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Q09666

- AHNK_HUMAN

UniProt

Q09666 - AHNK_HUMAN

Protein

Neuroblast differentiation-associated protein AHNAK

Gene

AHNAK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    May be required for neuronal cell differentiation.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. S100 protein binding Source: UniProt
    4. structural molecule activity conferring elasticity Source: UniProt

    GO - Biological processi

    1. protein oligomerization Source: UniProt
    2. regulation of RNA splicing Source: UniProt
    3. regulation of voltage-gated calcium channel activity Source: UniProt

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuroblast differentiation-associated protein AHNAK
    Alternative name(s):
    Desmoyokin
    Gene namesi
    Name:AHNAK
    Synonyms:PM227
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:347. AHNAK.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProt
    2. cell-cell contact zone Source: UniProt
    3. costamere Source: UniProt
    4. cytoplasm Source: UniProt
    5. cytosol Source: UniProt
    6. extracellular vesicular exosome Source: UniProt
    7. lysosomal membrane Source: UniProtKB
    8. membrane Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. plasma membrane Source: UniProt
    11. sarcolemma Source: UniProt
    12. T-tubule Source: UniProt
    13. vesicle Source: UniProt

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24640.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 58905890Neuroblast differentiation-associated protein AHNAKPRO_0000064504Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei41 – 411Phosphoserine5 Publications
    Modified residuei93 – 931Phosphoserine4 Publications
    Modified residuei101 – 1011Phosphothreonine1 Publication
    Modified residuei135 – 1351Phosphoserine2 Publications
    Modified residuei177 – 1771Phosphoserine2 Publications
    Modified residuei210 – 2101Phosphoserine1 Publication
    Modified residuei212 – 2121Phosphoserine1 Publication
    Modified residuei216 – 2161Phosphoserine1 Publication
    Modified residuei490 – 4901Phosphothreonine4 Publications
    Modified residuei511 – 5111Phosphoserine9 Publications
    Modified residuei559 – 5591Phosphoserine2 Publications
    Modified residuei570 – 5701Phosphoserine3 Publications
    Modified residuei793 – 7931Phosphoserine2 Publications
    Modified residuei1068 – 10681Phosphoserine1 Publication
    Modified residuei1192 – 11921Phosphothreonine1 Publication
    Modified residuei1286 – 12861Phosphoserine1 Publication
    Modified residuei1986 – 19861Phosphothreonine1 Publication
    Modified residuei2181 – 21811Phosphothreonine1 Publication
    Modified residuei2309 – 23091Phosphothreonine1 Publication
    Modified residuei2397 – 23971Phosphoserine2 Publications
    Modified residuei2670 – 26701Phosphoserine1 Publication
    Modified residuei2798 – 27981Phosphoserine1 Publication
    Modified residuei2832 – 28321Phosphothreonine1 Publication
    Modified residuei2845 – 28451Phosphothreonine1 Publication
    Modified residuei3054 – 30541Phosphoserine1 Publication
    Modified residuei3409 – 34091Phosphoserine1 Publication
    Modified residuei3412 – 34121Phosphoserine1 Publication
    Modified residuei3426 – 34261Phosphoserine1 Publication
    Modified residuei3716 – 37161Phosphothreonine1 Publication
    Modified residuei3836 – 38361Phosphoserine1 Publication
    Modified residuei4092 – 40921Phosphoserine1 Publication
    Modified residuei4100 – 41001Phosphothreonine2 Publications
    Modified residuei4220 – 42201Phosphoserine1 Publication
    Modified residuei4430 – 44301Phosphothreonine1 Publication
    Modified residuei4516 – 45161Phosphoserine1 Publication
    Modified residuei4684 – 46841Phosphoserine1 Publication
    Modified residuei4766 – 47661Phosphothreonine1 Publication
    Modified residuei4812 – 48121Phosphoserine1 Publication
    Modified residuei4903 – 49031Phosphoserine1 Publication
    Modified residuei4960 – 49601Phosphoserine2 Publications
    Modified residuei4986 – 49861Phosphoserine2 Publications
    Modified residuei4993 – 49931Phosphoserine1 Publication
    Modified residuei5009 – 50091Phosphothreonine1 Publication
    Modified residuei5077 – 50771Phosphoserine2 Publications
    Modified residuei5099 – 50991Phosphoserine3 Publications
    Modified residuei5110 – 51101Phosphoserine3 Publications
    Modified residuei5125 – 51251Phosphoserine1 Publication
    Modified residuei5332 – 53321Phosphoserine1 Publication
    Modified residuei5386 – 53861Phosphoserine1 Publication
    Modified residuei5400 – 54001Phosphoserine1 Publication
    Modified residuei5415 – 54151Phosphothreonine1 Publication
    Modified residuei5448 – 54481Phosphoserine3 Publications
    Modified residuei5552 – 55521Phosphoserine3 Publications
    Modified residuei5620 – 56201Phosphoserine1 Publication
    Modified residuei5731 – 57311Phosphoserine5 Publications
    Modified residuei5739 – 57391Phosphoserine1 Publication
    Modified residuei5749 – 57491Phosphoserine4 Publications
    Modified residuei5752 – 57521Phosphoserine6 Publications
    Modified residuei5763 – 57631Phosphoserine4 Publications
    Modified residuei5780 – 57801Phosphoserine2 Publications
    Modified residuei5782 – 57821Phosphoserine2 Publications
    Modified residuei5790 – 57901Phosphoserine1 Publication
    Modified residuei5793 – 57931Phosphoserine1 Publication
    Modified residuei5794 – 57941Phosphothreonine1 Publication
    Modified residuei5824 – 58241Phosphothreonine1 Publication
    Modified residuei5830 – 58301Phosphoserine2 Publications
    Modified residuei5841 – 58411Phosphoserine3 Publications
    Modified residuei5857 – 58571Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ09666.
    PaxDbiQ09666.
    PeptideAtlasiQ09666.
    PRIDEiQ09666.

    PTM databases

    PhosphoSiteiQ09666.

    Expressioni

    Gene expression databases

    ArrayExpressiQ09666.
    BgeeiQ09666.
    CleanExiHS_AHNAK.
    GenevestigatoriQ09666.

    Organism-specific databases

    HPAiHPA019010.
    HPA019070.
    HPA026643.

    Interactioni

    Subunit structurei

    Interacts with DYSF; the interaction is direct and Ca2+-independent.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EGFRP005333EBI-2555881,EBI-297353

    Protein-protein interaction databases

    BioGridi122494. 29 interactions.
    IntActiQ09666. 23 interactions.
    MINTiMINT-4998803.
    STRINGi9606.ENSP00000367263.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DRWX-ray3.50E/F5654-5673[»]
    4FTGX-ray2.51E5654-5673[»]
    4HRGX-ray2.00C/D5655-5668[»]
    ProteinModelPortaliQ09666.
    SMRiQ09666. Positions 8-91.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 9082PDZPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi4971 – 49799Nuclear localization signalSequence Analysis
    Motifi5019 – 50279Nuclear localization signalSequence Analysis
    Motifi5034 – 50396Nuclear localization signalSequence Analysis
    Motifi5706 – 571611Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi5772 – 57798Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5458 – 5654197Gly-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000033865.
    HOVERGENiHBG104864.
    InParanoidiQ09666.
    OMAiVASFHRD.
    OrthoDBiEOG7BCNB3.
    PhylomeDBiQ09666.
    TreeFamiTF350595.

    Family and domain databases

    Gene3Di2.30.42.10. 1 hit.
    InterProiIPR001478. PDZ.
    [Graphical view]
    SMARTiSM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    PROSITEiPS50106. PDZ. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q09666-1) [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

    MEKEETTREL LLPNWQGSGS HGLTIAQRDD GVFVQEVTQN SPAARTGVVK     50
    EGDQIVGATI YFDNLQSGEV TQLLNTMGHH TVGLKLHRKG DRSPEPGQTW 100
    TREVFSSCSS EVVLSGDDEE YQRIYTTKIK PRLKSEDGVE GDLGETQSRT 150
    ITVTRRVTAY TVDVTGREGA KDIDISSPEF KIKIPRHELT EISNVDVETQ 200
    SGKTVIRLPS GSGAASPTGS AVDIRAGAIS ASGPELQGAG HSKLQVTMPG 250
    IKVGGSGVNV NAKGLDLGGR GGVQVPAVDI SSSLGGRAVE VQGPSLESGD 300
    HGKIKFPTMK VPKFGVSTGR EGQTPKAGLR VSAPEVSVGH KGGKPGLTIQ 350
    APQLEVSVPS ANIEGLEGKL KGPQITGPSL EGDLGLKGAK PQGHIGVDAS 400
    APQIGGSITG PSVEVQAPDI DVQGPGSKLN VPKMKVPKFS VSGAKGEETG 450
    IDVTLPTGEV TVPGVSGDVS LPEIATGGLE GKMKGTKVKT PEMIIQKPKI 500
    SMQDVDLSLG SPKLKGDIKV SAPGVQGDVK GPQVALKGSR VDIETPNLEG 550
    TLTGPRLGSP SGKTGTCRIS MSEVDLNVAA PKVKGGVDVT LPRVEGKVKV 600
    PEVDVRGPKV DVSAPDVEAH GPEWNLKMPK MKMPTFSTPG AKGEGPDVHM 650
    TLPKGDISIS GPKVNVEAPD VNLEGLGGKL KGPDVKLPDM SVKTPKISMP 700
    DVDLHVKGTK VKGEYDVTVP KLEGELKGPK VDIDAPDVDV HGPDWHLKMP 750
    KMKMPKFSVP GFKAEGPEVD VNLPKADVDI SGPKIDVTAP DVSIEEPEGK 800
    LKGPKFKMPE MNIKVPKISM PDVDLHLKGP NVKGEYDVTM PKVESEIKVP 850
    DVELKSAKMD IDVPDVEVQG PDWHLKMPKM KMPKFSMPGF KAEGPEVDVN 900
    LPKADVDISG PKVGVEVPDV NIEGPEGKLK GPKFKMPEMN IKAPKISMPD 950
    VDLHMKGPKV KGEYDMTVPK LEGDLKGPKV DVSAPDVEMQ GPDWNLKMPK 1000
    IKMPKFSMPS LKGEGPEFDV NLSKANVDIS APKVDTNAPD LSLEGPEGKL 1050
    KGPKFKMPEM HFRAPKMSLP DVDLDLKGPK MKGNVDISAP KIEGEMQVPD 1100
    VDIRGPKVDI KAPDVEGQGL DWSLKIPKMK MPKFSMPSLK GEGPEVDVNL 1150
    PKADVVVSGP KVDIEAPDVS LEGPEGKLKG PKFKMPEMHF KTPKISMPDV 1200
    DLHLKGPKVK GDVDVSVPKV EGEMKVPDVE IKGPKMDIDA PDVEVQGPDW 1250
    HLKMPKMKMP KFSMPGFKGE GREVDVNLPK ADIDVSGPKV DVEVPDVSLE 1300
    GPEGKLKGPK FKMPEMHFKA PKISMPDVDL NLKGPKLKGD VDVSLPEVEG 1350
    EMKVPDVDIK GPKVDISAPD VDVHGPDWHL KMPKVKMPKF SMPGFKGEGP 1400
    EVDVKLPKAD VDVSGPKMDA EVPDVNIEGP DAKLKGPKFK MPEMSIKPQK 1450
    ISIPDVGLHL KGPKMKGDYD VTVPKVEGEI KAPDVDIKGP KVDINAPDVE 1500
    VHGPDWHLKM PKVKMPKFSM PGFKGEGPEV DMNLPKADLG VSGPKVDIDV 1550
    PDVNLEAPEG KLKGPKFKMP SMNIQTHKIS MPDVGLNLKA PKLKTDVDVS 1600
    LPKVEGDLKG PEIDVKAPKM DVNVGDIDIE GPEGKLKGPK FKMPEMHFKA 1650
    PKISMPDVDL HLKGPKVKGD MDVSVPKVEG EMKVPDVDIK GPKVDIDAPD 1700
    VEVHDPDWHL KMPKMKMPKF SMPGFKAEGP EVDVNLPKAD IDVSGPSVDT 1750
    DAPDLDIEGP EGKLKGSKFK MPKLNIKAPK VSMPDVDLNL KGPKLKGEID 1800
    ASVPELEGDL RGPQVDVKGP FVEAEVPDVD LECPDAKLKG PKFKMPEMHF 1850
    KAPKISMPDV DLHLKGPKVK GDADVSVPKL EGDLTGPSVG VEVPDVELEC 1900
    PDAKLKGPKF KMPDMHFKAP KISMPDVDLH LKGPKVKGDV DVSVPKLEGD 1950
    LTGPSVGVEV PDVELECPDA KLKGPKFKMP EMHFKTPKIS MPDVDLHLKG 2000
    PKVKGDMDVS VPKVEGEMKV PDVDIKGPKM DIDAPDVDVH GPDWHLKMPK 2050
    MKMPKFSMPG FKAEGPEVDV NLPKADVVVS GPKVDVEVPD VSLEGPEGKL 2100
    KGPKLKMPEM HFKAPKISMP DVDLHLKGPK VKGDVDVSLP KLEGDLTGPS 2150
    VDVEVPDVEL ECPDAKLKGP KFKMPEMHFK TPKISMPDVN LNLKGPKVKG 2200
    DMDVSVPKVE GEMKVPDVDI RGPKVDIDAP DVDVHGPDWH LKMPKMKMPK 2250
    FSMPGFKGEG PEVDVNLPKA DVDVSGPKVD VEVPDVSLEG PEGKLKGPKF 2300
    KMPEMHFKTP KISMPDVDFN LKGPKIKGDV DVSAPKLEGE LKGPELDVKG 2350
    PKLDADMPEV AVEGPNGKWK TPKFKMPDMH FKAPKISMPD LDLHLKSPKA 2400
    KGEVDVDVPK LEGDLKGPHV DVSGPDIDIE GPEGKLKGPK FKMPDMHFKA 2450
    PNISMPDVDL NLKGPKIKGD VDVSVPEVEG KLEVPDMNIR GPKVDVNAPD 2500
    VQAPDWHLKM PKMKMPKFSM PGFKAEGPEV DVNLPKADVD ISGPKVDIEG 2550
    PDVNIEGPEG KLKGPKLKMP EMNIKAPKIS MPDFDLHLKG PKVKGDVDVS 2600
    LPKVEGDLKG PEVDIKGPKV DINAPDVGVQ GPDWHLKMPK VKMPKFSMPG 2650
    FKGEGPDGDV KLPKADIDVS GPKVDIEGPD VNIEGPEGKL KGPKFKMPEM 2700
    NIKAPKISMP DIDLNLKGPK VKGDVDVSLP KVEGDLKGPE VDIKGPKVDI 2750
    DAPDVDVHGP DWHLKMPKIK MPKISMPGFK GEGPDVDVNL PKADIDVSGP 2800
    KVDVECPDVN IEGPEGKWKS PKFKMPEMHF KTPKISMPDI DLNLTGPKIK 2850
    GDVDVTGPKV EGDLKGPEVD LKGPKVDIDV PDVNVQGPDW HLKMPKMKMP 2900
    KFSMPGFKAE GPEVDVNLPK ADVDVSGPKV DVEGPDVNIE GPEGKLKGPK 2950
    FKMPEMNIKA PKIPMPDFDL HLKGPKVKGD VDISLPKVEG DLKGPEVDIR 3000
    GPQVDIDVPD VGVQGPDWHL KMPKVKMPKF SMPGFKGEGP DVDVNLPKAD 3050
    LDVSGPKVDI DVPDVNIEGP EGKLKGPKFK MPEMNIKAPK ISMPDIDLNL 3100
    KGPKVKGDMD VSLPKVEGDM KVPDVDIKGP KVDINAPDVD VQGPDWHLKM 3150
    PKIKMPKISM PGFKGEGPEV DVNLPKADLD VSGPKVDVDV PDVNIEGPDA 3200
    KLKGPKFKMP EMNIKAPKIS MPDLDLNLKG PKMKGEVDVS LANVEGDLKG 3250
    PALDIKGPKI DVDAPDIDIH GPDAKLKGPK LKMPDMHVNM PKISMPEIDL 3300
    NLKGSKLKGD VDVSGPKLEG DIKAPSLDIK GPEVDVSGPK LNIEGKSKKS 3350
    RFKLPKFNFS GSKVQTPEVD VKGKKPDIDI TGPKVDINAP DVEVQGKVKG 3400
    SKFKMPFLSI SSPKVSMPDV ELNLKSPKVK GDLDIAGPNL EGDFKGPKVD 3450
    IKAPEVNLNA PDVDVHGPDW NLKMPKMKMP KFSVSGLKAE GPDVAVDLPK 3500
    GDINIEGPSM NIEGPDLNVE GPEGGLKGPK FKMPDMNIKA PKISMPDIDL 3550
    NLKGPKVKGD VDISLPKLEG DLKGPEVDIK GPKVDINAPD VDVHGPDWHL 3600
    KMPKVKMPKF SMPGFKGEGP EVDVTLPKAD IDISGPNVDV DVPDVNIEGP 3650
    DAKLKGPKFK MPEMNIKAPK ISMPDFDLNL KGPKMKGDVV VSLPKVEGDL 3700
    KGPEVDIKGP KVDIDTPDIN IEGSEGKFKG PKFKIPEMHL KAPKISMPDI 3750
    DLNLKGPKVK GDVDVSLPKM EGDLKGPEVD IKGPKVDINA PDVDVQGPDW 3800
    HLKMPKVKMP KFSMPGFKGE GPDVDVNLPK ADLDVSGPKV DIDVPDVNIE 3850
    GPEGKLKGPK FKMPEMNIKA PKISMPDIDL NLKGPKVKGD MDVSLPKVEG 3900
    DMQVPDLDIK GPKVDINAPD VDVRGPDWHL KMPKIKMPKI SMPGFKGEGP 3950
    EVDVNLPKAD LDVSGPKVDV DVPDVNIEGP DAKLKGPKFK MPEMNIKAPK 4000
    ISMPDFDLHL KGPKVKGDVD VSLPKMEGDL KAPEVDIKGP KVDIDAPDVD 4050
    VHGPDWHLKM PKVKMPKFSM PGFKGEGPEV DVNLPKADID VSGPKVDIDT 4100
    PDIDIHGPEG KLKGPKFKMP DLHLKAPKIS MPEVDLNLKG PKMKGDVDVS 4150
    LPKVEGDLKG PEVDIKGPKV DIDVPDVDVQ GPDWHLKMPK VKMPKFSMPG 4200
    FKGEGPDVDV NLPKADLDVS GPKVDIDVPD VNIEGPDAKL KGPKFKMPEM 4250
    NIKAPKISMP DFDLHLKGPK VKGDVDVSLP KVEGDLKGPE VDIKGPKVDI 4300
    DAPDVDVHGP DWHLKMPKVK MPKFSMPGFK GEGPDVDVTL PKADIEISGP 4350
    KVDIDAPDVS IEGPDAKLKG PKFKMPEMNI KAPKISMPDI DFNLKGPKVK 4400
    GDVDVSLPKV EGDLKGPEID IKGPSLDIDT PDVNIEGPEG KLKGPKFKMP 4450
    EMNIKAPKIS MPDFDLHLKG PKVKGDVDVS LPKVESDLKG PEVDIEGPEG 4500
    KLKGPKFKMP DVHFKSPQIS MSDIDLNLKG PKIKGDMDIS VPKLEGDLKG 4550
    PKVDVKGPKV GIDTPDIDIH GPEGKLKGPK FKMPDLHLKA PKISMPEVDL 4600
    NLKGPKVKGD MDISLPKVEG DLKGPEVDIR DPKVDIDVPD VDVQGPDWHL 4650
    KMPKVKMPKF SMPGFKGEGP DVDVNLPKAD IDVSGPKVDV DVPDVNIEGP 4700
    DAKLKGPKFK MPEMSIKAPK ISMPDIDLNL KGPKVKGDVD VTLPKVEGDL 4750
    KGPEADIKGP KVDINTPDVD VHGPDWHLKM PKVKMPKFSM PGFKGEGPDV 4800
    DVSLPKADID VSGPKVDVDI PDVNIEGPDA KLKGPKFKMP EINIKAPKIS 4850
    IPDVDLDLKG PKVKGDFDVS VPKVEGTLKG PEVDLKGPRL DFEGPDAKLS 4900
    GPSLKMPSLE ISAPKVTAPD VDLHLKAPKI GFSGPKLEGG EVDLKGPKVE 4950
    APSLDVHMDS PDINIEGPDV KIPKFKKPKF GFGAKSPKAD IKSPSLDVTV 5000
    PEAELNLETP EISVGGKGKK SKFKMPKIHM SGPKIKAKKQ GFDLNVPGGE 5050
    IDASLKAPDV DVNIAGPDAA LKVDVKSPKT KKTMFGKMYF PDVEFDIKSP 5100
    KFKAEAPLPS PKLEGELQAP DLELSLPAIH VEGLDIKAKA PKVKMPDVDI 5150
    SVPKIEGDLK GPKVQANLGA PDINIEGLDA KVKTPSFGIS APQVSIPDVN 5200
    VNLKGPKIKG DVPSVGLEGP DVDLQGPEAK IKFPKFSMPK IGIPGVKMEG 5250
    GGAEVHAQLP SLEGDLRGPD VKLEGPDVSL KGPGVDLPSV NLSMPKVSGP 5300
    DLDLNLKGPS LKGDLDASVP SMKVHAPGLN LSGVGGKMQV GGDGVKVPGI 5350
    DATTKLNVGA PDVTLRGPSL QGDLAVSGDI KCPKVSVGAP DLSLEASEGS 5400
    IKLPKMKLPQ FGISTPGSDL HVNAKGPQVS GELKGPGVDV NLKGPRISAP 5450
    NVDFNLEGPK VKGSLGATGE IKGPTVGGGL PGIGVQGLEG NLQMPGIKSS 5500
    GCDVNLPGVN VKLPTGQISG PEIKGGLKGS EVGFHGAAPD ISVKGPAFNM 5550
    ASPESDFGIN LKGPKIKGGA DVSGGVSAPD ISLGEGHLSV KGSGGEWKGP 5600
    QVSSALNLDT SKFAGGLHFS GPKVEGGVKG GQIGLQAPGL SVSGPQGHLE 5650
    SGSGKVTFPK MKIPKFTFSG RELVGREMGV DVHFPKAEAS IQAGAGDGEW 5700
    EESEVKLKKS KIKMPKFNFS KPKGKGGVTG SPEASISGSK GDLKSSKASL 5750
    GSLEGEAEAE ASSPKGKFSL FKSKKPRHRS NSFSDEREFS GPSTPTGTLE 5800
    FEGGEVSLEG GKVKGKHGKL KFGTFGGLGS KSKGHYEVTG SDDETGKLQG 5850
    SGVSLASKKS RLSSSSSNDS GNKVGIQLPE VELSVSTKKE 5890
    Length:5,890
    Mass (Da):629,101
    Last modified:November 13, 2007 - v2
    Checksum:iA82FC9645FDCA8DC
    GO
    Isoform 2 (identifier: Q09666-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         115-149: SGDDEEYQRIYTTKIKPRLKSEDGVEGDLGETQSR → NTPQPSALECKDQNKQKEASSQAGAVSVSTPNAGL
         150-5890: Missing.

    Show »
    Length:149
    Mass (Da):16,061
    Checksum:i4CB0471C1B60F60D
    GO

    Sequence cautioni

    The sequence AAA69899.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti288 – 2881A → P in AAA69899. (PubMed:1608957)Curated
    Sequence conflicti302 – 3021G → A in AAA69899. (PubMed:1608957)Curated
    Sequence conflicti1156 – 11561V → D in AAA69899. (PubMed:1608957)Curated
    Sequence conflicti1737 – 17371P → R in AAA69899. (PubMed:1608957)Curated
    Sequence conflicti1821 – 18211F → L in AAA69899. (PubMed:1608957)Curated
    Sequence conflicti4614 – 46141S → T in AAA69898. (PubMed:1608957)Curated
    Sequence conflicti4627 – 46271V → A in AAA69898. (PubMed:1608957)Curated
    Sequence conflicti4630 – 46312RD → KG in AAA69898. (PubMed:1608957)Curated
    Sequence conflicti4637 – 46382DV → NT in AAA69898. (PubMed:1608957)Curated
    Sequence conflicti4644 – 46441Q → H in AAA69898. (PubMed:1608957)Curated
    Sequence conflicti4830 – 48301A → P in AAA69898. (PubMed:1608957)Curated
    Sequence conflicti4834 – 48341G → V in AAA69898. (PubMed:1608957)Curated
    Sequence conflicti4837 – 48371F → V in AAA69898. (PubMed:1608957)Curated
    Sequence conflicti4984 – 49841A → P in AAA69898. (PubMed:1608957)Curated
    Sequence conflicti5445 – 54451P → S in AAA69898. (PubMed:1608957)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti962 – 9621G → V.
    Corresponds to variant rs664761 [ dbSNP | Ensembl ].
    VAR_039058
    Natural varianti2114 – 21141A → T.
    Corresponds to variant rs1298288 [ dbSNP | Ensembl ].
    VAR_039059
    Natural varianti2247 – 22471K → T.
    Corresponds to variant rs61524789 [ dbSNP | Ensembl ].
    VAR_061551
    Natural varianti2439 – 24391P → L.
    Corresponds to variant rs11824660 [ dbSNP | Ensembl ].
    VAR_039060
    Natural varianti3003 – 30031Q → K.
    Corresponds to variant rs566144 [ dbSNP | Ensembl ].
    VAR_039061
    Natural varianti3190 – 31901V → I.
    Corresponds to variant rs11231129 [ dbSNP | Ensembl ].
    VAR_039062
    Natural varianti3724 – 37241S → P.
    Corresponds to variant rs11231128 [ dbSNP | Ensembl ].
    VAR_039063
    Natural varianti4304 – 43041D → G.
    Corresponds to variant rs11828907 [ dbSNP | Ensembl ].
    VAR_061552
    Natural varianti4561 – 45611G → D.
    Corresponds to variant rs12795508 [ dbSNP | Ensembl ].
    VAR_039064
    Natural varianti4611 – 46111M → V.
    Corresponds to variant rs12801302 [ dbSNP | Ensembl ].
    VAR_039065
    Natural varianti4613 – 46131I → V.
    Corresponds to variant rs12801153 [ dbSNP | Ensembl ].
    VAR_039066
    Natural varianti4631 – 46311D → G.
    Corresponds to variant rs12801123 [ dbSNP | Ensembl ].
    VAR_039067
    Natural varianti5415 – 54151T → A.
    Corresponds to variant rs11231126 [ dbSNP | Ensembl ].
    VAR_039068

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei115 – 14935SGDDE…ETQSR → NTPQPSALECKDQNKQKEAS SQAGAVSVSTPNAGL in isoform 2. 1 PublicationVSP_044233Add
    BLAST
    Alternative sequencei150 – 58905741Missing in isoform 2. 1 PublicationVSP_044234Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP001363 Genomic DNA. No translation available.
    AP003064 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74019.1.
    BC128460 mRNA. Translation: AAI28461.1.
    M80899 mRNA. Translation: AAA69898.1.
    M80902 mRNA. Translation: AAA69899.1. Different initiation.
    CCDSiCCDS31584.1. [Q09666-1]
    CCDS44625.1. [Q09666-2]
    PIRiA45259.
    RefSeqiNP_001611.1. NM_001620.2. [Q09666-1]
    NP_076965.2. NM_024060.3. [Q09666-2]
    XP_005274297.1. XM_005274240.1. [Q09666-1]
    XP_005274298.1. XM_005274241.1. [Q09666-1]
    UniGeneiHs.502756.

    Genome annotation databases

    EnsembliENST00000257247; ENSP00000257247; ENSG00000124942. [Q09666-2]
    ENST00000378024; ENSP00000367263; ENSG00000124942. [Q09666-1]
    GeneIDi79026.
    KEGGihsa:79026.
    UCSCiuc001ntk.2. human. [Q09666-2]
    uc001ntl.3. human. [Q09666-1]

    Polymorphism databases

    DMDMi160332335.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP001363 Genomic DNA. No translation available.
    AP003064 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74019.1 .
    BC128460 mRNA. Translation: AAI28461.1 .
    M80899 mRNA. Translation: AAA69898.1 .
    M80902 mRNA. Translation: AAA69899.1 . Different initiation.
    CCDSi CCDS31584.1. [Q09666-1 ]
    CCDS44625.1. [Q09666-2 ]
    PIRi A45259.
    RefSeqi NP_001611.1. NM_001620.2. [Q09666-1 ]
    NP_076965.2. NM_024060.3. [Q09666-2 ]
    XP_005274297.1. XM_005274240.1. [Q09666-1 ]
    XP_005274298.1. XM_005274241.1. [Q09666-1 ]
    UniGenei Hs.502756.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DRW X-ray 3.50 E/F 5654-5673 [» ]
    4FTG X-ray 2.51 E 5654-5673 [» ]
    4HRG X-ray 2.00 C/D 5655-5668 [» ]
    ProteinModelPortali Q09666.
    SMRi Q09666. Positions 8-91.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122494. 29 interactions.
    IntActi Q09666. 23 interactions.
    MINTi MINT-4998803.
    STRINGi 9606.ENSP00000367263.

    PTM databases

    PhosphoSitei Q09666.

    Polymorphism databases

    DMDMi 160332335.

    Proteomic databases

    MaxQBi Q09666.
    PaxDbi Q09666.
    PeptideAtlasi Q09666.
    PRIDEi Q09666.

    Protocols and materials databases

    DNASUi 79026.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257247 ; ENSP00000257247 ; ENSG00000124942 . [Q09666-2 ]
    ENST00000378024 ; ENSP00000367263 ; ENSG00000124942 . [Q09666-1 ]
    GeneIDi 79026.
    KEGGi hsa:79026.
    UCSCi uc001ntk.2. human. [Q09666-2 ]
    uc001ntl.3. human. [Q09666-1 ]

    Organism-specific databases

    CTDi 79026.
    GeneCardsi GC11M062202.
    H-InvDB HIX0171266.
    HIX0171345.
    HGNCi HGNC:347. AHNAK.
    HPAi HPA019010.
    HPA019070.
    HPA026643.
    MIMi 103390. gene.
    neXtProti NX_Q09666.
    PharmGKBi PA24640.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000033865.
    HOVERGENi HBG104864.
    InParanoidi Q09666.
    OMAi VASFHRD.
    OrthoDBi EOG7BCNB3.
    PhylomeDBi Q09666.
    TreeFami TF350595.

    Miscellaneous databases

    ChiTaRSi AHNAK. human.
    GeneWikii AHNAK.
    GenomeRNAii 79026.
    NextBioi 67715.
    PROi Q09666.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q09666.
    Bgeei Q09666.
    CleanExi HS_AHNAK.
    Genevestigatori Q09666.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    InterProi IPR001478. PDZ.
    [Graphical view ]
    SMARTi SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 2).
    4. "A human gene (AHNAK) encoding an unusually large protein with a 1.2-microns polyionic rod structure."
      Shtivelman E., Cohen F.E., Bishop J.M.
      Proc. Natl. Acad. Sci. U.S.A. 89:5472-5476(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 114-1930 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 4614-5890 (ISOFORM 1).
      Tissue: Placenta.
    5. Erratum
      Shtivelman E., Cohen F.E., Bishop J.M.
      Proc. Natl. Acad. Sci. U.S.A. 90:4328-4328(1993)
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-93; THR-490; SER-511; THR-4100; THR-4766; SER-5077; SER-5110; SER-5448; SER-5552 AND SER-5752, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-511; SER-5731 AND SER-5763, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration."
      Huang Y., Laval S.H., van Remoortere A., Baudier J., Benaud C., Anderson L.V., Straub V., Deelder A., Frants R.R., den Dunnen J.T., Bushby K., van der Maarel S.M.
      FASEB J. 21:732-742(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DYSF.
    9. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-490; SER-511; SER-4986; SER-5099; SER-5110 AND SER-5552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5749 AND SER-5752, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-93; SER-511; SER-570; SER-793; SER-4903; SER-4960; SER-4993; THR-5009; SER-5099; THR-5415; SER-5731; SER-5749; SER-5752; SER-5763; SER-5780; SER-5782; SER-5793; THR-5794; SER-5830 AND SER-5841, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    14. Carrascal M., Abian J.
      Submitted (JAN-2008) to UniProtKB
      Cited for: PHOSPHORYLATION AT SER-5749, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511 AND SER-5752, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511; SER-570; SER-2397; SER-5448; SER-5731; SER-5749; SER-5752 AND SER-5763, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-93; THR-101; SER-135; SER-177; SER-210; SER-212; SER-216; THR-490; SER-511; SER-559; SER-570; SER-793; SER-1068; THR-1192; SER-1286; THR-1986; THR-2181; THR-2309; SER-2397; SER-2670; SER-2798; THR-2832; THR-2845; SER-3054; SER-3409; SER-3412; SER-3426; THR-3716; SER-3836; SER-4092; THR-4100; SER-4220; THR-4430; SER-4516; SER-4684; SER-4812; SER-4960; SER-4986; SER-5077; SER-5099; SER-5110; SER-5125; SER-5332; SER-5386; SER-5400; SER-5448; SER-5552; SER-5620; SER-5731; SER-5739; SER-5752; SER-5763; SER-5780; SER-5782; SER-5790; THR-5824; SER-5830; SER-5841 AND SER-5857, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-135; SER-177; THR-490; SER-511; SER-559; SER-5731 AND SER-5841, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAHNK_HUMAN
    AccessioniPrimary (citable) accession number: Q09666
    Secondary accession number(s): A1A586
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3