ANK1

ANK1
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1N11, 2YQF, 2YVI, 3F59, 3KBT, 3KBU, 3UD1, 3UD2
Identifikatori
Aliasi	ANK1
Vanjski ID-jevi	OMIM: 612641 MGI: 88024 HomoloGene: 55427 GeneCards: ANK1
Lokacija gena (čovjek)
Hrom.	Hromosom 8 (čovjek)
Kraj	41,896,762 bp
Lokacija gena (miš)
Hrom.	Hromosom 8 (miš)
Kraj	23,640,513 bp
Obrazac RNK ekspresije
	; ; ; ;
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• spectrin binding; • ATPase binding; • structural molecule activity; • structural constituent of cytoskeleton; • GO:0001948, GO:0016582 vezivanje za proteine; • vezivanje enzima; • cytoskeletal anchor activity;
Ćelijska komponenta	• M band; • citosol; • postsynaptic membrane; • membrana; • ćelijska membrana; • Sarkoplazmatski retikulum; • basolateral plasma membrane; • Z discdkac; • axolemma; • spectrin-associated cytoskeleton; • neuron projection; • Sarkolema; • A band; • citoskelet; • jedro; • citoplazma;
Biološki proces	• positive regulation of organelle organization; • endoplasmic reticulum to Golgi vesicle-mediated transport; • maintenance of epithelial cell apical/basal polarity; • cytoskeleton organization; • GO:0072468 Transdukcija signala; • Egzocitoza; • protein localization to plasma membrane;
	Izvori:Amigo / QuickGO
Ortolozi
	286
	11733
	ENSG00000029534
	ENSMUSG00000031543
	P16157
	Q02357
NM_000037; NM_001142445; NM_001142446; NM_020475; NM_020476;
	NM_020477; NM_020478; NM_020479; NM_020480; NM_020481
NM_001110783; NM_001277280; NM_001277281; NM_001277284; NM_001277286;
	NM_001277289; NM_031158; NM_001310436; NM_001310437
NP_000028; NP_001135917; NP_001135918; NP_065208; NP_065209;
	NP_065210; NP_065211; NP_065213
NP_001104253; NP_001264209; NP_001264210; NP_001264213; NP_001264215;
	NP_001264218; NP_001297365; NP_001297366; NP_112435
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Eritrocitni ankirin 1, znan i kao ANK1, je protein koji je kod ljudi kodiran genom ANK1.^[5]^[6]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 1.881 aminokiselina, а molekulska težina 206.265 Da.^[7]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MPYSVGFREA	DAATSFLRAA	RSGNLDKALD	HLRNGVDINT	CNQNGLNGLH
LASKEGHVKM	VVELLHKEII	LETTTKKGNT	ALHIAALAGQ	DEVVRELVNY
GANVNAQSQK	GFTPLYMAAQ	ENHLEVVKFL	LENGANQNVA	TEDGFTPLAV
ALQQGHENVV	AHLINYGTKG	KVRLPALHIA	ARNDDTRTAA	VLLQNDPNPD
VLSKTGFTPL	HIAAHYENLN	VAQLLLNRGA	SVNFTPQNGI	TPLHIASRRG
NVIMVRLLLD	RGAQIETKTK	DELTPLHCAA	RNGHVRISEI	LLDHGAPIQA
KTKNGLSPIH	MAAQGDHLDC	VRLLLQYDAE	IDDITLDHLT	PLHVAAHCGH
HRVAKVLLDK	GAKPNSRALN	GFTPLHIACK	KNHVRVMELL	LKTGASIDAV
TESGLTPLHV	ASFMGHLPIV	KNLLQRGASP	NVSNVKVETP	LHMAARAGHT
EVAKYLLQNK	AKVNAKAKDD	QTPLHCAARI	GHTNMVKLLL	ENNANPNLAT
TAGHTPLHIA	AREGHVETVL	ALLEKEASQA	CMTKKGFTPL	HVAAKYGKVR
VAELLLERDA	HPNAAGKNGL	TPLHVAVHHN	NLDIVKLLLP	RGGSPHSPAW
NGYTPLHIAA	KQNQVEVARS	LLQYGGSANA	ESVQGVTPLH	LAAQEGHAEM
VALLLSKQAN	GNLGNKSGLT	PLHLVAQEGH	VPVADVLIKH	GVMVDATTRM
GYTPLHVASH	YGNIKLVKFL	LQHQADVNAK	TKLGYSPLHQ	AAQQGHTDIV
TLLLKNGASP	NEVSSDGTTP	LAIAKRLGYI	SVTDVLKVVT	DETSFVLVSD
KHRMSFPETV	DEILDVSEDE	GEELISFKAE	RRDSRDVDEE	KELLDFVPKL
DQVVESPAIP	RIPCAMPETV	VIRSEEQEQA	SKEYDEDSLI	PSSPATETSD
NISPVASPVH	TGFLVSFMVD	ARGGSMRGSR	HNGLRVVIPP	RTCAAPTRIT
CRLVKPQKLS	TPPPLAEEEG	LASRIIALGP	TGAQFLSPVI	VEIPHFASHG
RGDRELVVLR	SENGSVWKEH	RSRYGESYLD	QILNGMDEEL	GSLEELEKKR
VCRIITTDFP	LYFVIMSRLC	QDYDTIGPEG	GSLKSKLVPL	VQATFPENAV
TKRVKLALQA	QPVPDELVTK	LLGNQATFSP	IVTVEPRRRK	FHRPIGLRIP
LPPSWTDNPR	DSGEGDTTSL	RLLCSVIGGT	DQAQWEDITG	TTKLVYANEC
ANFTTNVSAR	FWLSDCPRTA	EAVNFATLLY	KELTAVPYMA	KFVIFAKMND
PREGRLRCYC	MTDDKVDKTL	EQHENFVEVA	RSRDIEVLEG	MSLFAELSGN
LVPVKKAAQQ	RSFHFQSFRE	NRLAMPVKVR	DSSREPGGSL	SFLRKAMKYE
DTQHILCHLN	ITMPPCAKGS	GAEDRRRTPT	PLALRYSILS	ESTPGSLSGT
EQAEMKMAVI	SEHLGLSWAE	LARELQFSVE	DINRIRVENP	NSLLEQSVAL
LNLWVIREGQ	NANMENLYTA	LQSIDRGEIV	NMLEGSGRQS	RNLKPDRRHT
DRDYSLSPSQ	MNGYSSLQDE	LLSPASLGCA	LSSPLRADQY	WNEVAVLDAI
PLAATEHDTM	LEMSDMQVWS	AGLTPSLVTA	EDSSLECSKA	EDSDATGHEW
KLEGALSEEP	RGPELGSLEL	VEDDTVDSDA	TNGLIDLLEQ	EEGQRSEEKL
PGSKRQDDAT	GAGQDSENEV	SLVSGHQRGQ	ARITHSPTVS	QVTERSQDRL
QDWDADGSIV	SYLQDAAQGS	WQEEVTQGPH	SFQGTSTMTE	GLEPGGSQEY
EKVLVSVSEH	TWTEQPEAES	SQADRDRRQQ	GQEEQVQEAK	NTFTQVVQGN
EFQNIPGEQV	TEEQFTDEQG	NIVTKKIIRK	VVRQIDLSSA	DAAQEHEEVT
VEGPLEDPSE	LEVDIDYFMK	HSKDHTSTPN	P

Funkcija

Protein ANK1 pripada porodici ankirina za koju se vjeruje da povezuje integralne membranske proteine s osnovnim spektrin-aktin citoskeletom i ima ključnu ulogu u aktivnosti poput pokretljivosti ćelija, aktivacije, proliferacije, kontakta i održavanja specijaliziranih membranskih domena. Više izoformi ankirina s različitim afinitetima za različite ciljne proteine izraženo je na tkivo specifičan, razvojno reguliran način. Većina ankirina se obično sastoji od tri strukturna domena: amino-terminalni domen koji sadrži više ponavljanja ankirina; centralna regija sa visoko konzerviranim domenom vezanja spektra, i karboksi-terminalno regulacijsko područje, koje je najmanje konzervirano i podložno promjenama.^[6]

Male varijante prerašenih proteina ANK1 (sAnk1) uspostavljaju kontakt sa opskurinom, divovskim proteinom koji okružuje kontraktilni aparat u prugastim mišićima.^[8]

Tkivna distribucija

Protein kodiran ovim genom, ankirin 1, prototip je porodice ankirina, prvi put je otkriven u eritrocitima, ali je od tada pronađen i u mozgu i mišićima.^[6]

Genetika

Opisani su složeni obrasci alternativnih prerada u regulatornom domenu, koji uzrokuju različite izoforme ankirina 1, ali precizne funkcije različitih izoformi nisu poznate . Prijavljena je i alternativna poliadenilacija koja predstavlja iRNK eritrocitnog ankirina 1 različite veličine. Skraćene mišićno specifične izoforme ankirina 1 nastale korištenjem zamjenskog promotora su također identificirane.^[6]

Vezane bolesti

Mutacije u eritrocitnom ankirinu 1 povezane su s otprilike polovinom svih pacijenata s nasljednom sferocitozom.^[6]

Kod Alzheimerove bolesti, ANK1 pokazuje promijenjenu metilaciju i ekspresiju.^[9]^[10] Studija ekspresije gena posmrtnog mozga pokazala je da ANK1 stupa u interakciju sa signalizacijom interferona-γ.^[11]

Interakcije

Pokazalo se da ANK1 stupa u interakciju sa invazivnim limfomom T-ćelija i proteinom 1 koji izaziva metastaze,^[12] Titinom,^[13] RHAG-om^[14] i OBSCN-om.^[15]

Također pogledajte

Ankirin

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000029534 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000031543 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Lambert S, Yu H, Prchal JT, et al. (mart 1990). "cDNA sequence for human erythrocyte ankyrin". Proc. Natl. Acad. Sci. U.S.A. 87 (5): 1730–4. Bibcode:1990PNAS...87.1730L. doi:10.1073/pnas.87.5.1730. PMC 53556. PMID 1689849.
^ ^a ^b ^c ^d ^e "Entrez Gene: ANK1 ankyrin 1, erythrocytic".
^ "UniProt, P16157". Pristupljeno 13. 9. 2021.
^ Borzok MA, Catino DH, Nicholson JD, Kontrogianni-Konstantopoulos A, Bloch RJ (novembar 2007). "Mapping the binding site on small ankyrin 1 for obscurin". J. Biol. Chem. 282 (44): 32384–96. doi:10.1074/jbc.M704089200. PMID 17720975.
^ De Jager, P. L.; Srivastava, G; Lunnon, K; Burgess, J; Schalkwyk, L. C.; Yu, L; Eaton, M. L.; Keenan, B. T.; Ernst, J; McCabe, C; Tang, A; Raj, T; Replogle, J; Brodeur, W; Gabriel, S; Chai, H. S.; Younkin, C; Younkin, S. G.; Zou, F; Szyf, M; Epstein, C. B.; Schneider, J. A.; Bernstein, B. E.; Meissner, A; Ertekin-Taner, N; Chibnik, L. B.; Kellis, M; Mill, J; Bennett, D. A. (2014). "Alzheimer's disease: Early alterations in brain DNA methylation at ANK1, BIN1, RHBDF2 and other loci". Nature Neuroscience. 17 (9): 1156–63. doi:10.1038/nn.3786. PMC 4292795. PMID 25129075.
^ Lunnon, K; Smith, R; Hannon, E; De Jager, P. L.; Srivastava, G; Volta, M; Troakes, C; Al-Sarraj, S; Burrage, J; MacDonald, R; Condliffe, D; Harries, L. W.; Katsel, P; Haroutunian, V; Kaminsky, Z; Joachim, C; Powell, J; Lovestone, S; Bennett, D. A.; Schalkwyk, L. C.; Mill, J (2014). "Methylomic profiling implicates cortical deregulation of ANK1 in Alzheimer's disease". Nature Neuroscience. 17 (9): 1164–70. doi:10.1038/nn.3782. PMC 4410018. PMID 25129077.
^ Liscovitch, N; French, L (2014). "Differential Co-Expression between α-Synuclein and IFN-γ Signaling Genes across Development and in Parkinson's Disease". PLOS ONE. 9 (12): e115029. Bibcode:2014PLoSO...9k5029L. doi:10.1371/journal.pone.0115029. PMC 4262449. PMID 25493648.
^ Bourguignon, L Y; Zhu H; Shao L; Chen Y W (juli 2000). "Ankyrin-Tiam1 interaction promotes Rac1 signaling and metastatic breast tumor cell invasion and migration". J. Cell Biol. 150 (1): 177–91. doi:10.1083/jcb.150.1.177. ISSN 0021-9525. PMC 2185563. PMID 10893266.
^ Kontrogianni-Konstantopoulos, Aikaterini; Bloch Robert J (februar 2003). "The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin". J. Biol. Chem. 278 (6): 3985–91. doi:10.1074/jbc.M209012200. ISSN 0021-9258. PMID 12444090.
^ Nicolas, Virginie; Le Van Kim, Caroline; Gane, Pierre; Birkenmeier, Connie; Cartron, Jean-Pierre; Colin, Yves; Mouro-Chanteloup, Isabelle (juli 2003). "Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation". J. Biol. Chem. 278 (28): 25526–33. doi:10.1074/jbc.M302816200. ISSN 0021-9258. PMID 12719424.
^ Kontrogianni-Konstantopoulos, Aikaterini; Jones Ellene M; Van Rossum Damian B; Bloch Robert J (mart 2003). "Obscurin is a ligand for small ankyrin 1 in skeletal muscle". Mol. Biol. Cell. 14 (3): 1138–48. doi:10.1091/mbc.E02-07-0411. ISSN 1059-1524. PMC 151585. PMID 12631729.

Dopunska literatura

Bennett V, Baines AJ (2001). "Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues". Physiol. Rev. 81 (3): 1353–92. doi:10.1152/physrev.2001.81.3.1353. PMID 11427698.
Bennett V (1979). "Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissues". Nature. 281 (5732): 597–9. Bibcode:1979Natur.281..597B. doi:10.1038/281597a0. PMID 492324. S2CID 263106.
Lambert S, Yu H, Prchal JT, et al. (1990). "cDNA sequence for human erythrocyte ankyrin". Proc. Natl. Acad. Sci. U.S.A. 87 (5): 1730–4. Bibcode:1990PNAS...87.1730L. doi:10.1073/pnas.87.5.1730. PMC 53556. PMID 1689849.
Fujimoto T, Lee K, Miwa S, Ogawa K (1991). "Immunocytochemical localization of fodrin and ankyrin in bovine chromaffin cells in vitro". J. Histochem. Cytochem. 39 (11): 1485–93. doi:10.1177/39.11.1833445. PMID 1833445.
Lux SE, John KM, Bennett V (1990). "Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins". Nature. 344 (6261): 36–42. Bibcode:1990Natur.344...36L. doi:10.1038/344036a0. PMID 2137557. S2CID 4351060.
Davis LH, Bennett V (1990). "Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin". J. Biol. Chem. 265 (18): 10589–96. doi:10.1016/S0021-9258(18)86987-3. PMID 2141335.
Korsgren C, Cohen CM (1988). "Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3". J. Biol. Chem. 263 (21): 10212–8. doi:10.1016/S0021-9258(19)81500-4. PMID 2968981.
Cianci CD, Giorgi M, Morrow JS (1988). "Phosphorylation of ankyrin down-regulates its cooperative interaction with spectrin and protein 3". J. Cell. Biochem. 37 (3): 301–15. doi:10.1002/jcb.240370305. PMID 2970468. S2CID 42349239.
Steiner JP, Bennett V (1988). "Ankyrin-independent membrane protein-binding sites for brain and erythrocyte spectrin". J. Biol. Chem. 263 (28): 14417–25. doi:10.1016/S0021-9258(18)68236-5. PMID 2971657.
Hargreaves WR, Giedd KN, Verkleij A, Branton D (1981). "Reassociation of ankyrin with band 3 in erythrocyte membranes and in lipid vesicles". J. Biol. Chem. 255 (24): 11965–72. doi:10.1016/S0021-9258(19)70228-2. PMID 6449514.
Bourguignon LY, Lokeshwar VB, Chen X, Kerrick WG (1994). "Hyaluronic acid-induced lymphocyte signal transduction and HA receptor (GP85/CD44)-cytoskeleton interaction". J. Immunol. 151 (12): 6634–44. PMID 7505012.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Morgans CW, Kopito RR (1993). "Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin". J. Cell Sci. 105. ( Pt 4) (4): 1137–42. doi:10.1242/jcs.105.4.1137. PMID 8227202.
Bourguignon LY, Jin H, Iida N, et al. (1993). "The involvement of ankyrin in the regulation of inositol 1,4,5-trisphosphate receptor-mediated internal Ca2 release from Ca2 storage vesicles in mouse T-lymphoma cells". J. Biol. Chem. 268 (10): 7290–7. doi:10.1016/S0021-9258(18)53175-6. PMID 8385102.
Eber SW, Gonzalez JM, Lux ML, et al. (1996). "Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis". Nat. Genet. 13 (2): 214–8. doi:10.1038/ng0696-214. PMID 8640229. S2CID 10946374.
Lanfranchi G, Muraro T, Caldara F, et al. (1996). "Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization". Genome Res. 6 (1): 35–42. doi:10.1101/gr.6.1.35. PMID 8681137.
del Giudice EM, Hayette S, Bozon M, et al. (1996). "Ankyrin Napoli: a de novo deletional frameshift mutation in exon 16 ankyrin gene (ANK1) associated with spherocytosis". Br. J. Haematol. 93 (4): 828–34. doi:10.1046/j.1365-2141.1996.d01-1746.x. PMID 8703812. S2CID 28906962.
Zhou D, Birkenmeier CS, Williams MW, et al. (1997). "Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated with the sarcoplasmic reticulum of mammalian skeletal muscle". J. Cell Biol. 136 (3): 621–31. doi:10.1083/jcb.136.3.621. PMC 2134284. PMID 9024692.
Gallagher PG, Tse WT, Scarpa AL, et al. (1997). "Structure and organization of the human ankyrin-1 gene. Basis for complexity of pre-mRNA processing". J. Biol. Chem. 272 (31): 19220–8. doi:10.1074/jbc.272.31.19220. PMID 9235914.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.

Vanjski linkovi

ANK1 protein, human na US National Library of Medicine Medical Subject Headings (MeSH)
Lokacija ljudskog genoma ANK1 i stranica sa detaljima o genu ANK1 u UCSC Genome Browseru.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000029534 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000031543 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1689849-5] Lambert S, Yu H, Prchal JT, et al. (mart 1990). "cDNA sequence for human erythrocyte ankyrin". Proc. Natl. Acad. Sci. U.S.A. 87 (5): 1730–4. Bibcode:1990PNAS...87.1730L. doi:10.1073/pnas.87.5.1730. PMC 53556. PMID 1689849.

[entrez_286-6] "Entrez Gene: ANK1 ankyrin 1, erythrocytic".

[UniProt-7] "UniProt, P16157". Pristupljeno 13. 9. 2021.

[pmid17720975-8] Borzok MA, Catino DH, Nicholson JD, Kontrogianni-Konstantopoulos A, Bloch RJ (novembar 2007). "Mapping the binding site on small ankyrin 1 for obscurin". J. Biol. Chem. 282 (44): 32384–96. doi:10.1074/jbc.M704089200. PMID 17720975.

[9] De Jager, P. L.; Srivastava, G; Lunnon, K; Burgess, J; Schalkwyk, L. C.; Yu, L; Eaton, M. L.; Keenan, B. T.; Ernst, J; McCabe, C; Tang, A; Raj, T; Replogle, J; Brodeur, W; Gabriel, S; Chai, H. S.; Younkin, C; Younkin, S. G.; Zou, F; Szyf, M; Epstein, C. B.; Schneider, J. A.; Bernstein, B. E.; Meissner, A; Ertekin-Taner, N; Chibnik, L. B.; Kellis, M; Mill, J; Bennett, D. A. (2014). "Alzheimer's disease: Early alterations in brain DNA methylation at ANK1, BIN1, RHBDF2 and other loci". Nature Neuroscience. 17 (9): 1156–63. doi:10.1038/nn.3786. PMC 4292795. PMID 25129075.

[10] Lunnon, K; Smith, R; Hannon, E; De Jager, P. L.; Srivastava, G; Volta, M; Troakes, C; Al-Sarraj, S; Burrage, J; MacDonald, R; Condliffe, D; Harries, L. W.; Katsel, P; Haroutunian, V; Kaminsky, Z; Joachim, C; Powell, J; Lovestone, S; Bennett, D. A.; Schalkwyk, L. C.; Mill, J (2014). "Methylomic profiling implicates cortical deregulation of ANK1 in Alzheimer's disease". Nature Neuroscience. 17 (9): 1164–70. doi:10.1038/nn.3782. PMC 4410018. PMID 25129077.

[11] Liscovitch, N; French, L (2014). "Differential Co-Expression between α-Synuclein and IFN-γ Signaling Genes across Development and in Parkinson's Disease". PLOS ONE. 9 (12): e115029. Bibcode:2014PLoSO...9k5029L. doi:10.1371/journal.pone.0115029. PMC 4262449. PMID 25493648.

[pmid10893266-12] Bourguignon, L Y; Zhu H; Shao L; Chen Y W (juli 2000). "Ankyrin-Tiam1 interaction promotes Rac1 signaling and metastatic breast tumor cell invasion and migration". J. Cell Biol. 150 (1): 177–91. doi:10.1083/jcb.150.1.177. ISSN 0021-9525. PMC 2185563. PMID 10893266.

[pmid12444090-13] Kontrogianni-Konstantopoulos, Aikaterini; Bloch Robert J (februar 2003). "The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin". J. Biol. Chem. 278 (6): 3985–91. doi:10.1074/jbc.M209012200. ISSN 0021-9258. PMID 12444090.

[pmid12719424-14] Nicolas, Virginie; Le Van Kim, Caroline; Gane, Pierre; Birkenmeier, Connie; Cartron, Jean-Pierre; Colin, Yves; Mouro-Chanteloup, Isabelle (juli 2003). "Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation". J. Biol. Chem. 278 (28): 25526–33. doi:10.1074/jbc.M302816200. ISSN 0021-9258. PMID 12719424.

[pmid12631729-15] Kontrogianni-Konstantopoulos, Aikaterini; Jones Ellene M; Van Rossum Damian B; Bloch Robert J (mart 2003). "Obscurin is a ligand for small ankyrin 1 in skeletal muscle". Mol. Biol. Cell. 14 (3): 1138–48. doi:10.1091/mbc.E02-07-0411. ISSN 1059-1524. PMC 151585. PMID 12631729.

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