Reviewed,
UniProtKB/Swiss-Prot Q01484 (ANK2_HUMAN)
Last modified
February 9, 2010.
Version 105.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
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Names and origin
| Protein names | Recommended name: Ankyrin-2 Short name=ANK-2 Alternative name(s): Brain ankyrin Ankyrin-B Non-erythroid ankyrin | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 3924 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Attaches integral membrane proteins to cytoskeletal elements. Also binds to cytoskeletal proteins. Required for coordinate assembly of Na/Ca exchanger, Na/K ATPase and InsP3 receptor at sarcoplasmic reticulum sites in cardiomyocytes. Required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) in the inner segment of rod photoreceptors. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate. Ref.8 |
| Subunit structure | |
| Subcellular location | Cytoplasm › cytoskeleton. Membrane. Cytoplasm › myofibril › sarcomere › M-band By similarity. Apical cell membrane By similarity. Cell membrane. Note: Expressed at the apical membrane of airway lung epithelial cells By similarity. Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distict intracellular compartment of neonatal cardiomyocytes By similarity. Ref.14 |
| Tissue specificity | Present in plasma membrane of neurons as well as glial cells throughout the brain. Expressed in fetal brain and in temporal cortex of adult brain. Also expressed in the inner segments of rod photoreceptors in retina. Ref.14 Ref.1 Ref.7 |
| Post-translational modification | Phosphorylated at multiple sites by different protein kinases and each phosphorylation event regulates the protein's structure and function Potential. Ref.11 Ref.12 Ref.13 |
| Involvement in disease | Defects in ANK2 are the cause of long QT syndrome type 4 (LQT4) [MIM:600919]; also known as sick sinus syndrome with bradycardia. Long QT syndromes are heart disorders characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress. LQT4 displays many atypical features compared to classical long QT syndromes, including pronounced sinus bradycardia, polyphasic T waves and atrial fibrillation. Cardiac repolarization defects may be not as severe as in classical LQT syndromes and prolonged QT interval on EKG is not a consistent feature. Ref.8 Ref.16 |
| Sequence similarities | Contains 24 ANK repeats. Contains 1 death domain. Contains 1 ZU5 domain. |
| Sequence caution | The sequence AAI25237.1 differs from that shown. Reason: Frameshift at position 1372. The sequence CAB42644.1 differs from that shown. Reason: Miscellaneous discrepancy. CDS lacks C-terminal region which is nevertheless present in the underlying cDNA. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Cytoplasm Cytoskeleton Membrane |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Disease | Disease mutation Long QT syndrome |
| Domain | ANK repeat Repeat |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | signal transduction Inferred from electronic annotation. Source: InterPro |
| Cellular component | M band Inferred from electronic annotation. Source: UniProtKB-SubCell apical plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell basolateral plasma membrane Ref.10Inferred from direct assay. Source: UniProtKB cytoskeletonInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | protein binding Ref.9 Inferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| DCTN4 | Q9UJW0 | 1 | EBI-941975,EBI-2134033 | |
| DMD | P11532-5 | 1 | EBI-941975,EBI-1018651 | |
| GRB2 | P62993 | 1 | EBI-941975,EBI-401755 | |
| NCK1 | P16333 | 1 | EBI-941975,EBI-389883 | |
| OBSCN | Q5VST9-3 | 1 | EBI-941994,EBI-941921 |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q01484-1) 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. | ||||||
| Isoform 2 (identifier: Q01484-2) The sequence of this isoform differs from the canonical sequence as follows: 1039-1039: Q → QFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTK 1444-3528: Missing. | ||||||
| Isoform 3 (identifier: Q01484-4) The sequence of this isoform differs from the canonical sequence as follows: 1039-1039: Q → QFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTK | ||||||
| Isoform 4 (identifier: Q01484-5) The sequence of this isoform differs from the canonical sequence as follows: 1-27: MMNEDAAQKSDSGEKFNGSSQRRKRPK → MTTMLQ 967-967: G → GRASPCLERDNSS 1039-1039: Q → QFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTK 1444-3528: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 5 (identifier: Q01484-7) The sequence of this isoform differs from the canonical sequence as follows: 1-1315: Missing. 1444-3528: Missing. 3837-3837: K → KELTEELGELEASSDEEAMVTTRVVRRRVIIQ |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 3924 | 3924 | Ankyrin-2 | PRO_0000066885 | |||||
Regions | |||||||||
| Repeat | 30 – 62 | 33 | ANK 1 | ||||||
| Repeat | 63 – 92 | 30 | ANK 2 | ||||||
| Repeat | 96 – 125 | 30 | ANK 3 | ||||||
| Repeat | 129 – 158 | 30 | ANK 4 | ||||||
| Repeat | 162 – 191 | 30 | ANK 5 | ||||||
| Repeat | 193 – 220 | 28 | ANK 6 | ||||||
| Repeat | 232 – 261 | 30 | ANK 7 | ||||||
| Repeat | 265 – 294 | 30 | ANK 8 | ||||||
| Repeat | 298 – 327 | 30 | ANK 9 | ||||||
| Repeat | 331 – 360 | 30 | ANK 10 | ||||||
| Repeat | 364 – 393 | 30 | ANK 11 | ||||||
| Repeat | 397 – 426 | 30 | ANK 12 | ||||||
| Repeat | 430 – 459 | 30 | ANK 13 | ||||||
| Repeat | 463 – 492 | 30 | ANK 14 | ||||||
| Repeat | 496 – 525 | 30 | ANK 15 | ||||||
| Repeat | 529 – 558 | 30 | ANK 16 | ||||||
| Repeat | 562 – 591 | 30 | ANK 17 | ||||||
| Repeat | 595 – 624 | 30 | ANK 18 | ||||||
| Repeat | 628 – 657 | 30 | ANK 19 | ||||||
| Repeat | 661 – 690 | 30 | ANK 20 | ||||||
| Repeat | 694 – 723 | 30 | ANK 21 | ||||||
| Repeat | 727 – 756 | 30 | ANK 22 | ||||||
| Repeat | 760 – 789 | 30 | ANK 23 | ||||||
| Repeat | 793 – 822 | 30 | ANK 24 | ||||||
| Domain | 966 – 1073 | 108 | ZU5 | ||||||
| Repeat | 1773 – 1784 | 12 | Repeat A | ||||||
| Repeat | 1785 – 1796 | 12 | Repeat A | ||||||
| Repeat | 1797 – 1808 | 12 | Repeat A | ||||||
| Repeat | 1809 – 1820 | 12 | Repeat A | ||||||
| Repeat | 1821 – 1832 | 12 | Repeat A | ||||||
| Repeat | 1833 – 1844 | 12 | Repeat A | ||||||
| Repeat | 1845 – 1856 | 12 | Repeat A | ||||||
| Repeat | 1857 – 1867 | 11 | Repeat A; approximate | ||||||
| Repeat | 1868 – 1879 | 12 | Repeat A | ||||||
| Repeat | 1880 – 1891 | 12 | Repeat A | ||||||
| Repeat | 1892 – 1902 | 11 | Repeat A; approximate | ||||||
| Repeat | 1903 – 1914 | 12 | Repeat A | ||||||
| Repeat | 1915 – 1926 | 12 | Repeat A | ||||||
| Repeat | 1927 – 1938 | 12 | Repeat A | ||||||
| Repeat | 1939 – 1950 | 12 | Repeat A | ||||||
| Domain | 3536 – 3620 | 85 | Death | ||||||
| Region | 966 – 1125 | 160 | Interaction with SPTBN1 | ||||||
| Region | 1773 – 1950 | 178 | Repeat-rich region | ||||||
Amino acid modifications | |||||||||
| Modified residue | 31 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 34 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 378 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 531 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 846 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 898 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 911 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 1349 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 1428 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1475 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 1490 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 2550 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 3060 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 3240 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3329 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3357 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3376 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3377 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 3702 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3743 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 3760 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 3762 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 3764 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 3769 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3770 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 3790 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3811 | 1 | Phosphothreonine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 1315 | 1315 | Missing in isoform 5. | VSP_037057 | |||||
| Alternative sequence | 1 – 27 | 27 | MMNED…RKRPK → MTTMLQ in isoform 4. | VSP_037058 | |||||
| Alternative sequence | 967 | 1 | G → GRASPCLERDNSS in isoform 4. | VSP_037059 | |||||
| Alternative sequence | 1039 | 1 | Q → QFLGKLHLPTAPPPLNEGES LVSRILQLGPPGTK in isoform 2, isoform 3 and isoform 4. | VSP_000267 | |||||
| Alternative sequence | 1444 – 3528 | 2085 | Missing in isoform 2, isoform 4 and isoform 5. | VSP_000268 | |||||
| Alternative sequence | 3837 | 1 | K → KELTEELGELEASSDEEAMV TTRVVRRRVIIQ in isoform 5. | VSP_037060 | |||||
| Natural variant | 685 | 1 | G → E in a breast cancer sample; somatic mutation. Ref.17 | VAR_035606 | |||||
| Natural variant | 687 | 1 | N → S: dbSNP rs29372. | VAR_055504 | |||||
| Natural variant | 1234 | 1 | G → R in a colorectal cancer sample; somatic mutation. Ref.17 | VAR_035607 | |||||
| Natural variant | 1425 | 1 | E → G in LQT4; loss of function. Ref.8 Ref.16 | VAR_022934 | |||||
| Natural variant | 2336 | 1 | V → A: dbSNP rs28377576. | VAR_055505 | |||||
| Natural variant | 3620 | 1 | T → K in a colorectal cancer sample; somatic mutation. Ref.17 | VAR_035608 | |||||
| Natural variant | 3707 | 1 | L → I in LQT4; loss of function. Ref.16 | VAR_022935 | |||||
| Natural variant | 3711 | 1 | T → N in LQT4; loss of function. Ref.16 | VAR_022936 | |||||
| Natural variant | 3873 | 1 | R → W in LQT4; loss of function. Ref.16 | VAR_022937 | |||||
| Natural variant | 3898 | 1 | E → K in LQT4; loss of function. Ref.16 | VAR_022938 | |||||
Experimental info | |||||||||
| Mutagenesis | 975 – 977 | 3 | DAR → AAA: Prevents binding to SPTBN1. | ||||||
| Mutagenesis | 1000 | 1 | A → P: Prevents binding to SPTBN1. Ref.9 | ||||||
| Mutagenesis | 1067 – 1070 | 4 | ENGD → AAGA: Weak binding to SPTBN1. Ref.9 | ||||||
| Sequence conflict | 220 | 1 | V → I in CAD97827. Ref.4 | ||||||
| Sequence conflict | 475 – 476 | 2 | GQ → PE in AAA62828. Ref.7 | ||||||
| Sequence conflict | 2754 | 1 | A → R in CAB42644. Ref.3 | ||||||
| Sequence conflict | 2966 | 1 | Q → L in CAB42644. Ref.3 | ||||||
| Sequence conflict | 3107 – 3108 | 2 | EE → RY in AC093879. Ref.5 | ||||||
| Sequence conflict | 3152 | 1 | D → S in CAB42644. Ref.3 | ||||||
| Sequence conflict | 3666 | 1 | V → A in CAD97827. Ref.4 | ||||||
| Sequence conflict | 3704 | 1 | A → S in CAA40279. Ref.1 | ||||||
| Sequence conflict | 3704 | 1 | A → S in CAB42644. Ref.3 | ||||||
| Sequence conflict | 3922 – 3923 | 2 | NN → SM in AC093879. Ref.5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes." Otto E., Kunimoto M., McLaughlin T., Bennett V. J. Cell Biol. 114:241-253(1991) [PubMed: 1830053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY. Tissue: Brain stem. |
| [2] | Carpenter S. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [3] | "440-kD ankyrinB: structure of the major developmentally regulated domain and selective localization in unmyelinated axons." Chan W., Kordeli E., Bennett V. J. Cell Biol. 123:1463-1473(1993) [PubMed: 8253844] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Brain stem. |
| [4] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Retina. |
| [5] | "Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K.Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). |
| [7] | "Isolation and chromosomal localization of a novel nonerythroid ankyrin gene." Tse W.T., Menninger J.C., Yang-Feng T.L., Francke U., Sahr K.E., Lux S.E., Ward D.C., Forget B.G. Genomics 10:858-866(1991) [PubMed: 1833308] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 463-495, TISSUE SPECIFICITY. |
| [8] | "Ankyrin-B mutation causes type 4 long-QT cardiac arrhythmia and sudden cardiac death." Mohler P.J., Schott J.-J., Gramolini A.O., Dilly K.W., Guatimosim S., duBell W.H., Song L.-S., Haurogne K., Kyndt F., Ali M.E., Rogers T.B., Lederer W.J., Escande D., Le Marec H., Bennett V. Nature 421:634-639(2003) [PubMed: 12571597] [Abstract] Cited for: FUNCTION, VARIANT LQT4 GLY-1425. |
| [9] | "Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes." Mohler P.J., Yoon W., Bennett V. J. Biol. Chem. 279:40185-40193(2004) [PubMed: 15262991] [Abstract] Cited for: INTERACTION WITH SPTBN1, MUTAGENESIS OF 975-ASP--ARG-977; ALA-1000 AND 1067-GLU--ASP-1070. |
| [10] | "The ammonium transporter RhBG: requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells." Lopez C., Metral S., Eladari D., Drevensek S., Gane P., Chambrey R., Bennett V., Cartron J.-P., Le Van Kim C., Colin Y. J. Biol. Chem. 280:8221-8228(2005) [PubMed: 15611082] [Abstract] Cited for: INTERACTION WITH RHBG. |
| [11] | "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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2550, MASS SPECTROMETRY. Tissue: Epithelium. |
| [12] | "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911; SER-1475 AND THR-1490, MASS SPECTROMETRY. |
| [13] | "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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3760; SER-3762 AND THR-3764, MASS SPECTROMETRY. |
| [14] | "Ankyrin-B is required for coordinated expression of beta-2-spectrin, the Na/K-ATPase and the Na/Ca exchanger in the inner segment of rod photoreceptors." Kizhatil K., Sandhu N.K., Peachey N.S., Bennett V. Exp. Eye Res. 88:57-64(2009) [PubMed: 19007774] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
| [15] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [16] | "A cardiac arrhythmia syndrome caused by loss of ankyrin-B function." Mohler P.J., Splawski I., Napolitano C., Bottelli G., Sharpe L., Timothy K., Priori S.G., Keating M.T., Bennett V. Proc. Natl. Acad. Sci. U.S.A. 101:9137-9142(2004) [PubMed: 15178757] [Abstract] Cited for: VARIANTS LQT4 GLY-1425; ILE-3707; ASN-3711; TRP-3873 AND LYS-3898, CHARACTERIZATION OF VARIANTS LQT4. |
| [17] | "The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E.Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-685; ARG-1234 AND LYS-3620. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X56957 mRNA. Translation: CAA40278.1. X56958 mRNA. Translation: CAA40279.2. Z26634 mRNA. Translation: CAB42644.1. Sequence problems. BX537758 mRNA. Translation: CAD97827.1. AC004057 Genomic DNA. No translation available. AC093617 Genomic DNA. No translation available. AC093879 Genomic DNA. No translation available. AC093900 Genomic DNA. No translation available. BC125235 mRNA. Translation: AAI25236.1. BC125236 mRNA. Translation: AAI25237.1. Frameshift. M37123 Genomic DNA. Translation: AAA62828.1. |
| IPI | IPI00007834. IPI00074962. IPI00305279. IPI00384928. IPI00895856. |
| PIR | S37431. |
| RefSeq | NP_001120965.1. NP_001139.3. NP_066187.2. |
| UniGene | Hs.620557 |
3D structure databases | |
| DisProt | DP00467. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q01484. 6 interactions. |
| STRING | Q01484. |
Protein family/group databases | |
| TCDB | 8.A.28.1.1. ankyrin family. |
PTM databases | |
| PhosphoSite | Q01484. |
Genome annotation databases | |
| Ensembl | ENST00000361149; ENSP00000354873; ENSG00000145362; Homo sapiens. [Genome view] |
| GeneID | 287. |
| KEGG | hsa:287. |
| UCSC | uc003ibe.2. human. uc003ibf.2. human. |
Organism-specific databases | |
| CTD | 287. |
| GeneCards | GC04P114132. |
| HGNC | HGNC:493. ANK2. |
| MIM | 106410. gene. 600919. phenotype. |
| Orphanet | 768. Long QT syndrome, familial. |
| PharmGKB | PA24799. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG17755. |
| HOVERGEN | Q01484. |
| OMA | KTEKHSP. |
| OrthoDB | EOG9VHNS3. |
Gene expression databases | |
| ArrayExpress | Q01484. |
| Bgee | Q01484. |
| CleanEx | HS_ANK2. |
| Genevestigator | Q01484. |
| GermOnline | ENSG00000145362. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR000488. Death. IPR011029. DEATH-like. IPR000906. ZU5. [Graphical view] |
| Gene3D | G3DSA:1.25.40.20. ANK. 4 hits. G3DSA:1.10.533.10. DEATH_like. 1 hit. |
| Pfam | PF00023. Ank. 19 hits. PF00531. Death. 1 hit. PF00791. ZU5. 1 hit. [Graphical view] |
| SMART | SM00248. ANK. 23 hits. SM00005. DEATH. 1 hit. SM00218. ZU5. 1 hit. [Graphical view] |
| PROSITE | PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 20 hits. PS50017. DEATH_DOMAIN. 1 hit. PS51145. ZU5. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| SOURCE | Search... |
Entry information
| Entry name | ANK2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q01484 Secondary accession number(s): Q01485 Q7Z3L5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 4 Human chromosome 4: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


