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Q71LX4

- TLN2_MOUSE

UniProt

Q71LX4 - TLN2_MOUSE

Protein

Talin-2

Gene

Tln2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    As a major component of focal adhesion plaques that links integrin to the actin cytoskeleton, may play an important role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques and strongly activates its kinase activity By similarity.By similarity

    GO - Molecular functioni

    1. structural constituent of cytoskeleton Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: InterPro
    2. cytoskeletal anchoring at plasma membrane Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Talin-2
    Gene namesi
    Name:Tln2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1917799. Tln2.

    Subcellular locationi

    Cell junctionfocal adhesion By similarity. Cell junctionsynapse By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity
    Note: Focal adhesion plaques and synapses.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: InterPro
    2. cytoplasm Source: UniProtKB-KW
    3. fascia adherens Source: MGI
    4. focal adhesion Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB-SubCell
    6. ruffle Source: InterPro
    7. synapse Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Synapse

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 23752375Talin-2PRO_0000219432Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1666 – 16661Phosphotyrosine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ71LX4.
    PaxDbiQ71LX4.
    PRIDEiQ71LX4.

    Expressioni

    Gene expression databases

    CleanExiMM_TLN2.
    GenevestigatoriQ71LX4.

    Interactioni

    Subunit structurei

    Interacts directly with PIP5K1C.By similarity

    Protein-protein interaction databases

    DIPiDIP-53098N.
    IntActiQ71LX4. 1 interaction.
    MINTiMINT-4997511.

    Structurei

    Secondary structure

    1
    2375
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi211 – 22616
    Helixi234 – 24916
    Turni254 – 2563
    Helixi264 – 2663
    Helixi270 – 2723
    Helixi278 – 28811
    Turni289 – 2913
    Helixi294 – 30714
    Turni309 – 3124
    Beta strandi314 – 3218
    Beta strandi328 – 3358
    Beta strandi337 – 3437
    Turni345 – 3473
    Beta strandi350 – 3556
    Helixi356 – 3583
    Beta strandi361 – 3655
    Beta strandi368 – 3725
    Helixi374 – 3763
    Beta strandi381 – 3844
    Helixi388 – 40720

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3G9WX-ray2.16A/B198-408[»]
    ProteinModelPortaliQ71LX4.
    SMRiQ71LX4. Positions 1-408, 489-915, 917-1047, 1209-1360, 1362-1794, 1887-2203, 2208-2375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ71LX4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini88 – 406319FERMPROSITE-ProRule annotationAdd
    BLAST
    Domaini2205 – 2375171I/LWEQPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni312 – 40695Interaction with PIP5K1CBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi862 – 94382Ala-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation
    Contains 1 I/LWEQ domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG324465.
    HOGENOMiHOG000006734.
    HOVERGENiHBG023870.
    KOiK06271.

    Family and domain databases

    Gene3Di1.20.1410.10. 4 hits.
    1.20.1420.10. 1 hit.
    1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR019749. 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.
    IPR015711. Talin-2.
    IPR015224. Talin_cent.
    IPR029071. Ubiquitin-rel_dom.
    IPR015009. Vinculin-bd_dom.
    IPR006077. Vinculin/catenin.
    [Graphical view]
    PANTHERiPTHR19981:SF15. PTHR19981:SF15. 1 hit.
    PfamiPF00373. 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]
    ProDomiPD011820. ILWEQ. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00295. B41. 1 hit.
    [Graphical view]
    SUPFAMiSSF109880. SSF109880. 1 hit.
    SSF109885. SSF109885. 5 hits.
    SSF47031. SSF47031. 1 hit.
    SSF47220. SSF47220. 4 hits.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    PS50945. I_LWEQ. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q71LX4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVALSLKICV RHCNVVKTMQ FEPSTAVYDA CRVIRERVPE AQTGQASDYG     50
    LFLSDEDPRK GIWLEAGRTL DYYMLRNGDI LEYKKKQRPQ KIRMLDGSVK 100
    TVMVDDSKTV GELLVTICSR IGITNYEEYS LIQETIEEKK EEGTGTLKKD 150
    RTLLRDERKM EKLKAKLHTD DDLNWLDHSR TFREQGVDEN ETLLLRRKFF 200
    YSDQNVDSRD PVQLNLLYVQ ARDDILNGSH PVSFEKACEF GGFQAQIQFG 250
    PHVEHKHKPG FLDLKEFLPK EYIKQRGAEK RIFQEHKNCG EMSEIEAKVK 300
    YVKLARSLRT YGVSFFLVKE KMKGKNKLVP RLLGITKDSV MRVDEKTKEV 350
    LQEWPLTTVK RWAASPKSFT LDFGEYQESY YSVQTTEGEQ ISQLIAGYID 400
    IILKKKQSKD RFGLEGDEES TMLEESVSPK KRSTILQQQF NRTGKAEHGS 450
    VALPAVMRSG SSGPETFNVG SMPSPQQQVM VGQMHRGHMP PLTSAQQALM 500
    GTINTSMHAV QQAQDDLSEL DSLPPLGQDM ASRVWVQNKV DESKHEIHSQ 550
    VDAITAGTAS VVNLTAGDPA DTDYTAVGCA ITTISSNLTE MSKGVKLLAA 600
    LMDDDVGSGE DLLRAARTLA GAVSDLLKAV QPTSGEPRQT VLTAAGSIGQ 650
    ASGDLLRQIG ENETDERFQD VLMSLAKAVA NAAAMLVLKA KNVAQVAEDT 700
    VLQNRVIAAA TQCALSTSQL VACAKVVSPT ISSPVCQEQL IEAGKLVDRS 750
    VENCVRACQA ATSDSELLKQ VSAAASVVSQ ALHDLLQHVR QFASRGEPIG 800
    RYDQATDTIM CVTESIFSSM GDAGEMVRQA RVLAQATSDL VNAMRSDAEA 850
    EIDMENSKKL LAAAKLLADS TARMVEAAKG AAANPENEDQ QQRLREAAEG 900
    LRVATNAAAQ NAIKKKIVNR LEVAAKQAAA AATQTIAASQ NAAISNKNPS 950
    AQQQLVQSCK AVADHIPQLV QGVRGSQAQA EDLSAQLALI ISSQNFLQPG 1000
    SKMVSSAKAA VPTVSDQAAA MQLSQCAKNL ATSLAELRTA SQKAHEACGP 1050
    MEIDSALNTV QTLKNELQDA KMAAAESQLK PLPGETLEKC AQDLGSTSKG 1100
    VGSSMAQLLT CAAQGNEHYT GVAARETAQA LKTLAQAARG VAASTNDPEA 1150
    AHAMLDSARD VMEGSAMLIQ EAKQALIAPG DTESQQRLAQ VAKAVSHSLN 1200
    NCVNCLPGQK DVDVALKSIG EASKKLLVDS LPPSTKPFQE AQSELNQAAA 1250
    DLNQSAGEVV HATRGQSGEL AAASGKFSDD FDEFLDAGIE MAGQAQTKED 1300
    QMQVIGNLKN ISMASSKLLL AAKSLSVDPG APNAKNLLAA AARAVTESIN 1350
    QLIMLCTQQA PGQKECDNAL RELETVKGML ENPNEPVSDL SYFDCIESVM 1400
    ENSKVLGESM AGISQNAKTG DLPAFGECVG IASKALCGLT EAAAQAAYLV 1450
    GISDPNSQAG HQGLVDPIQF ARANQAIQMA CQNLVDPGSS PSQVLSAATI 1500
    VAKHTSALCN ACRIASSKTA NPVAKRHFVQ SAKEVANSTA NLVKTIKALD 1550
    GDFSEDNRNK CRIATTPLIE AVENLTAFAS NPEFASIPAQ ISSEGSQAQE 1600
    PILVSAKTML ESSSYLIRTA RSLAINPKDP PTWSVLAGHS HTVSDSIKSL 1650
    ITSIRDKAPG QRECDYSIDG INRCIRDIEQ ASLAAVSQSL ATRDDISVEA 1700
    LQEQLTSVVQ EIGHLIDPIA TAARGEAAQL GHKVTQLASY FEPLILAAVG 1750
    VASKMLDHQQ QMTVLDQTKT LAESALQMLY AAKEGGGNPK AVHTAPEPKG 1800
    TFVDYQTTVV KYSKAIAVTA QEMIGFQIRT RVQDLGHGCI FLVQKAGALQ 1850
    VCPTDSYTKR ELIECARSVT EKVSLVLSAL QAGNKGTQAC ITAATAVSGI 1900
    IADLDTTIMF ATAGTLNAEN GETFADHREN ILKTAKALVE DTKLLVSGAA 1950
    STPDKLAQAA QSSAATITQL AEVVKLGAAS LGSNDPETQV VLINAIKDVA 2000
    KALSDLIGAT KGAASKPADD PSMYQLKGAA KVMVTNVTSL LKTVKAVEDE 2050
    ATRGTRALEA TIEYIKQELT VFQSKDIPEK TSSPEESIRM TKGITMATAK 2100
    AVAAGNSCRQ EDVIATANLS RKAVSDMLIA CKQASFYPDV SEEVRTRALR 2150
    YGTECTLGYL DLLEHVLVIL QKPTPELKHQ LAAFSKRVAG AVTELIQAAE 2200
    AMKGTEWVDP EDPTVIAETE LLGAAASIEA AAKKLEQLKP RAKPKQADET 2250
    LDFEEQILEA AKSIAAATSA LVKSASAAQR ELVAQGKVGS IPANAADDGQ 2300
    WSQGLISAAR MVAAATSSLC EAANASVQGH ASEEKLISSA KQVAASTAQL 2350
    LVACKVKADQ DSEAMKRLQA AGNAV 2375
    Length:2,375
    Mass (Da):253,621
    Last modified:July 27, 2011 - v3
    Checksum:i2264EEEC374476FC
    GO

    Sequence cautioni

    The sequence AAQ05019.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAC34927.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021V → K in BAC34927. (PubMed:16141072)Curated
    Sequence conflicti432 – 4321R → Q in AAQ05019. 1 PublicationCurated
    Sequence conflicti447 – 4471E → K in AAQ05019. 1 PublicationCurated
    Sequence conflicti1003 – 10031M → V in AAQ05019. 1 PublicationCurated
    Sequence conflicti1030 – 10301L → P in AAQ05019. 1 PublicationCurated
    Sequence conflicti1755 – 17551M → I in AAQ05019. 1 PublicationCurated
    Sequence conflicti1775 – 17751A → V in AAQ05019. 1 PublicationCurated
    Sequence conflicti1792 – 17921V → Q in AAQ05019. 1 PublicationCurated
    Sequence conflicti1795 – 17951A → S in AAQ05019. 1 PublicationCurated
    Sequence conflicti1816 – 18161I → V in AAQ05019. 1 PublicationCurated
    Sequence conflicti2047 – 20471V → A in AAQ05019. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC107740 Genomic DNA. No translation available.
    AC107755 Genomic DNA. No translation available.
    AC173343 Genomic DNA. No translation available.
    AF467081 mRNA. Translation: AAQ05019.1. Different initiation.
    AK052301 mRNA. Translation: BAC34927.1. Different initiation.
    RefSeqiNP_001074711.2. NM_001081242.2.
    UniGeneiMm.33645.

    Genome annotation databases

    GeneIDi70549.
    KEGGimmu:70549.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC107740 Genomic DNA. No translation available.
    AC107755 Genomic DNA. No translation available.
    AC173343 Genomic DNA. No translation available.
    AF467081 mRNA. Translation: AAQ05019.1 . Different initiation.
    AK052301 mRNA. Translation: BAC34927.1 . Different initiation.
    RefSeqi NP_001074711.2. NM_001081242.2.
    UniGenei Mm.33645.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3G9W X-ray 2.16 A/B 198-408 [» ]
    ProteinModelPortali Q71LX4.
    SMRi Q71LX4. Positions 1-408, 489-915, 917-1047, 1209-1360, 1362-1794, 1887-2203, 2208-2375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-53098N.
    IntActi Q71LX4. 1 interaction.
    MINTi MINT-4997511.

    Proteomic databases

    MaxQBi Q71LX4.
    PaxDbi Q71LX4.
    PRIDEi Q71LX4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 70549.
    KEGGi mmu:70549.

    Organism-specific databases

    CTDi 83660.
    MGIi MGI:1917799. Tln2.

    Phylogenomic databases

    eggNOGi NOG324465.
    HOGENOMi HOG000006734.
    HOVERGENi HBG023870.
    KOi K06271.

    Miscellaneous databases

    EvolutionaryTracei Q71LX4.
    NextBioi 331831.
    PROi Q71LX4.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_TLN2.
    Genevestigatori Q71LX4.

    Family and domain databases

    Gene3Di 1.20.1410.10. 4 hits.
    1.20.1420.10. 1 hit.
    1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR019749. 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.
    IPR015711. Talin-2.
    IPR015224. Talin_cent.
    IPR029071. Ubiquitin-rel_dom.
    IPR015009. Vinculin-bd_dom.
    IPR006077. Vinculin/catenin.
    [Graphical view ]
    PANTHERi PTHR19981:SF15. PTHR19981:SF15. 1 hit.
    Pfami PF00373. 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 ]
    ProDomi PD011820. ILWEQ. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00295. B41. 1 hit.
    [Graphical view ]
    SUPFAMi SSF109880. SSF109880. 1 hit.
    SSF109885. SSF109885. 5 hits.
    SSF47031. SSF47031. 1 hit.
    SSF47220. SSF47220. 4 hits.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    PS50945. I_LWEQ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-135.
      Strain: C57BL/6J.
      Tissue: Embryonic heart.
    3. "Expression of the newly identified Mus musculus talin 2 gene."
      Dubois A., Albiges-Rizo C., Block M., Faessler R.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-2375.
      Tissue: Kidney.
    4. "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-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.

    Entry informationi

    Entry nameiTLN2_MOUSE
    AccessioniPrimary (citable) accession number: Q71LX4
    Secondary accession number(s): E9QM49, Q8BWK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 98 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, 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