Reviewed,
UniProtKB/Swiss-Prot Q12802 (AKP13_HUMAN)
Last modified
June 16, 2009.
Version 74.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
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Names and origin
| Protein names | Recommended name: A-kinase anchor protein 13 Short name=AKAP 13 Alternative name(s): Protein kinase A-anchoring protein 13 Breast cancer nuclear receptor-binding auxiliary protein Human thyroid-anchoring protein 31 Guanine nucleotide exchange factor Lbc AKAP-Lbc P47 Lymphoid blast crisis oncogene Short name=LBC oncogene Non-oncogenic Rho GTPase-specific GTP exchange factor | ||||
| 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 | 2813 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Anchors cAMP-dependent protein kinase (PKA) and acts as an adapter protein to selectively couple G alpha-13 and Rho. Augments gene activation by the estrogen receptor in an element-specific and ligand-dependent manner. Activates estrogen receptor beta by a p38 MAPK-dependent pathway. Isoform 6 stimulates exchange activity on Rho proteins in vitro, but not on CDC42, Ras or Rac and may bind calcium ions. Ref.2 Ref.3 Ref.6 Ref.11 |
| Subunit structure | Binds cAMP-dependent protein kinase (PKA) and to the RII-alpha regulatory subunit of PKA. Interacts with ESR1, ESR2, THRA, PPARA, RHOA and NME2. Ref.2 Ref.6 Ref.11 Ref.5 Ref.12 |
| Subcellular location | Isoform 3: Cytoplasm. Nucleus. Ref.2 Ref.3 Ref.6 Isoform 2: Cytoplasm. Ref.2 Ref.3 Ref.6 |
| Tissue specificity | Isoform 3 and isoform 6 are found in hematopoietic cells, skeletal muscle, lung, heart, estrogen-responsive reproductive tissues, including breast ductal epithelium. Also found in testis and breast cancer cell lines. Isoform 6 is not found in brain, placenta, liver, pancreas or kidney. Isoform 7 is expressed in myeloid and lymphoid lineages, a variety of epithelial tissues and skeletal muscle. Isoform 2 is predominantly found in the heart and at lower levels in the lung, placenta, kidney, pancreas, skeletal muscle and liver. Ref.2 Ref.3 Ref.6 |
| Domain | Both the DH and PH domains are required for transforming activity. Ref.3 |
| Sequence similarities | Contains 1 DH (DBL-homology) domain. Contains 1 PH domain. Contains 1 phorbol-ester/DAG-type zinc finger. |
| Sequence caution | The sequence AAD21311.1 differs from that shown. Reason: Frameshift at positions 2614 and 2647. The sequence AAL40923.1 differs from that shown. Reason: Frameshift at positions 2614 and 2647. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| BAK1 | Q16611 | 1 | EBI-1373806,EBI-519866 | |
| TGM2 | P21980 | 3 | EBI-1373806,EBI-727668 | |
| YWHAB | P31946 | 1 | EBI-1373806,EBI-359815 |
Alternative products
| This entry describes 7 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q12802-1) 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: Q12802-2) The sequence of this isoform differs from the canonical sequence as follows: 1583-1598: SMRVLGDVVRRPPIHR → MSWCPSGVQYSAGLSADFNY | ||||||
| Isoform 3 (identifier: Q12802-3) The sequence of this isoform differs from the canonical sequence as follows: 1-1384: Missing. 1385-1387: TQA → MLY | ||||||
| Isoform 4 (identifier: Q12802-4) The sequence of this isoform differs from the canonical sequence as follows: 1581-1598: Missing. 1950-1951: Missing. | ||||||
| Isoform 5 (identifier: Q12802-5) The sequence of this isoform differs from the canonical sequence as follows: 160-179: DAGPRETLMHFAVRLGLLRL → GENLYDLQTHFKFVIFLLFF 180-2813: Missing. | ||||||
| Isoform 6 (identifier: Q12802-6) Also known as: LBC; The sequence of this isoform differs from the canonical sequence as follows: 1-1918: Missing. 1950-1951: Missing. 2336-2344: NRDEDEGIP → SGNGWRCFN 2345-2813: Missing. | ||||||
| Isoform 7 (identifier: Q12802-7) The sequence of this isoform differs from the canonical sequence as follows: 1-1918: Missing. 1950-1951: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2813 | 2813 | A-kinase anchor protein 13 | PRO_0000080963 | |||||
Regions | |||||||||
| Domain | 1994 – 2191 | 198 | DH | ||||||
| Domain | 2231 – 2333 | 103 | PH | ||||||
| Zinc finger | 1791 – 1838 | 48 | Phorbol-ester/DAG-type | ||||||
| Region | 494 – 516 | 23 | RII-binding | ||||||
| Region | 1919 – 2813 | 895 | Interaction with ESR1 | ||||||
| Coiled coil | 1758 – 1790 | 33 | Potential | ||||||
| Coiled coil | 2345 – 2381 | 37 | Potential | ||||||
| Coiled coil | 2568 – 2683 | 116 | Potential | ||||||
| Compositional bias | 1471 – 1474 | 4 | Poly-Ser | ||||||
| Compositional bias | 1534 – 1537 | 4 | Poly-Glu | ||||||
| Compositional bias | 2778 – 2790 | 13 | Poly-Lys | ||||||
Amino acid modifications | |||||||||
| Modified residue | 983 | 1 | Phosphoserine Ref.14 Ref.15 Ref.16 | ||||||
| Modified residue | 1559 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 1645 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 1647 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 1876 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 1929 | 1 | Phosphoserine Ref.16 Ref.13 | ||||||
| Modified residue | 1932 | 1 | Phosphoserine Ref.16 Ref.13 | ||||||
| Modified residue | 2398 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 2402 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 2703 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 2709 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 2728 | 1 | Phosphoserine Ref.14 Ref.16 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 1918 | 1918 | Missing in isoform 6 and isoform 7. | VSP_023484 | |||||
| Alternative sequence | 1 – 1384 | 1384 | Missing in isoform 3. | VSP_023485 | |||||
| Alternative sequence | 160 – 179 | 20 | DAGPR…GLLRL → GENLYDLQTHFKFVIFLLFF in isoform 5. | VSP_023486 | |||||
| Alternative sequence | 180 – 2813 | 2634 | Missing in isoform 5. | VSP_023487 | |||||
| Alternative sequence | 1385 – 1387 | 3 | TQA → MLY in isoform 3. | VSP_023488 | |||||
| Alternative sequence | 1581 – 1598 | 18 | Missing in isoform 4. | VSP_023489 | |||||
| Alternative sequence | 1583 – 1598 | 16 | SMRVL…PPIHR → MSWCPSGVQYSAGLSADFNY in isoform 2. | VSP_023490 | |||||
| Alternative sequence | 1950 – 1951 | 2 | Missing in isoform 4, isoform 6 and isoform 7. | VSP_023491 | |||||
| Alternative sequence | 2336 – 2344 | 9 | NRDEDEGIP → SGNGWRCFN in isoform 6. | VSP_023492 | |||||
| Alternative sequence | 2345 – 2813 | 469 | Missing in isoform 6. | VSP_023493 | |||||
| Natural variant | 452 | 1 | M → T: dbSNP rs2061821. Ref.7 | VAR_030925 | |||||
| Natural variant | 494 | 1 | W → R: dbSNP rs2061822. Ref.7 | VAR_030926 | |||||
| Natural variant | 526 | 1 | K → Q: dbSNP rs34434221. | VAR_051986 | |||||
| Natural variant | 574 | 1 | R → C: dbSNP rs2061824. Ref.5 Ref.7 | VAR_030927 | |||||
| Natural variant | 624 | 1 | G → V: dbSNP rs745191. Ref.6 | VAR_030928 | |||||
| Natural variant | 689 | 1 | E → K: dbSNP rs7177107. Ref.7 | VAR_030929 | |||||
| Natural variant | 845 | 1 | V → A: dbSNP rs4075256. Ref.7 | VAR_030930 | |||||
| Natural variant | 897 | 1 | V → M: dbSNP rs4075254. Ref.6 Ref.7 | VAR_030931 | |||||
| Natural variant | 1062 | 1 | P → A: dbSNP rs4843074. Ref.7 | VAR_030932 | |||||
| Natural variant | 1086 | 1 | D → N: dbSNP rs4843075. Ref.7 | VAR_030933 | |||||
| Natural variant | 1216 | 1 | M → T: dbSNP rs7162168. Ref.7 | VAR_030934 | |||||
| Natural variant | 1525 | 1 | S → G: dbSNP rs35079107. | VAR_051987 | |||||
| Natural variant | 2457 | 1 | G → S: dbSNP rs2241268. Ref.2 Ref.6 Ref.5 Ref.10 | VAR_030935 | |||||
| Natural variant | 2801 | 1 | A → T: dbSNP rs2614668. | VAR_030936 | |||||
Experimental info | |||||||||
| Mutagenesis | 1251 | 1 | A → P: Loss of PKA anchoring; when associated with P-1260. Ref.6 | ||||||
| Mutagenesis | 1260 | 1 | I → P: Loss of PKA anchoring; when associated with P-1251. Ref.6 | ||||||
| Mutagenesis | 1265 | 1 | A → P: Abolishes RII-binding. Ref.9 | ||||||
| Mutagenesis | 2153 | 1 | Y → F: Loss of interaction with RHOA. Ref.6 | ||||||
| Sequence conflict | 191 | 1 | G → R in AAL40923. Ref.5 | ||||||
| Sequence conflict | 354 | 1 | C → R in AAL40923. Ref.5 | ||||||
| Sequence conflict | 609 | 1 | A → V in AAL40923. Ref.5 | ||||||
| Sequence conflict | 614 | 1 | A → T in AAL40923. Ref.5 | ||||||
| Sequence conflict | 618 | 1 | S → P in AAL40923. Ref.5 | ||||||
| Sequence conflict | 619 | 1 | D → A in AAL11723. Ref.6 | ||||||
| Sequence conflict | 755 | 1 | M → S in AAA58670. Ref.9 | ||||||
| Sequence conflict | 1547 | 1 | N → H in BAD92651. Ref.10 | ||||||
| Sequence conflict | 2035 | 1 | V → D in AAD21311. Ref.2 | ||||||
| Sequence conflict | 2488 | 1 | D → G in AAD21311. Ref.2 | ||||||
| Sequence conflict | 2667 – 2668 | 2 | QL → HV in AAD21311. Ref.2 | ||||||
| Sequence conflict | 2667 – 2668 | 2 | QL → HV in BAB62913. Ref.7 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Novel human oncogene lbc detected by transfection with distinct homology regions to signal transduction products." Toksoz D., Williams D.A. Oncogene 9:621-628(1994) [PubMed: 8290273] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6). |
| [2] | "Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action." Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O., Pagliai K., Gray K., Gutkind S., Segars J. Oncogene 16:2513-2526(1998) [PubMed: 9627117] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ESR1; THRA AND PPARA, VARIANT SER-2457. Tissue: Testis. |
| [3] | "Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting." Sterpetti P., Hack A.A., Bashar M.P., Park B., Cheng S.-D., Knoll J.H.M., Urano T., Feig L.A., Toksoz D. Mol. Cell. Biol. 19:1334-1345(1999) [PubMed: 9891067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), ALTERNATIVE SPLICING (ISOFORM 6), FUNCTION, SUBCELLULAR LOCATION, DOMAIN, TISSUE SPECIFICITY. Tissue: Skeletal muscle. |
| [4] | Erratum Sterpetti P., Hack A.A., Bashar M.P., Park B., Cheng S.D., Knoll J.H., Urano T., Feig L.A., Toksoz D. Mol. Cell. Biol. 19:3930-3930(1999) |
| [5] | "Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling." Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V., Klauschenz E., Hundsrucker C., Maric K., Rosenthal W. FEBS Lett. 507:264-268(2001) [PubMed: 11696353] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RHOA, VARIANTS CYS-574 AND SER-2457. |
| [6] | "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation." Diviani D., Soderling J., Scott J.D. J. Biol. Chem. 276:44247-44257(2001) [PubMed: 11546812] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RHOA; RHOB AND RHOC, MUTAGENESIS OF ALA-1251; ILE-1260 AND TYR-2153, VARIANTS VAL-624; MET-897 AND SER-2457. |
| [7] | Miyamoto M., Ono Y. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-452; ARG-494; CYS-574; LYS-689; ALA-845; MET-897; ALA-1062; ASN-1086 AND THR-1216. Tissue: Lung. |
| [8] | "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). Tissue: Brain. |
| [9] | "Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain." Carr D.W., Hausken Z.E., Fraser I.D.C., Stofko-Hahn R.E., Scott J.D. J. Biol. Chem. 267:13376-13382(1992) [PubMed: 1618839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 754-1768, PKA AND RII BINDING, MUTAGENESIS OF ALA-1265. Tissue: Thyroid. |
| [10] | Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1486-2813 (ISOFORM 4), VARIANT SER-2457. Tissue: Brain. |
| [11] | "The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway." Driggers P.H., Segars J.H., Rubino D.M. J. Biol. Chem. 276:46792-46797(2001) [PubMed: 11579095] [Abstract] Cited for: FUNCTION, INTERACTION WITH ESR2. |
| [12] | "Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2." Iwashita S., Fujii M., Mukai H., Ono Y., Miyamoto M. Biochem. Biophys. Res. Commun. 320:1063-1068(2004) [PubMed: 15249197] [Abstract] Cited for: INTERACTION WITH NME2. |
| [13] | "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-1929 AND SER-1932, MASS SPECTROMETRY. Tissue: Epithelium. |
| [14] | "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-983 AND SER-2728, MASS SPECTROMETRY. Tissue: Epithelium. |
| [15] | "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-983, MASS SPECTROMETRY. |
| [16] | "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-983; SER-1559; SER-1645; SER-1647; SER-1876; SER-1929; SER-1932; SER-2398; SER-2402; SER-2703; SER-2709 AND SER-2728, MASS SPECTROMETRY. |
| [17] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [18] | "A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes." Newlon M.G., Roy M., Morikis D., Carr D.W., Westphal R., Scott J.D., Jennings P.A. EMBO J. 20:1651-1662(2001) [PubMed: 11285229] [Abstract] Cited for: STRUCTURE BY NMR OF 493-516. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| U03634 mRNA. Translation: AAC50065.1. AF126008 mRNA. Translation: AAD21311.1. Frameshift. AF127481 mRNA. Translation: AAD40799.1. AF387101 mRNA. Translation: AAL40923.1. Frameshift. AF406992 mRNA. Translation: AAL11723.1. AB055890 mRNA. Translation: BAB62913.1. BC050312 mRNA. Translation: AAH50312.1. M90360 mRNA. Translation: AAA58670.1. Different termination. AB209414 mRNA. Translation: BAD92651.1. | |||||||||||||
| IPI | IPI00065931. IPI00329783. IPI00375281. IPI00384381. IPI00829717. IPI00829774. IPI00829853. | ||||||||||||
| PIR | A42915. I38434. | ||||||||||||
| RefSeq | NP_006729.4. NP_009131.2. NP_658913.1. | ||||||||||||
| UniGene | Hs.459211 Hs.710656 | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q12802. 4 interactions. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q12802. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q12802. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000170776. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 11214. | ||||||||||||
| KEGG | hsa:11214. | ||||||||||||
Organism-specific databases | |||||||||||||
| GeneCards | GC15P083724. | ||||||||||||
| HGNC | HGNC:371. AKAP13. | ||||||||||||
| MIM | 604686. gene. | ||||||||||||
| PharmGKB | PA24665. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | Q12802. | ||||||||||||
| OMA | Q12802. QQLMKTN. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| Reactome | REACT_11044. Signaling by Rho GTPases. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q12802. | ||||||||||||
| Bgee | Q12802. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR002219. DAG_PE_bd. IPR000219. DH-domain. IPR001331. GDS_CDC24_CS. IPR011993. PH_type. IPR001849. Pleckstrin_homology. IPR015721. RhoGEF-like. IPR018459. RII_binding_1. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:2.30.29.30. PH_type. 1 hit. G3DSA:1.20.900.10. RhoGEF. 1 hit. | ||||||||||||
| PANTHER | PTHR22825. RhoGEF_like. 1 hit. | ||||||||||||
| Pfam | PF00130. C1_1. 1 hit. PF00169. PH. 1 hit. PF00621. RhoGEF. 1 hit. PF10522. RII_binding_1. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00109. C1. 1 hit. SM00233. PH. 1 hit. SM00325. RhoGEF. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00741. DH_1. False negative. PS50010. DH_2. 1 hit. PS50003. PH_DOMAIN. 1 hit. PS00479. ZF_DAG_PE_1. 1 hit. PS50081. ZF_DAG_PE_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 42679. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | AKP13_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q12802 Secondary accession number(s): Q14572 Q9Y5T6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 15 Human chromosome 15: 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


