SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P02468

- LAMC1_MOUSE

UniProt

P02468 - LAMC1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Laminin subunit gamma-1

Gene
Lamc1, Lamb-2, Lamc-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.

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: HGNC
  2. glycosphingolipid binding Source: MGI
  3. protein binding Source: IntAct

GO - Biological processi

  1. cell adhesion Source: HGNC
  2. cell migration Source: HGNC
  3. extracellular matrix disassembly Source: HGNC
  4. hemidesmosome assembly Source: HGNC
  5. neuron projection development Source: MGI
  6. protein complex assembly 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 gamma-1
Alternative name(s):
Laminin B2 chain
Laminin-1 subunit gamma
Laminin-10 subunit gamma
Laminin-11 subunit gamma
Laminin-2 subunit gamma
Laminin-3 subunit gamma
Laminin-4 subunit gamma
Laminin-6 subunit gamma
Laminin-7 subunit gamma
Laminin-8 subunit gamma
Laminin-9 subunit gamma
S-laminin subunit gamma
Short name:
S-LAM gamma
Gene namesi
Name:Lamc1
Synonyms:Lamb-2, Lamc-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:99914. Lamc1.

Subcellular locationi

GO - Cellular componenti

  1. basal lamina Source: MGI
  2. basement membrane Source: HGNC
  3. extracellular region Source: Reactome
  4. laminin-10 complex 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 – 3333Add
BLAST
Chaini34 – 16071574Laminin subunit gamma-1PRO_0000017075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi58 – 581N-linked (GlcNAc...) Reviewed prediction
Glycosylationi132 – 1321N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi284 ↔ 293 By similarity
Disulfide bondi286 ↔ 303 By similarity
Disulfide bondi305 ↔ 314 By similarity
Disulfide bondi340 ↔ 349 By similarity
Disulfide bondi342 ↔ 365 By similarity
Disulfide bondi368 ↔ 377 By similarity
Disulfide bondi380 ↔ 393 By similarity
Disulfide bondi396 ↔ 408 By similarity
Disulfide bondi398 ↔ 414 By similarity
Disulfide bondi416 ↔ 425 By similarity
Disulfide bondi428 ↔ 440 By similarity
Disulfide bondi443 ↔ 454 By similarity
Disulfide bondi445 ↔ 461 By similarity
Disulfide bondi463 ↔ 472 By similarity
Disulfide bondi475 ↔ 490 By similarity
Glycosylationi574 – 5741N-linked (GlcNAc...) Reviewed prediction
Glycosylationi648 – 6481N-linked (GlcNAc...)1 Publication
Disulfide bondi722 ↔ 731 By similarity
Disulfide bondi724 ↔ 738 By similarity
Disulfide bondi740 ↔ 749 By similarity
Disulfide bondi752 ↔ 768 By similarity
Disulfide bondi771 ↔ 779
Disulfide bondi773 ↔ 790
Disulfide bondi793 ↔ 802
Disulfide bondi805 ↔ 823
Disulfide bondi826 ↔ 840
Disulfide bondi828 ↔ 847
Disulfide bondi850 ↔ 859
Disulfide bondi862 ↔ 879
Disulfide bondi882 ↔ 896
Disulfide bondi884 ↔ 903
Disulfide bondi905 ↔ 914
Disulfide bondi917 ↔ 930
Disulfide bondi933 ↔ 945 By similarity
Disulfide bondi935 ↔ 952 By similarity
Disulfide bondi954 ↔ 963 By similarity
Disulfide bondi966 ↔ 978 By similarity
Disulfide bondi981 ↔ 993 By similarity
Disulfide bondi983 ↔ 999 By similarity
Disulfide bondi1001 ↔ 1010 By similarity
Disulfide bondi1013 ↔ 1026 By similarity
Glycosylationi1020 – 10201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1029 – 1029Interchain Inferred
Disulfide bondi1032 – 1032Interchain Inferred
Glycosylationi1105 – 11051N-linked (GlcNAc...)1 Publication
Glycosylationi1159 – 11591N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1173 – 11731N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1203 – 12031N-linked (GlcNAc...)1 Publication
Glycosylationi1221 – 12211N-linked (GlcNAc...)1 Publication
Glycosylationi1239 – 12391N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1378 – 13781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1393 – 13931N-linked (GlcNAc...)1 Publication
Glycosylationi1437 – 14371N-linked (GlcNAc...) Reviewed prediction
Modified residuei1491 – 14911Phosphoserine By similarity
Disulfide bondi1598 – 1598Interchain (with beta-1 chain)

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP02468.
PaxDbiP02468.
PRIDEiP02468.

PTM databases

PhosphoSiteiP02468.

Expressioni

Tissue specificityi

Found in the basement membranes (major component).

Gene expression databases

CleanExiMM_LAMC1.
GenevestigatoriP02468.

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. Gamma-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-6 (laminin-311 or K-laminin), laminin-7 (laminin-321 or KS-laminin), laminin-8 (laminin-411), laminin-9 (laminin-421), laminin-10 (laminin-511) and laminin-11 (laminin-521).

Binary interactionsi

WithEntry#Exp.IntActNotes
Lamb1P024694EBI-7059830,EBI-6662997

Protein-protein interaction databases

DIPiDIP-41793N.
IntActiP02468. 4 interactions.
MINTiMINT-1031545.

Structurei

Secondary structure

1
1607
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni55 – 584
Beta strandi62 – 643
Beta strandi72 – 754
Beta strandi87 – 904
Beta strandi92 – 943
Turni95 – 973
Helixi101 – 1044
Beta strandi110 – 1123
Helixi121 – 1233
Beta strandi126 – 1283
Beta strandi131 – 15323
Beta strandi156 – 16813
Beta strandi171 – 1777
Helixi180 – 1845
Beta strandi202 – 2054
Beta strandi212 – 2143
Beta strandi216 – 2216
Turni222 – 2254
Helixi229 – 2346
Helixi236 – 2416
Beta strandi243 – 25311
Helixi259 – 2613
Helixi265 – 2684
Beta strandi274 – 28411
Beta strandi293 – 2953
Beta strandi301 – 3033
Beta strandi309 – 3113
Helixi342 – 3443
Beta strandi349 – 3513
Helixi353 – 3586
Beta strandi363 – 3653
Turni369 – 3713
Beta strandi372 – 3743
Beta strandi382 – 3854
Beta strandi779 – 7813
Beta strandi783 – 7853
Beta strandi788 – 7903
Beta strandi797 – 7993
Beta strandi809 – 8124
Beta strandi816 – 8194
Beta strandi821 – 8255
Beta strandi834 – 8374
Turni842 – 8443
Beta strandi846 – 8494
Turni856 – 8594
Beta strandi866 – 8683
Helixi875 – 8773
Beta strandi878 – 8814
Turni886 – 8883
Helixi890 – 8923
Turni898 – 9003
Beta strandi909 – 9113
Helixi924 – 9263

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KLOX-ray2.10A771-932[»]
1NPEX-ray2.30B769-932[»]
1TLENMR-A824-881[»]
4AQTX-ray3.20A33-395[»]
ProteinModelPortaliP02468.
SMRiP02468. Positions 37-492, 680-1012, 1283-1522.

Miscellaneous databases

EvolutionaryTraceiP02468.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 283240Laminin N-terminalAdd
BLAST
Domaini284 – 33956Laminin EGF-like 1Add
BLAST
Domaini340 – 39556Laminin EGF-like 2Add
BLAST
Domaini396 – 44247Laminin EGF-like 3Add
BLAST
Domaini443 – 49250Laminin EGF-like 4Add
BLAST
Domaini493 – 50210Laminin EGF-like 5; first part
Domaini512 – 687176Laminin IV type AAdd
BLAST
Domaini688 – 72134Laminin EGF-like 5; second partAdd
BLAST
Domaini722 – 77049Laminin EGF-like 6Add
BLAST
Domaini771 – 82555Laminin EGF-like 7Add
BLAST
Domaini826 – 88156Laminin EGF-like 8; nidogen-bindingAdd
BLAST
Domaini882 – 93251Laminin EGF-like 9Add
BLAST
Domaini933 – 98048Laminin EGF-like 10Add
BLAST
Domaini981 – 102848Laminin EGF-like 11Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1029 – 1607579Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1034 – 1594561 Reviewed predictionAdd
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

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG235720.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiP02468.
PhylomeDBiP02468.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 10 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 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.

P02468-1 [UniParc]FASTAAdd to Basket

« Hide

MTGGGRAALA LQPRGRLWPL LAVLAAVAGC VRAAMDECAD EGGRPQRCMP     50
EFVNAAFNVT VVATNTCGTP PEEYCVQTGV TGVTKSCHLC DAGQQHLQHG 100
AAFLTDYNNQ ADTTWWQSQT MLAGVQYPNS INLTLHLGKA FDITYVRLKF 150
HTSRPESFAI YKRTREDGPW IPYQYYSGSC ENTYSKANRG FIRTGGDEQQ 200
ALCTDEFSDI SPLTGGNVAF STLEGRPSAY NFDNSPVLQE WVTATDIRVT 250
LNRLNTFGDE VFNEPKVLKS YYYAISDFAV GGRCKCNGHA SECVKNEFDK 300
LMCNCKHNTY GVDCEKCLPF FNDRPWRRAT AESASESLPC DCNGRSQECY 350
FDPELYRSTG HGGHCTNCRD NTDGAKCERC RENFFRLGNT EACSPCHCSP 400
VGSLSTQCDS YGRCSCKPGV MGDKCDRCQP GFHSLTEAGC RPCSCDLRGS 450
TDECNVETGR CVCKDNVEGF NCERCKPGFF NLESSNPKGC TPCFCFGHSS 500
VCTNAVGYSV YDISSTFQID EDGWRVEQRD GSEASLEWSS DRQDIAVISD 550
SYFPRYFIAP VKFLGNQVLS YGQNLSFSFR VDRRDTRLSA EDLVLEGAGL 600
RVSVPLIAQG NSYPSETTVK YIFRLHEATD YPWRPALSPF EFQKLLNNLT 650
SIKIRGTYSE RTAGYLDDVT LQSARPGPGV PATWVESCTC PVGYGGQFCE 700
TCLPGYRRET PSLGPYSPCV LCTCNGHSET CDPETGVCDC RDNTAGPHCE 750
KCSDGYYGDS TLGTSSDCQP CPCPGGSSCA IVPKTKEVVC THCPTGTAGK 800
RCELCDDGYF GDPLGSNGPV RLCRPCQCND NIDPNAVGNC NRLTGECLKC 850
IYNTAGFYCD RCKEGFFGNP LAPNPADKCK ACACNPYGTV QQQSSCNPVT 900
GQCQCLPHVS GRDCGTCDPG YYNLQSGQGC ERCDCHALGS TNGQCDIRTG 950
QCECQPGITG QHCERCETNH FGFGPEGCKP CDCHHEGSLS LQCKDDGRCE 1000
CREGFVGNRC DQCEENYFYN RSWPGCQECP ACYRLVKDKA AEHRVKLQEL 1050
ESLIANLGTG DDMVTDQAFE DRLKEAEREV TDLLREAQEV KDVDQNLMDR 1100
LQRVNSSLHS QISRLQNIRN TIEETGILAE RARSRVESTE QLIEIASREL 1150
EKAKMAAANV SITQPESTGE PNNMTLLAEE ARRLAERHKQ EADDIVRVAK 1200
TANETSAEAY NLLLRTLAGE NQTALEIEEL NRKYEQAKNI SQDLEKQAAR 1250
VHEEAKRAGD KAVEIYASVA QLTPVDSEAL ENEANKIKKE AADLDRLIDQ 1300
KLKDYEDLRE DMRGKEHEVK NLLEKGKAEQ QTADQLLARA DAAKALAEEA 1350
AKKGRSTLQE ANDILNNLKD FDRRVNDNKT AAEEALRRIP AINRTIAEAN 1400
EKTREAQLAL GNAAADATEA KNKAHEAERI ASAVQKNATS TKADAERTFG 1450
EVTDLDNEVN GMLRQLEEAE NELKRKQDDA DQDMMMAGMA SQAAQEAELN 1500
ARKAKNSVSS LLSQLNNLLD QLGQLDTVDL NKLNEIEGSL NKAKDEMKAS 1550
DLDRKVSDLE SEARKQEAAI MDYNRDIAEI IKDIHNLEDI KKTLPTGCFN 1600
TPSIEKP 1607
Length:1,607
Mass (Da):177,298
Last modified:July 1, 1989 - v2
Checksum:i81B7B08E4869F242
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161G → A in AAA39409. 1 Publication
Sequence conflicti260 – 2601E → D1 Publication
Sequence conflicti337 – 3371S → C in AAA39408. 1 Publication
Sequence conflicti447 – 4482LR → PS in AAA39408. 1 Publication
Sequence conflicti544 – 5441D → Y in AAA39408. 1 Publication
Sequence conflicti662 – 6621T → S in AAA39408. 1 Publication
Sequence conflicti886 – 8861Missing in AAA39408. 1 Publication
Sequence conflicti1158 – 11581Missing in AAA39408. 1 Publication
Sequence conflicti1434 – 14341V → A in AAA39408. 1 Publication
Sequence conflicti1475 – 14751R → K in CAA28838. 1 Publication
Sequence conflicti1576 – 15761D → N in CAA28838. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05211 mRNA. Translation: CAA28838.1.
J03484 mRNA. Translation: AAA39405.1.
J02930 mRNA. Translation: AAA39408.1.
J03749 Genomic DNA. Translation: AAA39409.1.
CCDSiCCDS15370.1.
PIRiA28469. MMMSB2.
S55783.
UniGeneiMm.1249.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05211 mRNA. Translation: CAA28838.1 .
J03484 mRNA. Translation: AAA39405.1 .
J02930 mRNA. Translation: AAA39408.1 .
J03749 Genomic DNA. Translation: AAA39409.1 .
CCDSi CCDS15370.1.
PIRi A28469. MMMSB2.
S55783.
UniGenei Mm.1249.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KLO X-ray 2.10 A 771-932 [» ]
1NPE X-ray 2.30 B 769-932 [» ]
1TLE NMR - A 824-881 [» ]
4AQT X-ray 3.20 A 33-395 [» ]
ProteinModelPortali P02468.
SMRi P02468. Positions 37-492, 680-1012, 1283-1522.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-41793N.
IntActi P02468. 4 interactions.
MINTi MINT-1031545.

PTM databases

PhosphoSitei P02468.

Proteomic databases

MaxQBi P02468.
PaxDbi P02468.
PRIDEi P02468.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:99914. Lamc1.

Phylogenomic databases

eggNOGi NOG235720.
HOGENOMi HOG000019301.
HOVERGENi HBG100808.
InParanoidi P02468.
PhylomeDBi P02468.

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

EvolutionaryTracei P02468.
PROi P02468.
SOURCEi Search...

Gene expression databases

CleanExi MM_LAMC1.
Genevestigatori P02468.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
InterProi IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 10 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view ]
PROSITEi PS00022. EGF_1. 8 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The laminin B2 chain has a multidomain structure homologous to the B1 chain."
    Sasaki M., Yamada Y.
    J. Biol. Chem. 262:17111-17117(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Primary structure of the mouse laminin B2 chain and comparison with laminin B1."
    Durkin M.E., Bartos B.B., Liu S.-H., Phillips S.L., Chung A.E.
    Biochemistry 27:5198-5204(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The laminin B2 chain promoter contains unique repeat sequences and is active in transient transfection."
    Ogawa K., Burbelo P.D., Sasaki M., Yamada Y.
    J. Biol. Chem. 263:8384-8389(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-239.
  4. "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 1391-1607.
  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-648; ASN-1105; ASN-1203; ASN-1221 AND ASN-1393.
  6. "Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site."
    Stetefeld J., Mayer U., Timpl R., Huber R.
    J. Mol. Biol. 257:644-657(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 771-932.
  7. "Structure of the nidogen binding LE module of the laminin gamma1 chain in solution."
    Baumgartner R., Czisch M., Mayer U., Poeschl E., Huber R., Timpl R., Holak T.A.
    J. Mol. Biol. 257:658-668(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 824-881.

Entry informationi

Entry nameiLAMC1_MOUSE
AccessioniPrimary (citable) accession number: P02468
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: September 3, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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