Reviewed,
UniProtKB/Swiss-Prot P46527 (CDN1B_HUMAN)
Last modified
November 4, 2008.
Version 98.
History...
Clusters with 100%,
90%,
50% identity |
Documents (7) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cyclin-dependent kinase inhibitor 1B Alternative name(s): Cyclin-dependent kinase inhibitor p27 p27Kip1 | ||||
| Gene names |
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| 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 | 198 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Important regulator of cell cycle progrssion. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Positive regulator of cyclin D-dependent kinases such as CDK4. Regulated by phosphorylation and degradation events. |
| Subunit structure | Interacts with NUP50; the interaction leads to nuclear import and degradation of phosphorylated p27kip1. Interacts with COPS5, subunit of the COP9 signalosome complex; the interaction leads to p27KIP degradation. Interacts with SPDYA in the SPDYA/CDK2/p27kip1 complex. Interacts (Thr-198 phosphorylated-form) with 14-3-3 proteins, binds strongly YWHAQ, weakly YWHAE and YWHAH, but not YWHAB nor YWHAZ; the interaction with YWHAQ results in translocation to the cytoplasm. Interacts with AKT1, LYN and UHMK1; the interactions lead to cytoplasmic mislocation, phosphorylation of p27kip1 and inhibition of cell cycle arrest. Interacts (unphosphorylated form) with CDK2. Interacts (phosphorylated on Tyr-88 and Tyr-89) with CDK4; the interaction induces nuclear translocation. Interacts with GRB2. |
| Subcellular location | Nucleus. Cytoplasm. Note= Nuclear and cytoplasmic in quiescent cells. AKT- or RSK-mediated phosphorylation on Thr-198, binds 14-3-3, translocates to the cytoplasm and promotes cell cycle progression. Mitogen-activated UHMK1 phosphorylation on Ser-10 also results in translocation to the cytoplasm and cell cycle progression. Phosphorylation on Ser-10 facilitates nuclear export. Translocates to the nucleus on phosphorylation of Tyr-88 and Tyr-89. |
| Tissue specificity | Expressed in all tissues tested. Highest levels in skeletal muscle, lowest in liver and kidney. |
| Induction | Maximal levels in quiescence cells and early G(1). Levels decrease after mitogen stimulation as cells progress toward S-phase. |
| Domain | A peptide sequence containing only AA 28-79 retains substantial Kip1 cyclin A/CDK2 inhibitory activity. |
| Post-translational modification | Phosphorylated; phosphorylation occurs on serine, threonine and tyrosine residues. Phosphorylation on Ser-10 is the major site of phosphorylation in resting cells, takes place at the G(0)-G(1) phase and leads to protein stability. Phosphorylation on other sites is greatly enhanced by mitogens, growth factors, cMYC and in certain cancer cell lines. The phosphorylated form found in the cytoplasm is inactivate. Phosphorylation on Thr-198 is required for interaction with 14-3-3 proteins. Phosphorylation on Thr-187, by CDK2 leads to protein ubiquitination and proteasomal degradation. Tyrosine phosphorylation promotes this process. Phosphorylation by PKB/AKT1 can be suppressed by LY294002, an inhibitor of the catalytic subunit of PI3K. Phosphorylation on Tyr-88 and Tyr-89 has no effect on binding CDK2, but is required for binding CDK4. Dephosphorylated on tyrosine residues by G-CSF. Ubiquitinated; in the cytoplasm by the KPC1/KPC2 complex and, in the nucleus, by SCF/SKP2. The latter requires prior phosphorylation on Thr-187. |
| Involvement in disease | Defects in CDKN1B are the cause of multiple endocrine neoplasia type 4 (MEN4) [MIM:610755]. Multiple endocrine neoplasia (MEN) syndromes are inherited cancer syndromes of the thyroid. MEN4 is a MEN-like syndrome with a phenotypic overlap of both MEN1 and MEN2. |
| Miscellaneous | Decreased levels of p27Kip1, mainly due to proteosomal degradation, are found in various epithelial tumors originating from lung, breast, colon, ovary, esophagus, thyroid and prostate. |
| Sequence similarities | Belongs to the CDI family. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Abl1 | P00520 | 1 | EBI-519280,EBI-914519 | From a different organism. |
| CCNA2 | P20248 | 4 | EBI-519280,EBI-457097 | |
| CCNB1 | P14635 | 1 | EBI-519280,EBI-495332 | |
| CCND1 | P24385 | 2 | EBI-519280,EBI-375001 | |
| CCNE1 | P24864 | 2 | EBI-519280,EBI-519526 | |
| CCNE2 | O96020 | 1 | EBI-519280,EBI-375033 | |
| CDK2 | P24941 | 6 | EBI-519280,EBI-375096 | |
| CDK4 | P11802 | 2 | EBI-519280,EBI-295644 | |
| CDK5 | Q00535 | 2 | EBI-519280,EBI-1041567 | |
| COPS5 | Q92905 | 1 | EBI-519280,EBI-594661 | |
| KPNA3 | O00505 | 1 | EBI-519280,EBI-358297 | |
| KPNA5 | O15131 | 3 | EBI-519280,EBI-540602 | |
| LYN | P07948 | 2 | EBI-519280,EBI-79452 | |
| SRC | P12931 | 1 | EBI-519280,EBI-621482 | |
| STMN1 | P16949 | 1 | EBI-519280,EBI-445909 | |
| UCHL1 | P09936 | 1 | EBI-519280,EBI-714860 | |
| YES1 | P07947 | 1 | EBI-519280,EBI-515331 | |
| YWHAB | P31946 | 1 | EBI-519280,EBI-359815 | |
| YWHAE | P62258 | 1 | EBI-519280,EBI-356498 | |
| YWHAG | P61981 | 1 | EBI-519280,EBI-359832 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||
Molecule processing | |||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 198 | 198 | Cyclin-dependent kinase inhibitor 1B | PRO_0000190084 | |||||||||||||||||
Regions | |||||||||||||||||||||
| Motif | 153 – 169 | 17 | Nuclear localization signal Potential | ||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||
| Modified residue | 10 | 1 | Phosphoserine; by UHMK1 | ||||||||||||||||||
| Modified residue | 74 | 1 | Phosphotyrosine; by SRC | ||||||||||||||||||
| Modified residue | 88 | 1 | Phosphotyrosine; by ABL, LYN and SRC | ||||||||||||||||||
| Modified residue | 89 | 1 | Phosphotyrosine | ||||||||||||||||||
| Modified residue | 140 | 1 | Phosphoserine | ||||||||||||||||||
| Modified residue | 157 | 1 | Phosphothreonine; by PKB/AKT1 | ||||||||||||||||||
| Modified residue | 187 | 1 | Phosphothreonine; by PKB/AKT1 and CDK2 | ||||||||||||||||||
| Modified residue | 198 | 1 | Phosphothreonine; by PKB/AKT1; RPS6KA4 and RPS6KA5 | ||||||||||||||||||
Natural variations | |||||||||||||||||||||
| Natural variant | 15 | 1 | R → W: dbSNP rs2066828. | VAR_011871 | |||||||||||||||||
| Natural variant | 109 | 1 | V → G: dbSNP rs2066827. | VAR_011872 | |||||||||||||||||
Experimental info | |||||||||||||||||||||
| Mutagenesis | 10 | 1 | S → A: Loss of phosphorylation by UHMK1. No translocation to the cytoplasm. Greater cell cycle arrest | ||||||||||||||||||
| Mutagenesis | 10 | 1 | S → D: Exported to the cytoplasm. Inhibits cell cycle arrest | ||||||||||||||||||
| Mutagenesis | 10 | 1 | S → E: Increased stability in vivo and in vitro | ||||||||||||||||||
| Mutagenesis | 74 | 1 | Y → F: No change in binding CDK4. Translocates to nucleus | ||||||||||||||||||
| Mutagenesis | 88 | 1 | Y → F: Abolishes LYN-mediated phosphorylation. Reduced CDK2 phosphorylation on T-187. Greater cell cycle arrest into S-phase. No effect on binding CDK2 complexes. Reduction of CDK4 binding. No nuclear translocation. Completely abolishes CDK4 binding; when associated with F-89 | ||||||||||||||||||
| Mutagenesis | 89 | 1 | Y → F: No effect on binding CDK2 complexes. Reduction of CDK4 binding. No nuclear translocation. Completely abolishes CDK4 binding; when associated with F-88 | ||||||||||||||||||
| Mutagenesis | 157 | 1 | T → A: Greatly reduced PKB/AKT1-mediated phosphorylation. Nuclear location. Inhibits cyclin E/CDK2 cell cycle progression. No effect on binding AKT1. Completely abolishes PKB/AKT1-mediated phosphorylation and no cytoplasmic translocation; when associated with A-198 | ||||||||||||||||||
| Mutagenesis | 161 | 1 | S → A: No change in PKB/AKT1-mediated phosphorylation | ||||||||||||||||||
| Mutagenesis | 162 | 1 | T → A: No change in PKB/AKT1-mediated phosphorylation | ||||||||||||||||||
| Mutagenesis | 187 | 1 | T → A or D: No change in PKB/AKT1- nor UHMK1-mediated phosphorylation | ||||||||||||||||||
| Mutagenesis | 198 | 1 | T → A or D: Abolishes PKB/AKT1-mediated phosphorylation. 46% cytoplasmic location. Greatly reduced binding to YWHAQ. Equally reduced binding; when associated with A-10 and A-187. No nuclear import; when associated with A-157. Completely abolishes PKB/AKT1-mediated phosphorylation and no cytoplasmic translocation; when associated with A-157 | ||||||||||||||||||
| Sequence conflict | 22 | 1 | E → D in AAD14244. Ref.2 | ||||||||||||||||||
Secondary structure | |||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||
| Helix | 38 – 49 | 12 | |||||||||||||||||||
| Turn | 50 – 53 | 4 | |||||||||||||||||||
| Helix | 54 – 60 | 7 | |||||||||||||||||||
| Turn | 64 – 67 | 4 | |||||||||||||||||||
| Beta strand | 71 – 74 | 4 | |||||||||||||||||||
| Beta strand | 77 – 80 | 4 | |||||||||||||||||||
| Helix | 86 – 89 | 4 | |||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals." Polyak K., Lee M.-H., Erdjument-Bromage H., Koff A., Roberts J.M., Tempst P., Massague J. Cell 78:59-66(1994) [PubMed: 8033212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-79 AND 104-152. Tissue: Kidney. |
| [2] | "Assignment of the human p27Kip1 gene to 12p13 and its analysis in leukemias." Pietenpol J.A., Bohlander S.K., Sato Y., Papadopoulos N., Liu B., Friedman C., Trask B.J., Roberts J.M., Kinzler K.W., Rowley J.D. Cancer Res. 55:1206-1210(1995) [PubMed: 7882309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Rieder M.J., Braun A.C., Montoya M.A., Chung M.-W., Nguyen C.P., Nguyen D.A., Livingston R.J., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-15 AND GLY-109. |
| [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], VARIANT GLY-109. Tissue: Cervix. |
| [5] | "Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation." Montagnoli A., Fiore F., Eytan E., Carrano A.C., Draetta G.F., Hershko A., Pagano M. Genes Dev. 13:1181-1189(1999) [PubMed: 10323868] [Abstract] Cited for: UBIQUITINATION, PHOSPHORYLATION. |
| [6] | "Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability." Ishida N., Kitagawa M., Hatakeyama S., Nakayama K. J. Biol. Chem. 275:25146-25154(2000) [PubMed: 10831586] [Abstract] Cited for: PHOSPHORYLATION AT SER-10, FUNCTION. |
| [7] | "A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) and regulates cell cycle progression." Boehm M., Yoshimoto T., Crook M.F., Nallamshetty S., True A., Nabel G.J., Nabel E.G. EMBO J. 21:3390-3401(2002) [PubMed: 12093740] [Abstract] Cited for: INTERACTION WITH UHMK1, PHOSPHORYLATION AT SER-10, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-10 AND THR-187. |
| [8] | "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization." Fujita N., Sato S., Katayama K., Tsuruo T. J. Biol. Chem. 277:28706-28713(2002) [PubMed: 12042314] [Abstract] Cited for: PHOSPHORYLATION AT SER-10; THR-187 AND THR-198, INTERACTION WITH AKT1 AND YWHAQ, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-10; THR-157; THR-187 AND THR-198. |
| [9] | "Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer." Viglietto G., Motti M.L., Bruni P., Melillo R.M., D'Alessio A., Califano D., Vinci F., Chiappetta G., Tsichlis P., Bellacosa A., Fusco A., Santoro M. Nat. Med. 8:1136-1144(2002) [PubMed: 12244303] [Abstract] Cited for: PHOSPHORYLATION AT THR-157, SUBCELLULAR LOCATION, ASSOCIATED WITH BREAST CANCER, MUTAGENESIS OF THR-157. |
| [10] | "PKB/Akt mediates cell-cycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization." Shin I., Yakes F.M., Rojo F., Shin N.-Y., Bakin A.V., Baselga J., Arteaga C.L. Nat. Med. 8:1145-1152(2002) [PubMed: 12244301] [Abstract] Cited for: PHOSPHORYLATION AT THR-157, INTERACTION WITH AKT1, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF THR-157; SER-161 AND THR-162. |
| [11] | "Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6 kinases promotes its binding to 14-3-3 and cytoplasmic localization." Fujita N., Sato S., Tsuruo T. J. Biol. Chem. 278:49254-49260(2003) [PubMed: 14504289] [Abstract] Cited for: PHOSPHORYLATION AT SER-10 AND THR-198, INTERACTION WITH YWHAE; YWHAH; SFN; YWHAQ; RPS6KA4 AND RPS6KA5, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-157 AND THR-198. |
| [12] | "Spy1 interacts with p27Kip1 to allow G1/S progression." Porter L.A., Kong-Beltran M., Donoghue D.J. Mol. Biol. Cell 14:3664-3674(2003) [PubMed: 12972555] [Abstract] Cited for: INTERACTION WITH SPDYA. |
| [13] | "Akt-dependent T198 phosphorylation of cyclin-dependent kinase inhibitor p27kip1 in breast cancer." Motti M.L., De Marco C., Califano D., Fusco A., Viglietto G. Cell Cycle 3:1074-1080(2004) [PubMed: 15280662] [Abstract] Cited for: PHOSPHORYLATION AT THR-198, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-10; THR-157; THR-187 AND THR-198. |
| [14] | "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-10, MASS SPECTROMETRY. Tissue: Epithelium. |
| [15] | "Tyrosine phosphorylation modulates binding preference to cyclin-dependent kinases and subcellular localization of p27Kip1 in the acute promyelocytic leukemia cell line NB4." Kardinal C., Dangers M., Kardinal A., Koch A., Brandt D.T., Tamura T., Welte K. Blood 107:1133-1140(2006) [PubMed: 16195327] [Abstract] Cited for: PHOSPHORYLATION AT TYR-88 AND TYR-89, DEPHOSPHORYLATION, INTERACTION WITH GRB2; CDK2 AND CDK4, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-74; TYR-88 AND TYR-89. |
| [16] | "Germ-line mutations in p27(Kip1) cause a multiple endocrine neoplasia syndrome in rats and humans." Pellegata N.S., Quintanilla-Martinez L., Siggelkow H., Samson E., Bink K., Hoefler H., Fend F., Graw J., Atkinson M.J. Proc. Natl. Acad. Sci. U.S.A. 103:15558-15563(2006) [PubMed: 17030811] [Abstract] Cited for: ASSOCIATION WITH MEN4. |
| [17] | "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-140, MASS SPECTROMETRY. |
| [18] | "Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex." Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P. Nature 382:325-331(1996) [PubMed: 8684460] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-106 OF COMPLEX WITH CDK2 AND CG2A. |
| [19] | "Cdk-inhibitory activity and stability of p27Kip1 are directly regulated by oncogenic tyrosine kinases." Grimmler M., Wang Y., Mund T., Cilensek Z., Keidel E.-M., Waddell M.B., Jaekel H., Kullmann M., Kriwacki R.W., Hengst L. Cell 128:269-280(2007) [PubMed: 17254966] [Abstract] Cited for: STRUCTURE BY NMR OF 22-104, PHOSPHORYLATION AT TYR-88, FUNCTION, INDUCTION, INTERACTION WITH LYN, MASS SPECTROMETRY, MUTAGENESIS OF TYR-88 AND TYR-89. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| U10906 mRNA. Translation: AAA20240.1. S76988, S76986 Genomic DNA. Translation: AAD14244.1. AF480891 Genomic DNA. Translation: AAL78041.1. BC001971 mRNA. Translation: AAH01971.1. | |||||||||||||||||||||||||
| RefSeq | NP_004055.1. | ||||||||||||||||||||||||
| UniGene | Hs.238990 | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| |||||||||||||||||||||||||
| DisProt | DP00018. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| IntAct | P46527. | ||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||
| PhosphoSite | P46527. | ||||||||||||||||||||||||
Polymorphism databases | |||||||||||||||||||||||||
| NIEHS-SNPs | Search... | ||||||||||||||||||||||||
2-D gel databases | |||||||||||||||||||||||||
| SWISS-2DPAGE | P46527. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENSG00000111276. Homo sapiens. [Contig view] | ||||||||||||||||||||||||
| GeneID | 1027. | ||||||||||||||||||||||||
| KEGG | hsa:1027. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| H-InvDB | HIX0010441. | ||||||||||||||||||||||||
| HGNC | HGNC:1785. CDKN1B. | ||||||||||||||||||||||||
| HPA | CAB003691. | ||||||||||||||||||||||||
| MIM | 600778. gene. 610755. phenotype. | ||||||||||||||||||||||||
| PharmGKB | PA105. | ||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||
| GeneCards | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOGENOM | P46527. | ||||||||||||||||||||||||
| HOVERGEN | P46527. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| ArrayExpress | P46527. | ||||||||||||||||||||||||
| CleanEx | HS_CDKN1B. | ||||||||||||||||||||||||
| GermOnline | ENSG00000111276. Homo sapiens. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR003175. CDI. IPR015456. Cyclin_inhib_p27. [Graphical view] | ||||||||||||||||||||||||
| PANTHER | PTHR10265. CDI. 1 hit. PTHR10265:SF4. p27_Kip1. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF02234. CDI. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||
| LinkHub | P46527. | ||||||||||||||||||||||||
| NextBio | 4315. | ||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | CDN1B_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P46527 Secondary accession number(s): Q16307, Q9BUS6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 12 Human chromosome 12: 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 |
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

Clusters with