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Q09666

- AHNK_HUMAN

UniProt

Q09666 - AHNK_HUMAN

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Protein
Neuroblast differentiation-associated protein AHNAK
Gene
AHNAK, PM227
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May be required for neuronal cell differentiation.

GO - Molecular functioni

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

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
Complete GO annotation...

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

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 AHNAK
PRO_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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 9082PDZ
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi4971 – 49799Nuclear localization signal Reviewed prediction
Motifi5019 – 50279Nuclear localization signal Reviewed prediction
Motifi5034 – 50396Nuclear localization signal Reviewed prediction
Motifi5706 – 571611Nuclear localization signal Reviewed prediction
Add
BLAST
Motifi5772 – 57798Nuclear localization signal Reviewed prediction

Compositional bias

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

Sequence similaritiesi

Contains 1 PDZ (DHR) domain.

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.

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.
VSP_044233Add
BLAST
Alternative sequencei150 – 58905741Missing in isoform 2.
VSP_044234Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti288 – 2881A → P in AAA69899. 1 Publication
Sequence conflicti302 – 3021G → A in AAA69899. 1 Publication
Sequence conflicti1156 – 11561V → D in AAA69899. 1 Publication
Sequence conflicti1737 – 17371P → R in AAA69899. 1 Publication
Sequence conflicti1821 – 18211F → L in AAA69899. 1 Publication
Sequence conflicti4614 – 46141S → T in AAA69898. 1 Publication
Sequence conflicti4627 – 46271V → A in AAA69898. 1 Publication
Sequence conflicti4630 – 46312RD → KG in AAA69898. 1 Publication
Sequence conflicti4637 – 46382DV → NT in AAA69898. 1 Publication
Sequence conflicti4644 – 46441Q → H in AAA69898. 1 Publication
Sequence conflicti4830 – 48301A → P in AAA69898. 1 Publication
Sequence conflicti4834 – 48341G → V in AAA69898. 1 Publication
Sequence conflicti4837 – 48371F → V in AAA69898. 1 Publication
Sequence conflicti4984 – 49841A → P in AAA69898. 1 Publication
Sequence conflicti5445 – 54451P → S in AAA69898. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 122 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

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