Q14157 (UBP2L_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 98.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Ubiquitin-associated protein 2-like Alternative name(s): Protein NICE-4 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1087 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Tissue specificity | Ubiquitous. Ref.5 |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Acetylated. |
| Sequence similarities | Contains 1 UBA domain. |
| Sequence caution | The sequence CAB65100.2 differs from that shown. Reason: Frameshift at position 1085. |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Alternative splicing Polymorphism |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | binding of sperm to zona pellucida Inferred from mutant phenotype. Source: UniProtKB |
| Molecular function | protein binding Inferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q14157-2) 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: Q14157-1) The sequence of this isoform differs from the canonical sequence as follows: 969-1087: VSVTSSNTGV...AYNSYSWGAN → RKYPPPYKHFWTAES | ||||||
| Note: Acetylated on Lys-976. | ||||||
| Isoform 3 (identifier: Q14157-3) The sequence of this isoform differs from the canonical sequence as follows: 1057-1087: TGSGQRSQTSSIPQKPQTNKSAYNSYSWGAN → DILNFVDDQLGE | ||||||
| Isoform 4 (identifier: Q14157-4) The sequence of this isoform differs from the canonical sequence as follows: 143-150: GASRGREF → V 969-1087: VSVTSSNTGV...AYNSYSWGAN → RKYPPPYKHFWTAES | ||||||
| Note: Acetylated on Lys-969. No experimental confirmation available. | ||||||
| Isoform 5 (identifier: Q14157-5) The sequence of this isoform differs from the canonical sequence as follows: 1055-1055: G → GQLPYLQMILCCQRQQEE |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1087 | 1087 | Ubiquitin-associated protein 2-like | PRO_0000211020 | |||||
Regions | |||||||||
| Domain | 49 – 89 | 41 | UBA | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.21 | ||||||
| Modified residue | 360 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 416 | 1 | Phosphoserine Ref.13 Ref.14 Ref.16 Ref.19 Ref.20 | ||||||
| Modified residue | 419 | 1 | Phosphothreonine Ref.11 Ref.14 | ||||||
| Modified residue | 439 | 1 | Phosphoserine Ref.20 Ref.21 | ||||||
| Modified residue | 453 | 1 | Phosphoserine Ref.12 Ref.21 Ref.22 | ||||||
| Modified residue | 454 | 1 | Phosphoserine Ref.7 Ref.12 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 | ||||||
| Modified residue | 458 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 460 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 461 | 1 | Phosphothreonine Ref.21 | ||||||
| Modified residue | 462 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 467 | 1 | Phosphoserine Ref.7 Ref.19 Ref.20 Ref.21 Ref.22 | ||||||
| Modified residue | 470 | 1 | Phosphoserine Ref.20 Ref.21 Ref.22 Ref.23 | ||||||
| Modified residue | 471 | 1 | Phosphoserine Ref.20 Ref.21 | ||||||
| Modified residue | 475 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 476 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 477 | 1 | Phosphoserine Ref.19 Ref.20 Ref.21 Ref.23 | ||||||
| Modified residue | 604 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 605 | 1 | Phosphoserine Ref.8 Ref.19 Ref.20 | ||||||
| Modified residue | 607 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 608 | 1 | Phosphoserine Ref.20 Ref.21 | ||||||
| Modified residue | 609 | 1 | Phosphoserine Ref.7 Ref.8 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 | ||||||
| Modified residue | 834 | 1 | Phosphotyrosine Ref.10 | ||||||
| Modified residue | 835 | 1 | Phosphotyrosine Ref.9 | ||||||
| Modified residue | 844 | 1 | Phosphothreonine Ref.13 Ref.18 | ||||||
| Modified residue | 847 | 1 | Phosphothreonine Ref.23 | ||||||
| Modified residue | 852 | 1 | Phosphoserine Ref.16 Ref.20 | ||||||
| Modified residue | 859 | 1 | Phosphoserine Ref.20 Ref.23 | ||||||
Natural variations | |||||||||
| Alternative sequence | 143 – 150 | 8 | GASRGREF → V in isoform 4. | VSP_038235 | |||||
| Alternative sequence | 969 – 1087 | 119 | VSVTS…SWGAN → RKYPPPYKHFWTAES in isoform 2 and isoform 4. | VSP_019417 | |||||
| Alternative sequence | 1055 | 1 | G → GQLPYLQMILCCQRQQEE in isoform 5. | VSP_042167 | |||||
| Alternative sequence | 1057 – 1087 | 31 | TGSGQ…SWGAN → DILNFVDDQLGE in isoform 3. | VSP_021728 | |||||
| Natural variant | 482 | 1 | Q → H. Corresponds to variant rs17849745 [ dbSNP | Ensembl ]. | VAR_026829 | |||||
Experimental info | |||||||||
| Sequence conflict | 91 | 1 | P → S in BAG64560. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N. DNA Res. 2:167-174(1995) [PubMed: 8590280] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Bone marrow. |
| [2] | "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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Thymus. |
| [3] | "The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R.Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [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] (ISOFORM 1). Tissue: Skin. |
| [5] | "Identification of human epidermal differentiation complex (EDC)-encoded genes by subtractive hybridization of entire YACs to a gridded keratinocyte cDNA library." Marenholz I., Zirra M., Fischer D.F., Backendorf C., Ziegler A., Mischke D. Genome Res. 11:341-355(2001) [PubMed: 11230159] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-137 (ISOFORMS 1/2/3), NUCLEOTIDE SEQUENCE [MRNA] OF 671-1087 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 760-1087 (ISOFORM 5), TISSUE SPECIFICITY. Tissue: Keratinocyte. |
| [6] | "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 SER-607, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [7] | "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-454; SER-467 AND SER-609, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [8] | "Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605 AND SER-609, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma. |
| [9] | "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-835, MASS SPECTROMETRY. |
| [10] | "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-834, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [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-419, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "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-453 AND SER-454, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "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-416 AND THR-844, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [14] | "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-416 AND THR-419, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [15] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [16] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-609 AND SER-852, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [17] | "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-609, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [18] | "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 THR-844, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [19] | "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-416; SER-454; SER-467; SER-477; SER-604; SER-605 AND SER-609, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [20] | "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-416; SER-439; SER-454; SER-467; SER-470; SER-471; SER-477; SER-605; SER-608; SER-609; SER-852 AND SER-859, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [21] | "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-439; SER-453; SER-454; SER-458; SER-460; THR-461; SER-462; SER-467; SER-470; SER-471; SER-475; SER-476; SER-477; SER-608 AND SER-609, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [22] | "Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453; SER-454; SER-467 AND SER-470, MASS SPECTROMETRY. |
| [23] | "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-454; SER-470; SER-477; THR-847 AND SER-859, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [24] | "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-976 (ISOFORM 2), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-969 (ISOFORM 4), MASS SPECTROMETRY. |
| [25] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D63478 mRNA. Translation: BAA09765.1. AK303533 mRNA. Translation: BAG64560.1. AL590431 Genomic DNA. Translation: CAH71283.1. AL590431 Genomic DNA. Translation: CAH71284.1. AL590431 Genomic DNA. Translation: CAH71285.1. BC003170 mRNA. Translation: AAH03170.1. AJ243668 mRNA. Translation: CAB65099.1. AJ243670 mRNA. Translation: CAB65101.2. AJ243669 mRNA. Translation: CAB65100.2. Frameshift. |
| IPI | IPI00005416. IPI00029019. IPI00181306. IPI00514856. IPI00946257. |
| RefSeq | NP_001120792.1. NM_001127320.1. NP_055662.3. NM_014847.3. |
| UniGene | Hs.490551. |
3D structure databases | |
| ProteinModelPortal | Q14157. |
| SMR | Q14157. Positions 19-111. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q14157. 5 interactions. |
| MINT | MINT-1032368. |
| STRING | Q14157. |
PTM databases | |
| PhosphoSite | Q14157. |
Polymorphism databases | |
| DMDM | 109940042. |
Proteomic databases | |
| PRIDE | Q14157. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000343815; ENSP00000345308; ENSG00000143569. ENST00000361546; ENSP00000355343; ENSG00000143569. ENST00000368505; ENSP00000357491; ENSG00000143569. ENST00000428931; ENSP00000389445; ENSG00000143569. |
| GeneID | 9898. |
| KEGG | hsa:9898. |
| UCSC | uc001fep.2. human. uc009wot.1. human. |
Organism-specific databases | |
| CTD | 9898. |
| GeneCards | GC01P154192. |
| HGNC | HGNC:29877. UBAP2L. |
| HPA | HPA035068. |
| neXtProt | NX_Q14157. |
| PharmGKB | PA134883839. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG12053. |
| HOVERGEN | HBG058387. |
| InParanoid | Q14157. |
| OMA | PNDSTVH. |
| OrthoDB | EOG4V9TQ4. |
Gene expression databases | |
| ArrayExpress | Q14157. |
| Bgee | Q14157. |
| CleanEx | HS_UBAP2L. |
| Genevestigator | Q14157. |
| GermOnline | ENSG00000143569. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR022166. DUF3697_Uba2. IPR009060. UBA-like. IPR015940. UBA/transl_elong_EF1B_N_euk. [Graphical view] |
| Pfam | PF12478. DUF3697. 1 hit. [Graphical view] |
| SMART | SM00165. UBA. 1 hit. [Graphical view] |
| SUPFAM | SSF46934. UBA_like. 1 hit. |
| PROSITE | PS50030. UBA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 37319. |
| PMAP-CutDB | Q14157. |
Entry information
| Entry name | UBP2L_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q14157 Secondary accession number(s): B4E0U8 Q9UGL5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| 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 1 Human chromosome 1: 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with