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UniProtKB/Swiss-Prot Q8WWM7 (ATX2L_HUMAN)
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November 24, 2009.
Version 71.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Ataxin-2-like protein Alternative name(s): Ataxin-2 domain protein Ataxin-2-related protein | ||||
| 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 | 1075 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Subunit structure | Interacts with MPL/TPOR and EPOR and dissociates after ligand stimulation. Ref.1 |
| Subcellular location | |
| Tissue specificity | Expressed at high levels in thymus, lymph node, spleen, fetal kidney and adult testis. Constitutively associated with MPL and EPOR in hematopoietic cells. Ref.1 |
| Post-translational modification | Thrombopoietin triggers the phosphorylation on tyrosine residues in a way that is dependent on MPL C-terminal domain. Arg-361 is dimethylated, probably to asymmetric dimethylarginine. Ref.8 |
| Sequence similarities | Belongs to the ataxin-2 family. |
| Sequence caution | The sequence AAC69607.1 differs from that shown. Reason: Frameshift at positions 31, 429, 432 and 446. The sequence AAO12056.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAO12057.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAO12058.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAO12058.1 differs from that shown. Reason: Miscellaneous discrepancy. Exon duplication. The sequence AAO12059.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAO12059.1 differs from that shown. Reason: Miscellaneous discrepancy. Exon duplication. The sequence AAO12060.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAO12060.1 differs from that shown. Reason: Miscellaneous discrepancy. Exon duplication. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Coding sequence diversity | Alternative splicing |
| PTM | Acetylation Methylation Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Alternative products
| This entry describes 7 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q8WWM7-1) Also known as: A2D-A; 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: Q8WWM7-2) Also known as: A2D-B; The sequence of this isoform differs from the canonical sequence as follows: 1047-1075: REFSLAGGIWHGRAEGLQVGQDARVLGGE → PPFPPPGELKIVLAAT | ||||||
| Isoform 3 (identifier: Q8WWM7-3) Also known as: A2D-C; The sequence of this isoform differs from the canonical sequence as follows: 1047-1075: REFSLAGGIWHGRAEGLQVGQDARVLGGE → LCRVGRSHSR...ALSDPDCLLT | ||||||
| Isoform 4 (identifier: Q8WWM7-4) Also known as: A2D-D; The sequence of this isoform differs from the canonical sequence as follows: 1029-1075: GEQPGQAPGFPGGADDRIREFSLAGGIWHGRAEGLQVGQDARVLGGE → VQSHPSQQLPFHPPGN | ||||||
| Isoform 5 (identifier: Q8WWM7-5) Also known as: A2D-E; The sequence of this isoform differs from the canonical sequence as follows: 1029-1075: GEQPGQAPGFPGGADDRIREFSLAGGIWHGRAEGLQVGQDARVLGGE → APFPPPGELKIVLAAT | ||||||
| Isoform 6 (identifier: Q8WWM7-6) The sequence of this isoform differs from the canonical sequence as follows: 896-967: HQAGQAPHLG...TNMAHVTQAH → VPAMGGAEWS...HSRICTTQGP 968-1075: Missing. | ||||||
| Note: Due to intron retention. No experimental confirmation available. | ||||||
| Isoform 7 (identifier: Q8WWM7-7) The sequence of this isoform differs from the canonical sequence as follows: 354-400: QRVREGPRGG...SPGPGSEARG → HRGQGQGPAG...DGRSFIFYYL 401-1075: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1075 | 1075 | Ataxin-2-like protein | PRO_0000064754 | |||||
Regions | |||||||||
| Region | 98 – 121 | 24 | Interaction with MPL | ||||||
| Compositional bias | 4 – 84 | 81 | Pro-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.5 | ||||||
| Modified residue | 111 | 1 | Phosphoserine Ref.9 Ref.11 Ref.13 Ref.15 Ref.17 | ||||||
| Modified residue | 118 | 1 | Phosphotyrosine | ||||||
| Modified residue | 238 | 1 | Phosphoserine | ||||||
| Modified residue | 264 | 1 | Phosphotyrosine Ref.7 | ||||||
| Modified residue | 309 | 1 | Phosphotyrosine Ref.7 | ||||||
| Modified residue | 335 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 339 | 1 | Phosphoserine Ref.13 Ref.16 | ||||||
| Modified residue | 341 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 348 | 1 | N6-acetyllysine Ref.21 | ||||||
| Modified residue | 349 | 1 | Phosphotyrosine Ref.7 | ||||||
| Modified residue | 361 | 1 | Omega-N-methylated arginine Ref.8 | ||||||
| Modified residue | 390 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 391 | 1 | Phosphoserine Ref.7 Ref.12 | ||||||
| Modified residue | 409 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 449 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 493 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 496 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 557 | 1 | Phosphoserine Ref.13 Ref.17 | ||||||
| Modified residue | 558 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 559 | 1 | Phosphoserine Ref.9 Ref.13 Ref.15 Ref.17 Ref.12 | ||||||
| Modified residue | 563 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 589 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 594 | 1 | Phosphoserine Ref.9 Ref.11 Ref.13 Ref.17 Ref.16 Ref.10 Ref.14 | ||||||
| Modified residue | 597 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 598 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 630 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 634 | 1 | Phosphoserine Ref.15 Ref.17 | ||||||
| Modified residue | 684 | 1 | Phosphoserine Ref.17 Ref.12 | ||||||
Natural variations | |||||||||
| Alternative sequence | 354 – 400 | 47 | QRVRE…SEARG → HRGQGQGPAGVGGSCSAPAR PHPVLPSHPLIYSPAGDGRS FIFYYL in isoform 7. | VSP_011587 | |||||
| Alternative sequence | 401 – 1075 | 675 | Missing in isoform 7. | VSP_011588 | |||||
| Alternative sequence | 896 – 967 | 72 | HQAGQ…VTQAH → VPAMGGAEWSWCRNGWPEEG IELGVISEWRGLGASELLAC VALNLPLPSSIRRGRPHTWA VDSHSRICTTQGP in isoform 6. | VSP_011589 | |||||
| Alternative sequence | 968 – 1075 | 108 | Missing in isoform 6. | VSP_011590 | |||||
| Alternative sequence | 1029 – 1075 | 47 | GEQPG…VLGGE → VQSHPSQQLPFHPPGN in isoform 4. | VSP_011591 | |||||
| Alternative sequence | 1029 – 1075 | 47 | GEQPG…VLGGE → APFPPPGELKIVLAAT in isoform 5. | VSP_011592 | |||||
| Alternative sequence | 1047 – 1075 | 29 | REFSL…VLGGE → PPFPPPGELKIVLAAT in isoform 2. | VSP_011593 | |||||
| Alternative sequence | 1047 – 1075 | 29 | REFSL…VLGGE → LCRVGRSHSRRRQGLAPGSV LCFPPSSLSCDPAAPLPTAS PALSDPDCLLT in isoform 3. | VSP_011594 | |||||
Experimental info | |||||||||
| Sequence conflict | 337 | 1 | R → RG Ref.6 | ||||||
| Sequence conflict | 689 | 1 | T → S in CAC38068. Ref.1 | ||||||
| Sequence conflict | 689 | 1 | T → S in CAC38069. Ref.1 | ||||||
| Sequence conflict | 689 | 1 | T → S in CAC38070. Ref.1 | ||||||
| Sequence conflict | 689 | 1 | T → S in CAC38071. Ref.1 | ||||||
| Sequence conflict | 689 | 1 | T → S in CAC38072. Ref.1 | ||||||
| Sequence conflict | 726 | 1 | P → T in CAC38068. Ref.1 | ||||||
| Sequence conflict | 726 | 1 | P → T in CAC38069. Ref.1 | ||||||
| Sequence conflict | 726 | 1 | P → T in CAC38070. Ref.1 | ||||||
| Sequence conflict | 726 | 1 | P → T in CAC38071. Ref.1 | ||||||
| Sequence conflict | 726 | 1 | P → T in CAC38072. Ref.1 | ||||||
| Sequence conflict | 895 | 1 | Q → QQ in AAH10239. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of a family of proteins associated with Mpl." Meunier C.F., Bordereaux D., Porteu F., Gisselbrecht S., Chretien S., Courtois G. J. Biol. Chem. 277:9139-9147(2002) [PubMed: 11784712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY, INTERACTION WITH MPL AND EPOR. |
| [2] | "Identification and expression of the gene for human ataxin-2-related protein on chromosome 16." Figueroa K.P., Pulst S.M. Exp. Neurol. 184:669-678(2003) [PubMed: 14769358] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [3] | "A splicing form of human ataxin-2 like gene obtained from adult brain." Xia J.-H., Liu C.-Y., Wang D.-A., Ruan Q.-G., Deng H.-X. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6). Tissue: Brain. |
| [4] | "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] (ISOFORMS 1 AND 4). Tissue: Skin and Testis. |
| [5] | Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-25; 141-150; 156-165; 197-218; 259-283; 302-310; 383-399; 421-443; 499-507; 517-525; 540-546 AND 554-570, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Colon carcinoma. |
| [6] | "Moderate expansion of a normally biallelic trinucleotide repeat in spinocerebellar ataxia type 2." Pulst S.-M., Nechiporuk A., Nechiporuk T., Gispert S., Chen X.-N., Lopes-Cendes I., Pearlman S., Starkman S., Orozco-Diaz G., Lunkes A., DeJong P., Rouleau G.A., Auburger G., Korenberg J.R., Figueroa C., Sahba S. Nat. Genet. 14:269-276(1996) [PubMed: 8896555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-1075 (ISOFORM 7). |
| [7] | "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-264; TYR-309; TYR-349 AND SER-391, MASS SPECTROMETRY. Tissue: T-cell. |
| [8] | "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-361, MASS SPECTROMETRY. |
| [9] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-559 AND SER-594, MASS SPECTROMETRY. Tissue: Epithelium. |
| [10] | "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 SER-409; SER-493; SER-496 AND SER-594, MASS SPECTROMETRY. Tissue: Epithelium. |
| [11] | "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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111 AND SER-594, MASS SPECTROMETRY. Tissue: Epithelium. |
| [12] | "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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-391; SER-559 AND SER-684, MASS SPECTROMETRY. Tissue: Epithelium. |
| [13] | "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-111; SER-335; SER-339; SER-341; SER-557; SER-558; SER-559; SER-563; SER-589; SER-594; SER-597 AND SER-598, MASS SPECTROMETRY. |
| [14] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, MASS SPECTROMETRY. |
| [15] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-449; SER-559; SER-630 AND SER-634, MASS SPECTROMETRY. |
| [16] | "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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339 AND SER-594, MASS SPECTROMETRY. |
| [17] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-557; SER-559; SER-594; SER-634 AND SER-684, MASS SPECTROMETRY. |
| [18] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [19] | "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-496; SER-559; SER-594; SER-597; SER-598 AND SER-684, MASS SPECTROMETRY. |
| [20] | "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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; TYR-118; SER-238; SER-558; SER-559 AND SER-594, MASS SPECTROMETRY. Tissue: T-cell. |
| [21] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-348, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AJ317970 mRNA. Translation: CAC38068.1. AJ317971 mRNA. Translation: CAC38069.3. AJ317972 mRNA. Translation: CAC38070.3. AJ317973 mRNA. Translation: CAC38071.3. AJ317974 mRNA. Translation: CAC38072.3. AY188334 mRNA. Translation: AAO12056.1. Frameshift. AY188335 mRNA. Translation: AAO12057.1. Frameshift. AY188336 mRNA. Translation: AAO12058.1. Sequence problems. AY188337 mRNA. Translation: AAO12059.1. Sequence problems. AY188338 mRNA. Translation: AAO12060.1. Sequence problems. AF034373 mRNA. Translation: AAC69607.1. Frameshift. BC010239 mRNA. Translation: AAH10239.1. BC068012 mRNA. Translation: AAH68012.1. Sequence problems. BC136584 mRNA. Translation: AAI36585.1. U70671 mRNA. Translation: AAB19201.1. | |
| IPI | IPI00456359. IPI00456361. IPI00456363. IPI00456365. IPI00456367. IPI00456369. IPI00479363. |
| RefSeq | NP_009176.2. NP_663760.1. NP_680780.1. NP_680781.1. NP_680782.1. |
| UniGene | Hs.460499 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q8WWM7. 6 interactions. |
| STRING | Q8WWM7. |
PTM databases | |
| PhosphoSite | Q8WWM7. |
Proteomic databases | |
| PRIDE | Q8WWM7. |
Genome annotation databases | |
| Ensembl | ENST00000336783; ENSP00000338718; ENSG00000168488; Homo sapiens. [Genome view] ENST00000340394; ENSP00000341459; ENSG00000168488; Homo sapiens. [Genome view] |
| GeneID | 11273. |
| KEGG | hsa:11273. |
| UCSC | uc002dqy.1. human. uc002dqz.1. human. uc002dra.1. human. uc002drb.1. human. uc002drc.1. human. uc010byl.1. human. |
Organism-specific databases | |
| CTD | 11273. |
| GeneCards | GC16P028741. |
| H-InvDB | HIX0019790. |
| HGNC | HGNC:31326. ATXN2L. |
| MIM | 607931. gene. |
| PharmGKB | PA128394585. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | Q8WWM7. |
| OMA | PSQQLPF. |
| OrthoDB | EOG9WQ3NC. |
Gene expression databases | |
| ArrayExpress | Q8WWM7. |
| Bgee | Q8WWM7. |
| Genevestigator | Q8WWM7. |
| GermOnline | ENSG00000168488. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR009818. Ataxin-2_C. IPR009604. LsmAD_domain. [Graphical view] |
| Pfam | PF06741. LsmAD. 1 hit. PF07145. PAM2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 42897. |
| PMAP-CutDB | Q8WWM7. |
| SOURCE | Search... |
Entry information
| Entry name | ATX2L_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q8WWM7 Secondary accession number(s): B9EGM2  Q99703 | ||||||||
| 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 16 Human chromosome 16: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |
