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P26039 (TLN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Talin-1
Gene names
Name:Tln1
Synonyms:Tln
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2541 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts.

Subunit structure

Interacts with NRAP and LAYN. Interacts with SYNM. Interacts with ITGB1; the interaction is prevented by competitive binding of ITGB1BP1 By similarity. Binds with high affinity to VCL and with low affinity to integrins. Interacts with APBB1IP; this inhibits VCL binding. Interacts with PTK2/FAK1. Interacts with PIP5K1C. Ref.4 Ref.9 Ref.13

Subcellular location

Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity. Cell surface. Cell junctionfocal adhesion. Note: Colocalizes with LAYN at the membrane ruffles By similarity. Localized preferentially in focal adhesions than fibrillar adhesions. Ref.8

Sequence similarities

Contains 1 FERM domain.

Contains 1 I/LWEQ domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: InterPro

cell-substrate junction assembly

Inferred from mutant phenotype PubMed 12867986. Source: MGI

cortical actin cytoskeleton organization

Inferred from mutant phenotype PubMed 12867986. Source: MGI

cytoskeletal anchoring at plasma membrane

Inferred from electronic annotation. Source: InterPro

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: InterPro

cell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

centrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from sequence or structural similarity. Source: HGNC

intracellular membrane-bounded organelle

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from sequence or structural similarity. Source: HGNC

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction Ref.11PubMed 17218263PubMed 20308429PubMed 20399778. Source: IntAct

structural constituent of cytoskeleton

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ITGB3P051063EBI-1039593,EBI-702847From a different organism.
VCLP120033EBI-1039593,EBI-1039563From a different organism.
VclQ647272EBI-1039593,EBI-432047

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25412541Talin-1
PRO_0000219429

Regions

Domain86 – 403318FERM
Domain2293 – 2533241I/LWEQ
Region280 – 435156Interaction with LAYN By similarity
Region1327 – 1948622Interaction with SYNM By similarity

Amino acid modifications

Modified residue4251Phosphoserine By similarity
Modified residue11161Phosphotyrosine Ref.5 Ref.6
Modified residue15441N6-acetyllysine Ref.10
Modified residue20311N6-acetyllysine By similarity
Modified residue20401Phosphoserine By similarity
Modified residue21151N6-acetyllysine By similarity

Natural variations

Natural variant11051L → P.
Natural variant21801K → M.

Experimental info

Sequence conflict6731K → N in CAA39588. Ref.1
Sequence conflict12271S → L in CAA39588. Ref.1

Secondary structure

..................................................................................................................................................................................................................................................... 2541
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26039 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 78832388E2392B8E

FASTA2,541269,821
        10         20         30         40         50         60 
MVALSLKISI GNVVKTMQFE PSTMVYDACR MIRERIPEAL AGPPNDFGLF LSDDDPKKGI 

        70         80         90        100        110        120 
WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI MVDDSKTVTD MLMTICARIG 

       130        140        150        160        170        180 
ITNHDEYSLV RELMEEKKDE GTGTLRKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL 

       190        200        210        220        230        240 
REQGVEEHET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG 

       250        260        270        280        290        300 
FQCQIQFGPH NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK 

       310        320        330        340        350        360 
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WSLTNIKRWA 

       370        380        390        400        410        420 
ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML 

       430        440        450        460        470        480 
EDSVSPKKST VLQQQYNRVG KVEHGSVALP AIMRSGASGP ENFQVGSMPP AQQQITSGQM 

       490        500        510        520        530        540 
HRGHMPPLTS AQQALTGTIN SSMQAVQAAQ ATLDDFETLP PLGQDAASKA WRKNKMDESK 

       550        560        570        580        590        600 
HEIHSQVDAI TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED 

       610        620        630        640        650        660 
EGGNGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE LLQQIGESDT 

       670        680        690        700        710        720 
DPHFQDVLMQ LAKAVASAAA ALVLKAKSVA QRTEDSGLQT QVIAAATQCA LSTSQLVACT 

       730        740        750        760        770        780 
KVVAPTISSP VCQEQLVEAG RLVAKAVEGC VSASQAATED GQLLRGVGAA ATAVTQALNE 

       790        800        810        820        830        840 
LLQHVKAHAT GAGPAGRYDQ ATDTILTVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI 

       850        860        870        880        890        900 
KADAEGESDL ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA 

       910        920        930        940        950        960 
TNAAAQNAIK KKLVQRLEHA AKQAAASATQ TIAAAQHAAS APKASAGPQP LLVQSCKAVA 

       970        980        990       1000       1010       1020 
EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM VAAAKASVPT IQDQASAMQL 

      1030       1040       1050       1060       1070       1080 
SQCAKNLGTA LAELRTAAQK AQEACGPLEM DSALSVVQNL EKDLQEIKAA ARDGKLKPLP 

      1090       1100       1110       1120       1130       1140 
GETMEKCTQD LGNSTKAVSS AIAKLLGEIA QGNENYAGIA ARDVAGGLRS LAQAARGVAA 

      1150       1160       1170       1180       1190       1200 
LTSDPAVQAI VLDTASDVLD KASSLIEEAK KASGHPGDPE SQQRLAQVAK AVTQALNRCV 

      1210       1220       1230       1240       1250       1260 
SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN QAATELVQAS 

      1270       1280       1290       1300       1310       1320 
RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ VVSNLKGISM SSSKLLLAAK 

      1330       1340       1350       1360       1370       1380 
ALSTDPASPN LKSQLAAAAR AVTDSINQLI TMCTQQAPGQ KECDNALRQL ETVRELLENP 

      1390       1400       1410       1420       1430       1440 
VQPINDMSYF GCLDSVMENS KVLGEAMTGI SQNAKNGNLP EFGDAIATAS KALCGFTEAA 

      1450       1460       1470       1480       1490       1500 
AQAAYLVGVS DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK 

      1510       1520       1530       1540       1550       1560 
HTSALCNSCR LASARTANPT AKRQFVQSAK EVANSTANLV KTIKALDGDF TEENRAQCRA 

      1570       1580       1590       1600       1610       1620 
ATAPLLEAVD NLSAFASNPE FSSVPAQISP EGRAAMEPIV ISAKTMLESA GGLIQTARAL 

      1630       1640       1650       1660       1670       1680 
AVNPRDPPRW SVLAGHSRTV SDSIKKLITS MRDKAPGQLE CETAIAALNS CLRDLDQASL 

      1690       1700       1710       1720       1730       1740 
AAVSQQLAPR EGISQEALHT QMLTAVQEIS HLIEPLASAA RAEASQLGHK VSQMAQYFEP 

      1750       1760       1770       1780       1790       1800 
LTLAAVGAAS KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV 

      1810       1820       1830       1840       1850       1860 
QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGDPEGSF VDYQTTMVRT 

      1870       1880       1890       1900       1910       1920 
AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASQA KPAAVAAENE EIGAHIKHRV 

      1930       1940       1950       1960       1970       1980 
QELGHGCSAL VTKAGALQCS PSDVYTKKEL IECARRVSEK VSHVLAALQA GNRGTQACIT 

      1990       2000       2010       2020       2030       2040 
AASAVSGIIA DLDTTIMFAT AGTLNREGAE TFADHREGIL KTAKVLVEDT KVLVQNAAGS 

      2050       2060       2070       2080       2090       2100 
QEKLAQAAQS SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA 

      2110       2120       2130       2140       2150       2160 
AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT EHIRQELAVF 

      2170       2180       2190       2200       2210       2220 
CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED VIATANLSRR AIADMLRACK 

      2230       2240       2250       2260       2270       2280 
EAAFHPEVAP DVRLRALHYG RECANGYLEL LDHVLLTLQK PNPDLKQQLT GHSKRVAGSV 

      2290       2300       2310       2320       2330       2340 
TELIQAAEAM KGTEWVDPED PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN 

      2350       2360       2370       2380       2390       2400 
FEEQILEAAK SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV 

      2410       2420       2430       2440       2450       2460 
AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS EAMKRLQAAG 

      2470       2480       2490       2500       2510       2520 
NAVKRASDNL VKAAQKAAAF EDQENETVVV KEKMVGGIAQ IIAAQEEMLR KERELEEARK 

      2530       2540 
KLAQIRQQQY KFLPSELRDE H 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and domain structure of talin."
Rees D.J.G., Ades S.A., Singer S.J., Hynes R.O.
Nature 347:685-689(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Fibroblast.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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].
Tissue: Mammary gland.
[4]"Interaction of focal adhesion kinase with cytoskeletal protein talin."
Chen H.C., Appeddu P.A., Parsons J.T., Hildebrand J.D., Schaller M.D., Guan J.L.
J. Biol. Chem. 270:16995-16999(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK2/FAK1.
[5]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[7]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition."
Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.
J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover."
Goult B.T., Zacharchenko T., Bate N., Tsang R., Hey F., Gingras A.R., Elliott P.R., Roberts G.C., Ballestrem C., Critchley D.R., Barsukov I.L.
J. Biol. Chem. 288:8238-8249(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APBB1IP AND VCL.
[10]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[11]"Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle."
Papagrigoriou E., Gingras A.R., Barsukov I.L., Bate N., Fillingham I.J., Patel B., Frank R., Ziegler W.H., Roberts G.C.K., Critchley D.R., Emsley J.
EMBO J. 23:2942-2951(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 482-789 IN COMPLEX WITH VCL.
[12]"Structural basis for phosphatidylinositol phosphate kinase type Igamma binding to talin at focal adhesions."
de Pereda J.M., Wegener K.L., Santelli E., Bate N., Ginsberg M.H., Critchley D.R., Campbell I.D., Liddington R.C.
J. Biol. Chem. 280:8381-8386(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 209-410 IN COMPLEX WITH PIP5K1C.
[13]"A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head."
Fillingham I., Gingras A.R., Papagrigoriou E., Patel B., Emsley J., Critchley D.R., Roberts G.C.K., Barsukov I.L.
Structure 13:65-74(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 755-889, INTERACTION WITH VCL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56123 mRNA. Translation: CAA39588.1.
AL732506 Genomic DNA. Translation: CAM17190.1.
BC018557 mRNA. Translation: AAH18557.1.
BC150810 mRNA. Translation: AAI50811.1.
CCDSCCDS18101.1.
PIRS11661.
RefSeqNP_035732.2. NM_011602.5.
UniGeneMm.208601.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJ7X-ray2.50A/B/C482-655[»]
1SJ8X-ray2.60A482-789[»]
1T01X-ray2.06B605-628[»]
1U89NMR-A755-889[»]
1XWXmodel-A486-889[»]
1Y19X-ray2.60B/D/F/H/J/L209-410[»]
1ZW3X-ray3.30B1628-1652[»]
2B0HNMR-A1843-1973[»]
2G35NMR-A305-404[»]
2JSWNMR-A2300-2482[»]
2KBBNMR-A1655-1822[»]
2KC1NMR-A1-85[»]
2KC2NMR-A86-202[»]
2KGXNMR-A1655-1822[»]
B311-401[»]
2KMANMR-A1-202[»]
2KVPNMR-A1815-1973[»]
2L10NMR-A1206-1357[»]
2L7ANMR-A787-911[»]
2L7NNMR-A1046-1207[»]
2LQGNMR-A913-1044[»]
2QDQX-ray2.20A/B2494-2541[»]
2X0CX-ray2.00A1359-1659[»]
3DYJX-ray1.85A/B1974-2293[»]
3IVFX-ray1.94A1-400[»]
3S90X-ray1.97C/D1512-1546[»]
4F7GX-ray2.05A206-405[»]
B1654-1847[»]
DisProtDP00653.
ProteinModelPortalP26039.
SMRP26039. Positions 1-400, 485-911, 913-1044, 1046-1357, 1359-1973, 1975-2291, 2296-2482, 2496-2529.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204222. 5 interactions.
DIPDIP-647N.
IntActP26039. 12 interactions.
MINTMINT-258500.

PTM databases

PhosphoSiteP26039.

Proteomic databases

MaxQBP26039.
PaxDbP26039.
PRIDEP26039.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030187; ENSMUSP00000030187; ENSMUSG00000028465.
GeneID21894.
KEGGmmu:21894.
UCSCuc008sqe.2. mouse.

Organism-specific databases

CTD7094.
MGIMGI:1099832. Tln1.

Phylogenomic databases

eggNOGNOG324465.
GeneTreeENSGT00550000074542.
HOVERGENHBG023870.
InParanoidA2AIM8.
KOK06271.
OMAGAHIKHR.
OrthoDBEOG7TBC1J.
TreeFamTF314677.

Gene expression databases

ArrayExpressP26039.
BgeeP26039.
CleanExMM_TLN1.
GenevestigatorP26039.

Family and domain databases

Gene3D1.20.1410.10. 3 hits.
1.20.1420.10. 1 hit.
1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR002558. ILWEQ_dom.
IPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
IPR015710. Talin-1.
IPR015224. Talin_cent.
IPR029071. Ubiquitin-rel_dom.
IPR015009. Vinculin-bd_dom.
IPR006077. Vinculin/catenin.
[Graphical view]
PANTHERPTHR19981:SF7. PTHR19981:SF7. 1 hit.
PfamPF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF01608. I_LWEQ. 1 hit.
PF02174. IRS. 1 hit.
PF09141. Talin_middle. 1 hit.
PF08913. VBS. 2 hits.
[Graphical view]
ProDomPD011820. ILWEQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00295. B41. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view]
SUPFAMSSF109880. SSF109880. 1 hit.
SSF109885. SSF109885. 4 hits.
SSF47031. SSF47031. 1 hit.
SSF47220. SSF47220. 5 hits.
SSF54236. SSF54236. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTLN1. mouse.
EvolutionaryTraceP26039.
NextBio301428.
PROP26039.
SOURCESearch...

Entry information

Entry nameTLN1_MOUSE
AccessionPrimary (citable) accession number: P26039
Secondary accession number(s): A2AIM8, Q8VEF0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot