔ 344 By similarity
Disulfide bondi337 ↔ 362 By similarity
Glycosylationi356 – 3561N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi365 ↔ 374 By similarity
Disulfide bondi377 ↔ 395 By similarity
Disulfide bondi398 ↔ 411 By similarity
Disulfide bondi400 ↔ 426 By similarity
Disulfide bondi428 ↔ 437 By similarity
Disulfide bondi440 ↔ 455 By similarity
Disulfide bondi458 ↔ 472 By similarity
Disulfide bondi460 ↔ 479 By similarity
Disulfide bondi481 ↔ 490 By similarity
Disulfide bondi493 ↔ 507 By similarity
Disulfide bondi510 ↔ 522 By similarity
Disulfide bondi512 ↔ 529 By similarity
Glycosylationi519 – 5191N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi531 ↔ 540 By similarity
Glycosylationi677 – 6771N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi773 ↔ 785 By similarity
Disulfide bondi775 ↔ 792 By similarity
Disulfide bondi794 ↔ 803 By similarity
Disulfide bondi806 ↔ 818 By similarity
Disulfide bondi821 ↔ 833 By similarity
Disulfide bondi823 ↔ 840 By similarity
Disulfide bondi842 ↔ 851 By similarity
Disulfide bondi854 ↔ 864 By similarity
Disulfide bondi867 ↔ 876 By similarity
Disulfide bondi869 ↔ 883 By similarity
Disulfide bondi886 ↔ 895 By similarity
Disulfide bondi898 ↔ 914 By similarity
Disulfide bondi917 ↔ 933 By similarity
Disulfide bondi919 ↔ 944 By similarity
Disulfide bondi946 ↔ 955 By similarity
Disulfide bondi958 ↔ 973 By similarity
Disulfide bondi976 ↔ 990 By similarity
Disulfide bondi978 ↔ 997 By similarity
Disulfide bondi1000 ↔ 1009 By similarity
Disulfide bondi1012 ↔ 1025 By similarity
Disulfide bondi1028 ↔ 1040 By similarity
Disulfide bondi1030 ↔ 1054 By similarity
Glycosylationi1041 – 10411N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1056 ↔ 1065 By similarity
Disulfide bondi1068 ↔ 1081 By similarity
Disulfide bondi1084 ↔ 1096 By similarity
Disulfide bondi1086 ↔ 1103 By similarity
Disulfide bondi1105 ↔ 1114 By similarity
Disulfide bondi1117 ↔ 1129 By similarity
Disulfide bondi1132 ↔ 1144 By similarity
Disulfide bondi1134 ↔ 1151 By similarity
Disulfide bondi1153 ↔ 1162 By similarity
Disulfide bondi1165 ↔ 1176 By similarity
Disulfide bondi1179 – 1179Interchain Inferred
Disulfide bondi1182 – 1182Interchain Inferred
Glycosylationi1195 – 11951N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1279 – 12791N-linked (GlcNAc...)1 Publication
Glycosylationi1336 – 13361N-linked (GlcNAc...)1 Publication
Glycosylationi1343 – 13431N-linked (GlcNAc...)1 Publication
Glycosylationi1487 – 14871N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1542 – 15421N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1643 – 16431N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1785 – 1785Interchain Inferred

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP02469.
PaxDbiP02469.
PRIDEiP02469.

PTM databases

PhosphoSiteiP02469.

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

ArrayExpressiP02469.
BgeeiP02469.
CleanExiMM_LAMB1-1.
GenevestigatoriP02469.

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

WithEntry#Exp.IntActNotes
AGRNP316962EBI-6662997,EBI-457650From a different organism.
Lamc1P024684EBI-6662997,EBI-7059830

Protein-protein interaction databases

IntActiP02469. 6 interactions.
MINTiMINT-1206337.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 323
Beta strandi40 – 434
Helixi47 – 493
Beta strandi58 – 603
Beta strandi62 – 676
Beta strandi69 – 724
Beta strandi74 – 796
Turni87 – 893
Helixi96 – 983
Beta strandi122 – 14221
Beta strandi146 – 15510
Beta strandi161 – 1699
Turni170 – 1723
Beta strandi173 – 1775
Turni200 – 2023
Beta strandi204 – 2107
Beta strandi212 – 2143
Helixi222 – 2287
Beta strandi229 – 23911
Helixi252 – 2554
Beta strandi261 – 27010
Beta strandi304 – 3096
Beta strandi342 – 3465
Helixi348 – 3536
Beta strandi360 – 3645
Beta strandi369 – 3713
Beta strandi381 – 3833
Beta strandi385 – 3873
Beta strandi395 – 3973
Turni402 – 4043
Helixi407 – 4093
Helixi417 – 4193
Turni434 – 4374
Beta strandi454 – 4574
Turni462 – 4643
Turni474 – 4763
Turni488 – 4903

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AQSX-ray3.11A22-542[»]
ProteinModelPortaliP02469.
SMRiP02469. Positions 29-492.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 270240Laminin N-terminal
Add
BLAST
Domaini271 – 33464Laminin EGF-like 1
Add
BLAST
Domaini335 – 39763Laminin EGF-like 2
Add
BLAST
Domaini398 – 45760Laminin EGF-like 3
Add
BLAST
Domaini458 – 50952Laminin EGF-like 4
Add
BLAST
Domaini510 – 54031Laminin EGF-like 5; truncated
Add
BLAST
Domaini549 – 767219Laminin IV type B
Add
BLAST
Domaini773 – 82048Laminin EGF-like 6
Add
BLAST
Domaini821 – 86646Laminin EGF-like 7
Add
BLAST
Domaini867 – 91650Laminin EGF-like 8
Add
BLAST
Domaini917 – 97559Laminin EGF-like 9
Add
BLAST
Domaini976 – 102752Laminin EGF-like 10
Add
BLAST
Domaini1028 – 108356Laminin EGF-like 11
Add
BLAST
Domaini1084 – 113148Laminin EGF-like 12
Add
BLAST
Domaini1132 – 117847Laminin EGF-like 13
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1179 – 1397219Domain II
Add
BLAST
Regioni1398 – 143033Domain alpha
Add
BLAST
Regioni1431 – 1786356Domain I
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1216 – 1315100 Reviewed prediction
Add
BLAST
Coiled coili1368 – 138821 Reviewed prediction
Add
BLAST
Coiled coili1448 – 1778331 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG241384.
GeneTreeiENSGT00720000108616.
HOVERGENiHBG052301.
InParanoidiP02469.
KOiK05636.
OrthoDBiEOG75XGK0.

Family and domain databases

InterProiIPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02469-1 [UniParc]FASTAAdd to Basket

« Hide

MGLLQVFAFG VLALWGTRVC AQEPEFSYGC AEGSCYPATG DLLIGRAQKL     50
SVTSTCGLHK PEPYCIVSHL QEDKKCFICD SRDPYHETLN PDSHLIENVV 100
TTFAPNRLKI WWQSENGVEN VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI 150
ERSSDFGKAW GVYRYFAYDC ESSFPGISTG PMKKVDDIIC DSRYSDIEPS 200
TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL HTLGDNLLDS 250
RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGVNEEV EGMVHGHCMC 300
RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SSSCHFDMAV 350
FLATGNVSGG VCDNCQHNTM GRNCEQCKPF YFQHPERDIR DPNLCEPCTC 400
DPAGSENGGI CDGYTDFSVG LIAGQCRCKL HVEGERCDVC KEGFYDLSAE 450
DPYGCKSCAC NPLGTIPGGN PCDSETGYCY CKRLVTGQRC DQCLPQHWGL 500
SNDLDGCRPC DCDLGGALNN SCSEDSGQCS CLPHMIGRQC NEVESGYYFT 550
TLDHYIYEAE EANLGPGVIV VERQYIQDRI PSWTGPGFVR VPEGAYLEFF 600
IDNIPYSMEY EILIRYEPQL PDHWEKAVIT VQRPGKIPAS SRCGNTVPDD 650
DNQVVSLSPG SRYVVLPRPV CFEKGMNYTV RLELPQYTAS GSDVESPYTF 700
IDSLVLMPYC KSLDIFTVGG SGDGEVTNSA WETFQRYRCL ENSRSVVKTP 750
MTDVCRNIIF SISALIHQTG LACECDPQGS LSSVCDPNGG QCQCRPNVVG 800
RTCNRCAPGT FGFGPNGCKP CDCHLQGSAS AFCDAITGQC HCFQGIYARQ 850
CDRCLPGYWG FPSCQPCQCN GHALDCDTVT GECLSCQDYT TGHNCERCLA 900
GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY 950
IGSRCDDCAS GFFGNPSDFG GSCQPCQCHH NIDTTDPEAC DKETGRCLKC 1000
LYHTEGDHCQ LCQYGYYGDA LRQDCRKCVC NYLGTVKEHC NGSDCHCDKA 1050
TGQCSCLPNV IGQNCDRCAP NTWQLASGTG CGPCNCNAAH SFGPSCNEFT 1100
GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE TPQCDQSTGQ 1150
CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDAII GELTNRTHKF 1200
LEKAKALKIS GVIGPYRETV DSVEKKVNEI KDILAQSPAA EPLKNIGILF 1250
EEAEKLTKDV TEKMAQVEVK LTDTASQSNS TAGELGALQA EAESLDKTVK 1300
ELAEQLEFIK NSDIQGALDS ITKYFQMSLE AEKRVNASTT DPNSTVEQSA 1350
LTRDRVEDLM LERESPFKEQ QEEQARLLDE LAGKLQSLDL SAVAQMTCGT 1400
PPGADCSESE CGGPNCRTDE GEKKCGGPGC GGLVTVAHSA WQKAMDFDRD 1450
VLSALAEVEQ LSKMVSEAKV RADEAKQNAQ DVLLKTNATK EKVDKSNEDL 1500
RNLIKQIRNF LTEDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER 1550
VETLSQVEVI LQQSAADIAR AELLLEEAKR ASKSATDVKV TADMVKEALE 1600
EAEKAQVAAE KAIKQADEDI QGTQNLLTSI ESETAASEET LTNASQRISK 1650
LERNVEELKR KAAQNSGEAE YIEKVVYSVK QNADDVKKTL DGELDEKYKK 1700
VESLIAQKTE ESADARRKAE LLQNEAKTLL AQANSKLQLL EDLERKYEDN 1750
QKYLEDKAQE LVRLEGEVRS LLKDISEKVA VYSTCL 1786
Length:1,786
Mass (Da):197,090
Last modified:July 27, 2011 - v3
Checksum:iE7F258170C3626DD
GO

Sequence cautioni

The sequence AAA39407.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591A → T in AAA39407. 1 Publication
Sequence conflicti569 – 5691I → V in AAA39407. 1 Publication
Sequence conflicti993 – 9931E → D in AAA39407. 1 Publication
Sequence conflicti1393 – 13931V → A in AAA39407. 1 Publication
Sequence conflicti1393 – 13931V → A in CAA28839. 1 Publication
Sequence conflicti1531 – 15344MEMP → SGNA in AAA39407. 1 Publication
Sequence conflicti1692 – 16921G → C in CAA28839. 1 Publication
Sequence conflicti1749 – 17491D → N in CAA28839. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
PIRiA26413. MMMSB1.
RefSeqiXP_006515056.1. XM_006514993.1.
UniGeneiMm.172674.

Genome annotation databases

EnsembliENSMUST00000169088; ENSMUSP00000132778; ENSMUSG00000002900.
GeneIDi16777.
KEGGimmu:16777.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006515056.1. XM_006514993.1.
UniGenei Mm.172674.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AQS X-ray 3.11 A 22-542 [» ]
ProteinModelPortali P02469.
SMRi P02469. Positions 29-492.
ModBasei Search...

Protein-protein interaction databases

IntActi P02469. 6 interactions.
MINTi MINT-1206337.

PTM databases

PhosphoSitei P02469.

Proteomic databases

MaxQBi P02469.
PaxDbi P02469.
PRIDEi P02469.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000169088 ; ENSMUSP00000132778 ; ENSMUSG00000002900 .
GeneIDi 16777.
KEGGi mmu:16777.

Organism-specific databases

CTDi 3912.
MGIi MGI:96743. Lamb1.

Phylogenomic databases

eggNOGi NOG241384.
GeneTreei ENSGT00720000108616.
HOVERGENi HBG052301.
InParanoidi P02469.
KOi K05636.
OrthoDBi EOG75XGK0.

Enzyme and pathway databases

Reactomei REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.
REACT_219680. L1CAM interactions.

Miscellaneous databases

ChiTaRSi LAMB1. mouse.
PROi P02469.
SOURCEi Search...

Gene expression databases

ArrayExpressi P02469.
Bgeei P02469.
CleanExi MM_LAMB1-1.
Genevestigatori P02469.

Family and domain databases

InterProi IPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats."
    Sasaki M., Kato S., Kohno K., Martin G.R., Yamada Y.
    Proc. Natl. Acad. Sci. U.S.A. 84:935-939(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Sequencing of laminin B chain cDNAs reveals C-terminal regions of coiled-coil alpha-helix."
    Barlow D.P., Green N.M., Kurkinen M., Hogan B.L.M.
    EMBO J. 3:2355-2362(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1292-1786.
  4. "Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of endothelium."
    Frieser M., Noeckel H., Pausch F., Roeder C., Hahn A., Deutzmann R., Sorokin L.M.
    Eur. J. Biochem. 246:727-735(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 165-172; 539-547 AND 712-719.
    Strain: BALB/c.
    Tissue: Endothelial cell.
  5. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279; ASN-1336 AND ASN-1343.
  6. Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiLAMB1_MOUSE
AccessioniPrimary (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: September 3, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi