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Protein

Protein AHNAK2

Gene

AHNAK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Recommended name:
Protein AHNAK2
Gene namesi
Name:AHNAK2
Synonyms:C14orf78, KIAA2019
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20125. AHNAK2.

Subcellular locationi

GO - Cellular componenti

  • costamere Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle membrane Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: HPA
  • sarcolemma Source: UniProtKB
  • T-tubule Source: UniProtKB
  • Z disc Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162376085.

Polymorphism and mutation databases

BioMutaiAHNAK2.
DMDMi172045740.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 57955795Protein AHNAK2PRO_0000319962Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki116 – 116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei280 – 2801PhosphoserineCombined sources
Modified residuei294 – 2941PhosphoserineCombined sources
Modified residuei593 – 5931PhosphoserineCombined sources
Modified residuei842 – 8421PhosphoserineCombined sources
Modified residuei1007 – 10071PhosphoserineCombined sources
Modified residuei1112 – 11121PhosphoserineCombined sources
Modified residuei1337 – 13371PhosphoserineCombined sources
Modified residuei1418 – 14181PhosphoserineCombined sources
Modified residuei1502 – 15021PhosphoserineCombined sources
Modified residuei1510 – 15101N6-acetyllysineCombined sources
Modified residuei1667 – 16671PhosphoserineCombined sources
Modified residuei1832 – 18321PhosphoserineCombined sources
Modified residuei1840 – 18401N6-acetyllysineCombined sources
Modified residuei2162 – 21621PhosphoserineCombined sources
Modified residuei2243 – 22431PhosphoserineCombined sources
Modified residuei2408 – 24081PhosphoserineCombined sources
Modified residuei2492 – 24921PhosphoserineCombined sources
Modified residuei2500 – 25001N6-acetyllysineCombined sources
Modified residuei2738 – 27381PhosphoserineCombined sources
Modified residuei2822 – 28221PhosphoserineCombined sources
Modified residuei2987 – 29871PhosphoserineCombined sources
Modified residuei3068 – 30681PhosphoserineCombined sources
Modified residuei3152 – 31521PhosphoserineCombined sources
Modified residuei3233 – 32331PhosphoserineCombined sources
Modified residuei3408 – 34081PhosphoserineCombined sources
Modified residuei3812 – 38121PhosphoserineCombined sources
Modified residuei3977 – 39771PhosphoserineCombined sources
Modified residuei4142 – 41421PhosphoserineCombined sources
Modified residuei4307 – 43071PhosphoserineCombined sources
Modified residuei4388 – 43881PhosphoserineCombined sources
Modified residuei4472 – 44721PhosphoserineCombined sources
Modified residuei4477 – 44771PhosphoserineCombined sources
Modified residuei4894 – 48941PhosphoserineCombined sources
Modified residuei4897 – 48971PhosphoserineCombined sources
Modified residuei5707 – 57071PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8IVF2.
MaxQBiQ8IVF2.
PaxDbiQ8IVF2.
PeptideAtlasiQ8IVF2.
PRIDEiQ8IVF2.

PTM databases

iPTMnetiQ8IVF2.
PhosphoSiteiQ8IVF2.
SwissPalmiQ8IVF2.

Expressioni

Gene expression databases

BgeeiQ8IVF2.
GenevisibleiQ8IVF2. HS.

Organism-specific databases

HPAiHPA000878.
HPA002940.
HPA004145.
HPA020111.

Interactioni

Subunit structurei

Homodimer (via PDZ domain) (PubMed:24675079). Interacts with DYSF; the interaction is direct and Ca2+-independent (PubMed:17185750).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GABARAPL1Q9H0R83EBI-10217765,EBI-3464833
GABARAPL2P605203EBI-10217765,EBI-720116

Protein-protein interaction databases

BioGridi125226. 23 interactions.
IntActiQ8IVF2. 7 interactions.
STRINGi9606.ENSP00000353114.

Structurei

Secondary structure

1
5795
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi111 – 1166Combined sources
Beta strandi125 – 1306Combined sources
Beta strandi136 – 1416Combined sources
Helixi146 – 1494Combined sources
Beta strandi158 – 1658Combined sources
Helixi171 – 18111Combined sources
Beta strandi184 – 19310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CN0X-ray1.75A/B108-203[»]
ProteinModelPortaliQ8IVF2.
SMRiQ8IVF2. Positions 111-203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 19382PDZPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IGCZ. Eukaryota.
ENOG41116CJ. LUCA.
GeneTreeiENSGT00530000063716.
InParanoidiQ8IVF2.
OMAiGVGIKAH.
OrthoDBiEOG7BCNB3.
PhylomeDBiQ8IVF2.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IVF2-1) [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

        10         20         30         40         50
MCDCFHMVLP TWPGTPGSVS GRQLQPGEPG AETEDDHSVT EGPADEGIRP
60 70 80 90 100
RPQGSSPVYE YTTEAADFGL QEDAPGRQGS AGRRRSWWKR DSGDSRTFFR
110 120 130 140 150
MSRPEAVQEA TEVTLKTEVE AGASGYSVTG GGDQGIFVKQ VLKDSSAAKL
160 170 180 190 200
FNLREGDQLL STTVFFENIK YEDALKILQY SEPYKVQFKI RRQLPAPQDE
210 220 230 240 250
EWASSDAQHG PQGKEKEDTD VADGCRETPT KTLEGDGDQE RLISKPRVGR
260 270 280 290 300
GRQSQRERLS WPKFQSIKSK RGPGPQRSHS SSEAYEPRDA HDVSPTSTDT
310 320 330 340 350
EAQLTVERQE QKAGPGSQRR RKFLNLRFRT GSGQGPSSTG QPGRGFQSGV
360 370 380 390 400
GRAGVLEELG PWGDSLEETG AATGSRREER AEQDREVMPA QSMPLPTELG
410 420 430 440 450
DPRLCEGTPQ EGGLRAARLH GKTLEGQAQE TAVAQRKPRA QPTPGMSREG
460 470 480 490 500
EGEGLQSLEI GIARLSLRDT TEGGTQIGPP EIRVRVHDLK TPKFAFSTEK
510 520 530 540 550
EPERERRLST PQRGKRQDAS SKAGTGLKGE EVEGAGWMPG REPTTHAEAQ
560 570 580 590 600
GDEGDGEEGL QRTRITEEQD KGREDTEGQI RMPKFKIPSL GWSPSKHTKT
610 620 630 640 650
GREKATEDTE QGREGEATAT ADRREQRRTE EGLKDKEDSD SMTNTTKIQL
660 670 680 690 700
IHDEKRLKKE QILTEKEVAT KDSKFKMPKF KMPLFGASAP GKSMEASVDV
710 720 730 740 750
SAPKVEADVS LLSMQGDLKT TDLSVQTPSA DLEVQDGQVD VKLPEGPLPE
760 770 780 790 800
GASLKGHLPK VQRPSLKMPK VDLKGPKLDL KGPKAEVTAP DVKMSLSSME
810 820 830 840 850
VDVQAPRAKL DGARLEGDLS LADKEVTAKD SKFKMPKFKM PSFGVSAPGK
860 870 880 890 900
SMEDSVDVSA PKVEADVSLS SMQGDLKATD LSIQPPSADL EVQAGQVDVK
910 920 930 940 950
LPEGPVPEGA GPKVHLPKVE MPSFKMPKVD LKGPQIDVKG PKLDLKGPKA
960 970 980 990 1000
EVTAPDGEVS LPSMEVDVQA QKAKLDGAWL EGDLSLADKD VTAKDSKFKM
1010 1020 1030 1040 1050
PKFKMPSFGV SAPGKSIKAL VDVSAPKVEA DLSLPSMQGD LKTTDLSIQP
1060 1070 1080 1090 1100
ASTDLKVQAD QVDVKLPEGH LPEGAGLKGH LPKVEMPSFK MPKVALKGPQ
1110 1120 1130 1140 1150
VDVKGPKLDL KSPKAEVTAP DVEVSLPSVE VDVEAPGAKL DSARLEGELS
1160 1170 1180 1190 1200
LADKDVTAKD SRFKMPKFKM PSFGASAPGK SIEASVDVSA PKVEADVSLP
1210 1220 1230 1240 1250
SMQGDLKTTD LSIQPPSADL EVHAGQVDVK LLEGHVPEGA GFKGHLPKVQ
1260 1270 1280 1290 1300
MPSLKMPKVD LKGPQVEVRG PKLDLKGHKA EVTAHEVAVS LPSVEVDMQA
1310 1320 1330 1340 1350
PGAKLDGAQL DGDLSLADKD VTAKDSKFKM PKFKMPSFGV SAPGKSIEAS
1360 1370 1380 1390 1400
VDLSAPKVEA DMSLPSMQGD LKTTDLSIQP PSTDLELQAG QLDVKLPEGP
1410 1420 1430 1440 1450
VPEGAGLKGH LPKLQMPSFK VPKVDLKGPE IDIKGPKLDL KDPKVEVTAP
1460 1470 1480 1490 1500
DVEVSLPSVE VDVEAPGAKL DGGRLEEDMS LADKDLTTKD SKFKMPKFKM
1510 1520 1530 1540 1550
PSFGVSAPGK SIEASVDVSA PKVEADVSLP SMQGDLKATD LSIQPPSADL
1560 1570 1580 1590 1600
EVQAGQVDVK LPEGPVSEGA GLKGHLPKVQ MPSFKMPKVD LKGPQIDVKG
1610 1620 1630 1640 1650
PKLDLKGPKV EVTAPDVKMS LSSMEVDVQA PRAKLDGAQL EGDLSLADKA
1660 1670 1680 1690 1700
VTAKDSKFKM PKFKMPSFGV SAPGKSIEAS VDVSEPKVEA DVSLPSMQGD
1710 1720 1730 1740 1750
LKTTDLSIQS PSADLEVQAG QVNVKLPEGP LPEGAGFKGH LPKVQMPSLK
1760 1770 1780 1790 1800
MPKVALKGPQ MDVKGPKLDL KGPKAEVMAP DVEVSLPSVE VDVEAPGAKL
1810 1820 1830 1840 1850
DSVRLEGDLS LADKDVTAKD SKFKMPKFKM PSFGVSAPGK SIEASVDVSA
1860 1870 1880 1890 1900
PKVEAEVSLP SMQGDLKTTD LCIPLPSADL VVQAGQVDMK LPEGQVPEGA
1910 1920 1930 1940 1950
GLKGHLPKVD MPSFKMPKVD LKGPQTDVKG AKLDLKGPKA EVTAPDVEVS
1960 1970 1980 1990 2000
LPSMEVDVQA QKAKLDGARL EGDLSLADKD MTAKDSKFKM PKFKMPSFGV
2010 2020 2030 2040 2050
SAPGRSIEAS VDVPAPKVEA DVSLPSMQGD LKTTDLSIQP PSADLKVQTG
2060 2070 2080 2090 2100
QVDVKLPEGH VPEGAGLKGH LPKVEMPSLK MPKVDLKGPQ VDIKGPKLDL
2110 2120 2130 2140 2150
KDPKVEMRVP DVEVSLPSME VDVQAPRAKL DSAHLQGDLT LANKDLTTKD
2160 2170 2180 2190 2200
SKFKMPKFKM PSFGVSAPGK SIEASVDVSP PKVEADMSLP SMQGDLKTTD
2210 2220 2230 2240 2250
LSIQPLSADV KVQAGQVDVK LLEGPVPEEV GLKGHLPKLQ MPSFKVPKVD
2260 2270 2280 2290 2300
LKGPEIDIKG PKLDLKDPKV EVTAPDVEVS LPSVEVDVKA PGAKLDGARL
2310 2320 2330 2340 2350
EGDMSLADKD VTAKDSKFKM PKFKMLSFGV SALGKSIEAS ADVSALKVEA
2360 2370 2380 2390 2400
DVSLPSMQGD LKTTDLSVQP PSADLEVQAG QVDVKLPEGP VPEGAGLKGH
2410 2420 2430 2440 2450
LPKLQMPSFK MPKVDLKGPQ IDVKGPKLDL KGPKTDVMAP DVEVSQPSVE
2460 2470 2480 2490 2500
VDVEAPGAKL DGAWLEGDLS VADKDVTTKD SRFKIPKFKM PSFGVSAPGK
2510 2520 2530 2540 2550
SIEASVDVSA PKVEADGSLS SMQGDLKATD LSIQPPSADL EVQAGQVDVK
2560 2570 2580 2590 2600
LPEGPVPEGA GLKGHLPKVQ MPSFKMPEMD LKGPQLDVKG PKLDLKGPKA
2610 2620 2630 2640 2650
EVTAPDVEMS LSSMEVDVQA PRAKLDGARL EGDLSLADKG VTAKDSKFKM
2660 2670 2680 2690 2700
PKFKMPSFRV SAPGESIEAL VDVSELKVEA DMSLPSMQGD LKTTDISIQP
2710 2720 2730 2740 2750
PSAQLEVQAG QVDVKLPEGH VPEGAGLKGH LPKLQMPSFK MPEVDLKGPQ
2760 2770 2780 2790 2800
IDVKGPNVDL KGPKAEVTAP DVKMSLSSME VDVQAPRAKL DGARLEGDLS
2810 2820 2830 2840 2850
LADKGMTAKD SKFKMPKFKM PSFGVSAPGK SIEASVDVSE LKVEADGSFP
2860 2870 2880 2890 2900
SMQGDLKTTD IRIQPPSAQL EVQAGQVDVK LPEGHVPEGA GLKGHLPKVQ
2910 2920 2930 2940 2950
MPSFKMPKVD LKGPQIDVKG PKLDLKGPKA EVTAPDVEVS LPSVEVDVEA
2960 2970 2980 2990 3000
PRAKLDGARL EGDLSLADKD VTAKDSKFKM PKFKMPSFGV SAPGKSIEVS
3010 3020 3030 3040 3050
VDVSAPKVEA EVSLPSMQGD LKTTDISIEP PSAQLEVQAG QVDLKLPEGH
3060 3070 3080 3090 3100
VPEGAGLKGH LPKLQMPSFK MPKVDRKGPQ IDVKGPKLDL KGPKTDVTAP
3110 3120 3130 3140 3150
DVEVSQPGME VDVEAPGAKL DGARLEGDLS LADKDVTAKD SKFKMPKFKM
3160 3170 3180 3190 3200
PSFGVSAPGK SIEVLVDVSA PKVEADLSLP SMQGDLKNTD ISIEPPSAQL
3210 3220 3230 3240 3250
EVQAGQVDVK LPEGHVLEGA GLKGHLPKLQ MPSFKMPKVD RKGPQIDIKG
3260 3270 3280 3290 3300
PKLDLKGPKM DVTAPDVEVS QPSMEVDVEA PGAKLDGARL EGDLSLADKD
3310 3320 3330 3340 3350
VTAKDSKFKM PKFKMPSYRA SAPGKSIQAS VDVSAPKAEA DVSLPSMQGD
3360 3370 3380 3390 3400
LKTTDLSIQL PSVDLEVQAG QVDVKLPEGH VPEGAGLKGH LPKVEMPSFK
3410 3420 3430 3440 3450
MPKVDLKSPQ VDIKGPKLDL KVPKAEVTVP DVEVSLPSVE VDVQAPRAKL
3460 3470 3480 3490 3500
DGARLEGDLS LAEKDVTAKD SKFKMPKFKM PSFGVSAPGR SIEASLDVSA
3510 3520 3530 3540 3550
PKVEADVSLS SMQGDLKATD LSIQPPSADL EVQAVQVDVE LLEGPVPEGA
3560 3570 3580 3590 3600
GLKGHLPKVE MPSLKTPKVD LKGPQIDVKG PKLDLKGPKA EVRVPDVEVS
3610 3620 3630 3640 3650
LPSVEVDVQA PKAKLDAGRL EGDLSLADKD VTAKDSKFKM PKFKMPSFRV
3660 3670 3680 3690 3700
SAPGKSMEAS VDVSAPKVEA DVSLPSMQGD LKTTDLSIQP PSADLKVQAG
3710 3720 3730 3740 3750
QMDVKLPEGQ VPEGAGLKEH LPKVEMPSLK MPKVDLKGPQ VDIKGPKLDL
3760 3770 3780 3790 3800
KVSKAEVTAP DVEVSLPSVE VDVQAPRAKL DSAQLEGDLS LADKDVTAKD
3810 3820 3830 3840 3850
SKFKMPKFKM PSFGVSAPGK SIEASVHVSA PKVEADVSLP SMQGDLKTTD
3860 3870 3880 3890 3900
LSIQPHSADL TVQARQVDMK LLEGHVPEEA GLKGHLPKVQ MPSFKMPKVD
3910 3920 3930 3940 3950
LKGPEIDIKG PKLDLKDPKV EVTAPDVEVS LPSVEVDVEA PGAKLDGARL
3960 3970 3980 3990 4000
EGDLSLADKD MTAKDSKFKM PKFKMPSFGV SAPGKSMEAS VDVTAPKVEA
4010 4020 4030 4040 4050
DVSLPSMQGD LKATDLSVQP PSADLEVQAG QVDVKLPEGP VPEGASLKGH
4060 4070 4080 4090 4100
LPKVQMPSFK MPKVDLKGPQ IDVKGPKLDL KGPKAEVTAP DVKMSLSSME
4110 4120 4130 4140 4150
VDVQAPRAKL DGVQLEGDLS LADKDVTAKD SKFKMPKFKM PSFGVSAPGK
4160 4170 4180 4190 4200
SMEASVDVSE LKAKADVSLP SMQGDLKTTD LSIQSPSADL EVQAGQVDVK
4210 4220 4230 4240 4250
LPEGPLPKGA GLKGHLPKVQ MPCLKMPKVA LKGPQVDVKG PKLDLKGPKA
4260 4270 4280 4290 4300
DVMTPVVEVS LPSMEVDVEA PGAKLDSVRL EGDLSLADKD MTAKDSKFKM
4310 4320 4330 4340 4350
PKFKMPSFGV SAPGKSIEAS LDVSALKVEA DVSLPSMQGD LKTTHLSIQP
4360 4370 4380 4390 4400
PSADLEVQAG QEDVKLPEGP VHEGAGLKGH LPKLQMPSFK VPKVDLKGPQ
4410 4420 4430 4440 4450
IDVNVPKLDL KGPKVEVTSP NLDVSLPSME VDIQAPGAKL DSTRLEGDLS
4460 4470 4480 4490 4500
LADKDVTAKD SKFKMPKFKM PSFGMLSPGK SIEVSVDVSA PKMEADMSIP
4510 4520 4530 4540 4550
SMQGDLKTTD LRIQAPSADL EVQAGQVDLK LPEGHMPEVA GLKGHLPKVE
4560 4570 4580 4590 4600
MPSFKMPKVD LKGPQVDVKG PKLDLKGPKA EVMAPDVEVS LPSVETDVQA
4610 4620 4630 4640 4650
PGSMLDGARL EGDLSLAHED VAGKDSKFQG PKLSTSGFEW SSKKVSMSSS
4660 4670 4680 4690 4700
EIEGNVTFHE KTSTFPIVES VVHEGDLHDP SRDGNLGLAV GEVGMDSKFK
4710 4720 4730 4740 4750
KLHFKVPKVS FSSTKTPKDS LVPGAKSSIG LSTIPLSSSE CSSFELQQVS
4760 4770 4780 4790 4800
ACSEPSMQMP KVGFAGFPSS RLDLTGPHFE SSILSPCEDV TLTKYQVTVP
4810 4820 4830 4840 4850
RAALAPELAL EIPSGSQADI PLPKTECSTD LQPPEGVPTS QAESHSGPLN
4860 4870 4880 4890 4900
SMIPVSLGQV SFPKFYKPKF VFSVPQMAVP EGDLHAAVGA PVMSPLSPGE
4910 4920 4930 4940 4950
RVQCPLPSTQ LPSPGTCVSQ GPEELVASLQ TSVVAPGEAP SEDADHEGKG
4960 4970 4980 4990 5000
SPLKMPKIKL PSFRWSPKKE TGPKVDPECS VEDSKLSLVL DKDEVAPQSA
5010 5020 5030 5040 5050
IHMDLPPERD GEKGRSTKPG FAMPKLALPK MKASKSGVSL PQRDVDPSLS
5060 5070 5080 5090 5100
SATAGGSFQD TEKASSDGGR GGLGATASAT GSEGVNLHRP QVHIPSLGFA
5110 5120 5130 5140 5150
KPDLRSSKAK VEVSQPEADL PLPKHDLSTE GDSRGCGLGD VPVSQPCGEG
5160 5170 5180 5190 5200
IAPTPEDPLQ PSCRKPDAEV LTVESPEEEA MTKYSQESWF KMPKFRMPSL
5210 5220 5230 5240 5250
RRSFRDRGGA GKLEVAQTQA PAATGGEAAA KVKEFLVSGS NVEAAMSLQL
5260 5270 5280 5290 5300
PEADAEVTAS ESKSSTDILR CDLDSTGLKL HLSTAGMTGD ELSTSEVRIH
5310 5320 5330 5340 5350
PSKGPLPFQM PGMRLPETQV LPGEIDETPL SKPGHDLASM EDKTEKWSSQ
5360 5370 5380 5390 5400
PEGPLKLKAS STDMPSQISV VNVDQLWEDS VLTVKFPKLM VPRFSFPAPS
5410 5420 5430 5440 5450
SEDDVFIPTV REVQCPEANI DTALCKESPG LWGASILKAG AGVPGEQPVD
5460 5470 5480 5490 5500
LNLPLEAPPI SKVRVHIQGA QVESQEVTIH SIVTPEFVDL SVPRTFSTQI
5510 5520 5530 5540 5550
VRESEIPTSE IQTPSYGFSL LKVKIPEPHT QARVYTTMTQ HSRTQEGTEE
5560 5570 5580 5590 5600
APIQATPGVD SISGDLQPDT GEPFEMISSS VNVLGQQTLT FEVPSGHQLA
5610 5620 5630 5640 5650
DSCSDEEPAE ILEFPPDDSQ EATTPLADEG RAPKDKPESK KSGLLWFWLP
5660 5670 5680 5690 5700
NIGFSSSVDE TGVDSKNDVQ RSAPIQTQPE ARPEAELPKK QEKAGWFRFP
5710 5720 5730 5740 5750
KLGFSSSPTK KSKSTEDGAE LEEQKLQEET ITFFDARESF SPEEKEEGEL
5760 5770 5780 5790
IGPVGTGLDS RVMVTSAART ELILPEQDRK ADDESKGSGL GPNEG
Length:5,795
Mass (Da):616,629
Last modified:February 26, 2008 - v2
Checksum:iBEC73677308C1FAB
GO
Isoform 2 (identifier: Q8IVF2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5002: Missing.

Note: No experimental confirmation available.
Show »
Length:793
Mass (Da):85,128
Checksum:iE2543EB1BE640F9A
GO
Isoform 3 (identifier: Q8IVF2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.

Show »
Length:5,695
Mass (Da):605,648
Checksum:i3EC13F00BECDE25A
GO

Sequence cautioni

The sequence AAH49216.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH90889.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC23115.1 differs from that shown. Reason: Frameshift at position 3008. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3195 – 31951P → L in BAC23115 (Ref. 4) Curated
Sequence conflicti3198 – 31981A → V in BAC23115 (Ref. 4) Curated
Sequence conflicti4740 – 47401E → G in CAD98019 (PubMed:17974005).Curated
Sequence conflicti5269 – 52691L → P in CAD98019 (PubMed:17974005).Curated
Sequence conflicti5560 – 55601D → G in CAD97904 (PubMed:17974005).Curated
Sequence conflicti5577 – 55771I → V in CAD97904 (PubMed:17974005).Curated
Sequence conflicti5590 – 55901T → A in CAD97981 (PubMed:17974005).Curated
Sequence conflicti5601 – 56011D → G in CAD98034 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti525 – 5251T → A.
Corresponds to variant rs2278607 [ dbSNP | Ensembl ].
VAR_050635
Natural varianti1266 – 12661V → M.
Corresponds to variant rs11850930 [ dbSNP | Ensembl ].
VAR_039069
Natural varianti1298 – 12981M → I.
Corresponds to variant rs2819440 [ dbSNP | Ensembl ].
VAR_061548
Natural varianti1470 – 14701L → V.
Corresponds to variant rs12890949 [ dbSNP | Ensembl ].
VAR_039070
Natural varianti1856 – 18561E → D.
Corresponds to variant rs2819435 [ dbSNP | Ensembl ].
VAR_059560
Natural varianti2107 – 21071M → V.
Corresponds to variant rs11846918 [ dbSNP | Ensembl ].
VAR_050636
Natural varianti2115 – 21151S → R.
Corresponds to variant rs2582514 [ dbSNP | Ensembl ].
VAR_039071
Natural varianti2146 – 21461L → V.
Corresponds to variant rs12890949 [ dbSNP | Ensembl ].
VAR_059561
Natural varianti2410 – 24101K → R.
Corresponds to variant rs11845746 [ dbSNP | Ensembl ].
VAR_050637
Natural varianti2429 – 24291D → E.
Corresponds to variant rs11160826 [ dbSNP | Ensembl ].
VAR_039072
Natural varianti2430 – 24301L → V.
Corresponds to variant rs2819426 [ dbSNP | Ensembl ].
VAR_039073
Natural varianti2503 – 25031E → A.
Corresponds to variant rs2819429 [ dbSNP | Ensembl ].
VAR_059562
Natural varianti2616 – 26161V → A.
Corresponds to variant rs4264326 [ dbSNP | Ensembl ].
VAR_039074
Natural varianti2862 – 28621R → S.
Corresponds to variant rs2582514 [ dbSNP | Ensembl ].
VAR_059563
Natural varianti3176 – 31761D → E.
Corresponds to variant rs11160826 [ dbSNP | Ensembl ].
VAR_059564
Natural varianti3177 – 31771L → V.
Corresponds to variant rs2819426 [ dbSNP | Ensembl ].
VAR_059565
Natural varianti3336 – 33361P → L.
Corresponds to variant rs10438247 [ dbSNP | Ensembl ].
VAR_059566
Natural varianti3363 – 33631V → A.
Corresponds to variant rs4264326 [ dbSNP | Ensembl ].
VAR_059567
Natural varianti3654 – 36541G → E.
Corresponds to variant rs28380382 [ dbSNP | Ensembl ].
VAR_061549
Natural varianti3793 – 37931D → N.
Corresponds to variant rs11160825 [ dbSNP | Ensembl ].
VAR_059568
Natural varianti3796 – 37961V → L.
Corresponds to variant rs12890949 [ dbSNP | Ensembl ].
VAR_050638
Natural varianti3869 – 38691M → V.
Corresponds to variant rs10438246 [ dbSNP | Ensembl ].
VAR_059569
Natural varianti3902 – 39021K → N.
Corresponds to variant rs2819423 [ dbSNP | Ensembl ].
VAR_059570
Natural varianti3961 – 39611M → V.
Corresponds to variant rs10141053 [ dbSNP | Ensembl ].
VAR_050639
Natural varianti4071 – 40711I → M.
Corresponds to variant rs2582511 [ dbSNP | Ensembl ].
VAR_050640
Natural varianti4085 – 40851A → V.
Corresponds to variant rs2013462 [ dbSNP | Ensembl ].
VAR_059571
Natural varianti4138 – 41381F → L.
Corresponds to variant rs2582505 [ dbSNP | Ensembl ].
VAR_050641
Natural varianti4198 – 41981D → N.
Corresponds to variant rs11848082 [ dbSNP | Ensembl ].
VAR_059572
Natural varianti4232 – 42321K → N.
Corresponds to variant rs2819423 [ dbSNP | Ensembl ].
VAR_050642
Natural varianti4278 – 42781V → A.
Corresponds to variant rs2819422 [ dbSNP | Ensembl ].
VAR_050643
Natural varianti4326 – 43261L → P.
Corresponds to variant rs2819421 [ dbSNP | Ensembl ].
VAR_059573
Natural varianti4478 – 44781P → L.
Corresponds to variant rs2582513 [ dbSNP | Ensembl ].
VAR_059574
Natural varianti4536 – 45361M → L.
Corresponds to variant rs9672139 [ dbSNP | Ensembl ].
VAR_050644
Natural varianti4664 – 46641T → A.1 Publication
Corresponds to variant rs4465542 [ dbSNP | Ensembl ].
VAR_050645
Natural varianti5028 – 50281L → M.
Corresponds to variant rs9672139 [ dbSNP | Ensembl ].
VAR_039075
Natural varianti5072 – 50721G → R.
Corresponds to variant rs2819420 [ dbSNP | Ensembl ].
VAR_050646
Natural varianti5139 – 51391G → E.
Corresponds to variant rs61421370 [ dbSNP | Ensembl ].
VAR_061550
Natural varianti5184 – 51841Y → D.1 Publication
Corresponds to variant rs2819419 [ dbSNP | Ensembl ].
VAR_050647
Natural varianti5397 – 53971P → A.2 Publications
Corresponds to variant rs3742935 [ dbSNP | Ensembl ].
VAR_050648
Natural varianti5564 – 55641G → R.
Corresponds to variant rs2819420 [ dbSNP | Ensembl ].
VAR_039076
Natural varianti5732 – 57321T → M.
Corresponds to variant rs748358 [ dbSNP | Ensembl ].
VAR_050649

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 50025002Missing in isoform 2. 1 PublicationVSP_031550Add
BLAST
Alternative sequencei1 – 100100Missing in isoform 3. 2 PublicationsVSP_031551Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL512802 Genomic DNA. No translation available.
AI915159 mRNA. No translation available.
BC011859 mRNA. Translation: AAH11859.2.
BC033372 mRNA. Translation: AAH33372.1.
BC049216 mRNA. Translation: AAH49216.1. Different initiation.
BC090889 mRNA. Translation: AAH90889.1. Different initiation.
AK094143 mRNA. No translation available.
AB095939 mRNA. Translation: BAC23115.1. Frameshift.
AL834367 mRNA. Translation: CAD39030.1.
BX537923 mRNA. Translation: CAD97904.1.
BX538040 mRNA. Translation: CAD97981.1.
BX538106 mRNA. Translation: CAD98019.1.
BX538133 mRNA. Translation: CAD98034.1.
CCDSiCCDS45177.1. [Q8IVF2-1]
RefSeqiNP_612429.2. NM_138420.2. [Q8IVF2-1]
XP_005267356.1. XM_005267299.1. [Q8IVF2-3]
UniGeneiHs.441783.

Genome annotation databases

EnsembliENST00000333244; ENSP00000353114; ENSG00000185567. [Q8IVF2-1]
ENST00000557457; ENSP00000450998; ENSG00000185567. [Q8IVF2-2]
GeneIDi113146.
KEGGihsa:113146.
UCSCiuc010axc.2. human. [Q8IVF2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL512802 Genomic DNA. No translation available.
AI915159 mRNA. No translation available.
BC011859 mRNA. Translation: AAH11859.2.
BC033372 mRNA. Translation: AAH33372.1.
BC049216 mRNA. Translation: AAH49216.1. Different initiation.
BC090889 mRNA. Translation: AAH90889.1. Different initiation.
AK094143 mRNA. No translation available.
AB095939 mRNA. Translation: BAC23115.1. Frameshift.
AL834367 mRNA. Translation: CAD39030.1.
BX537923 mRNA. Translation: CAD97904.1.
BX538040 mRNA. Translation: CAD97981.1.
BX538106 mRNA. Translation: CAD98019.1.
BX538133 mRNA. Translation: CAD98034.1.
CCDSiCCDS45177.1. [Q8IVF2-1]
RefSeqiNP_612429.2. NM_138420.2. [Q8IVF2-1]
XP_005267356.1. XM_005267299.1. [Q8IVF2-3]
UniGeneiHs.441783.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CN0X-ray1.75A/B108-203[»]
ProteinModelPortaliQ8IVF2.
SMRiQ8IVF2. Positions 111-203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125226. 23 interactions.
IntActiQ8IVF2. 7 interactions.
STRINGi9606.ENSP00000353114.

PTM databases

iPTMnetiQ8IVF2.
PhosphoSiteiQ8IVF2.
SwissPalmiQ8IVF2.

Polymorphism and mutation databases

BioMutaiAHNAK2.
DMDMi172045740.

Proteomic databases

EPDiQ8IVF2.
MaxQBiQ8IVF2.
PaxDbiQ8IVF2.
PeptideAtlasiQ8IVF2.
PRIDEiQ8IVF2.

Protocols and materials databases

DNASUi113146.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333244; ENSP00000353114; ENSG00000185567. [Q8IVF2-1]
ENST00000557457; ENSP00000450998; ENSG00000185567. [Q8IVF2-2]
GeneIDi113146.
KEGGihsa:113146.
UCSCiuc010axc.2. human. [Q8IVF2-1]

Organism-specific databases

CTDi113146.
GeneCardsiAHNAK2.
H-InvDBHIX0012023.
HGNCiHGNC:20125. AHNAK2.
HPAiHPA000878.
HPA002940.
HPA004145.
HPA020111.
MIMi608570. gene.
neXtProtiNX_Q8IVF2.
PharmGKBiPA162376085.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGCZ. Eukaryota.
ENOG41116CJ. LUCA.
GeneTreeiENSGT00530000063716.
InParanoidiQ8IVF2.
OMAiGVGIKAH.
OrthoDBiEOG7BCNB3.
PhylomeDBiQ8IVF2.
TreeFamiTF350595.

Miscellaneous databases

ChiTaRSiAHNAK2. human.
GenomeRNAii113146.
PROiQ8IVF2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IVF2.
GenevisibleiQ8IVF2. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-77 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-647 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5281-5795 (ISOFORMS 1/2/3), VARIANT ALA-5397.
    Tissue: Eye, Kidney, Skin, Testis and Uterine adenocarcinoma.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-631 (ISOFORM 3).
    Tissue: Astrocyte.
  4. "The nucleotide sequence of a long cDNA clone isolated from human."
    Nagase T., Kikuno R., Ohara O.
    Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2994-5795 (ISOFORMS 1/3).
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4587-5795 (ISOFORMS 1/3), VARIANTS ALA-4664; ASP-5184 AND ALA-5397.
    Tissue: Colon endothelium, Melanoma and Uterus.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-294, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1510; LYS-1840 AND LYS-2500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-280; SER-593; SER-842; SER-1007; SER-1112; SER-1337; SER-1502; SER-1667; SER-1832; SER-2162; SER-2492; SER-2822; SER-2987; SER-3152; SER-3408; SER-3812; SER-3977; SER-4142; SER-4307; SER-4472; SER-4477; SER-4894 AND SER-4897, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-294; SER-593; SER-1418; SER-2243; SER-2408; SER-2738; SER-3068; SER-3233; SER-3408; SER-4388; SER-4477 AND SER-5707, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through domain swapping."
    Han H., Kursula P.
    J. Biol. Chem. 289:14121-14131(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 108-203, SUBUNIT.

Entry informationi

Entry nameiAHNK2_HUMAN
AccessioniPrimary (citable) accession number: Q8IVF2
Secondary accession number(s): Q5BKX7
, Q7Z343, Q7Z358, Q7Z394, Q7Z3G0, Q86WQ6, Q8IYY1, Q8N3G4, Q96EX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: July 6, 2016
This is version 102 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 14
    Human chromosome 14: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.