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P22736 (NR4A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear receptor subfamily 4 group A member 1
Alternative name(s):
Early response protein NAK1
Nuclear hormone receptor NUR/77
Short name=Nur77
Orphan nuclear receptor HMR
Orphan nuclear receptor TR3
ST-59
Testicular receptor 3
Gene names
Name:NR4A1
Synonyms:GFRP1, HMR, NAK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Orphan nuclear receptor. May act concomitantly with NURR1 in regulating the expression of delayed-early genes during liver regeneration. Binds the NGFI-B response element (NBRE) 5'-AAAAGGTCA-3' By similarity. May inhibit NF-kappa-B transactivation of IL2. Ref.8

Subunit structure

Binds DNA as a monomer By similarity. Interacts with GADD45GIP1. Ref.9

Subcellular location

Nucleus.

Tissue specificity

Fetal muscle and adult liver, brain and thyroid.

Induction

By growth-stimulating agents.

Post-translational modification

Phosphorylated at Ser-351 by RPS6KA1 and RPS6KA3 in response to mitogenic or stress stimuli. Ref.10

Sequence similarities

Belongs to the nuclear hormone receptor family. NR4 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell migration involved in sprouting angiogenesis

Inferred from direct assay PubMed 18059339. Source: BHF-UCL

cellular response to vascular endothelial growth factor stimulus

Inferred from mutant phenotype PubMed 18059339. Source: BHF-UCL

endothelial cell chemotaxis

Inferred from mutant phenotype PubMed 18059339. Source: BHF-UCL

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

induction of apoptosis

Inferred from electronic annotation. Source: Compara

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Compara

nerve growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 18059339. Source: BHF-UCL

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

transcription factor complex

Inferred from electronic annotation. Source: Compara

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Compara

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Traceable author statement Ref.2. Source: ProtInc

sequence-specific DNA binding

Inferred from electronic annotation. Source: Compara

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P22736-1)

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: P22736-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MWLAKACWSIQSEM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 598598Nuclear receptor subfamily 4 group A member 1
PRO_0000053715

Regions

DNA binding264 – 33976Nuclear receptor
Zinc finger267 – 28721NR C4-type
Zinc finger303 – 32725NR C4-type
Region409 – 45951Ligand-binding Potential
Compositional bias82 – 9211Poly-Ser
Compositional bias583 – 5864Poly-Pro

Amino acid modifications

Modified residue3411Phosphoserine; by PKA By similarity
Modified residue3511Phosphoserine Ref.10 Ref.12

Natural variations

Alternative sequence11M → MWLAKACWSIQSEM in isoform 2.
VSP_043086
Natural variant261L → V.
Corresponds to variant rs1882118 [ dbSNP | Ensembl ].
VAR_061534

Experimental info

Sequence conflict2531T → I Ref.7
Sequence conflict2621G → P in AAA36763. Ref.2
Sequence conflict3701R → L in AAA36763. Ref.2

Secondary structure

................................ 598
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 41DAAEA7C25FDA22

FASTA59864,463
        10         20         30         40         50         60 
MPCIQAQYGT PAPSPGPRDH LASDPLTPEF IKPTMDLASP EAAPAAPTAL PSFSTFMDGY 

        70         80         90        100        110        120 
TGEFDTFLYQ LPGTVQPCSS ASSSASSTSS SSATSPASAS FKFEDFQVYG CYPGPLSGPV 

       130        140        150        160        170        180 
DEALSSSGSD YYGSPCSAPS PSTPSFQPPQ LSPWDGSFGH FSPSQTYEGL RAWTEQLPKA 

       190        200        210        220        230        240 
SGPPQPPAFF SFSPPTGPSP SLAQSPLKLF PSQATHQLGE GESYSMPTAF PGLAPTSPHL 

       250        260        270        280        290        300 
EGSGILDTPV TSTKARSGAP GGSEGRCAVC GDNASCQHYG VRTCEGCKGF FKRTVQKNAK 

       310        320        330        340        350        360 
YICLANKDCP VDKRRRNRCQ FCRFQKCLAV GMVKEVVRTD SLKGRRGRLP SKPKQPPDAS 

       370        380        390        400        410        420 
PANLLTSLVR AHLDSGPSTA KLDYSKFQEL VLPHFGKEDA GDVQQFYDLL SGSLEVIRKW 

       430        440        450        460        470        480 
AEKIPGFAEL SPADQDLLLE SAFLELFILR LAYRSKPGEG KLIFCSGLVL HRLQCARGFG 

       490        500        510        520        530        540 
DWIDSILAFS RSLHSLLVDV PAFACLSALV LITDRHGLQE PRRVEELQNR IASCLKEHVA 

       550        560        570        580        590 
AVAGEPQPAS CLSRLLGKLP ELRTLCTQGL QRIFYLKLED LVPPPPIIDK IFMDTLPF 

« Hide

Isoform 2 [UniParc].

Checksum: 21F3BC282AE6BE8D
Show »

FASTA61165,998

References

« Hide 'large scale' references
[1]"A human early response gene homologous to murine nur77 and rat NGFI-B, and related to the nuclear receptor superfamily."
Nakai A., Kartha S., Sakurai A., Toback F.G., Degroot L.J.
Mol. Endocrinol. 4:1438-1443(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal skeletal muscle.
[2]"Isolation and characterization of human TR3 receptor: a member of steroid receptor superfamily."
Chang C., Kokontis J., Liao S., Chang Y.
J. Steroid Biochem. 34:391-395(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Skin.
[7]"Phorbol ester, forskolin, and serum induction of a human colon nuclear hormone receptor gene related to the NUR 77/NGFI-B genes."
Bondy G.P.
Cell Growth Differ. 2:203-208(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-398 (ISOFORM 1).
Tissue: Colon adenocarcinoma.
[8]"Negative cross-talk between the human orphan nuclear receptor Nur77/NAK-1/TR3 and nuclear factor-kappaB."
Harant H., Lindley I.J.
Nucleic Acids Res. 32:5280-5290(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"CR6-interacting factor 1 interacts with orphan nuclear receptor Nur77 and inhibits its transactivation."
Park K.C., Song K.-H., Chung H.K., Kim H., Kim D.W., Song J.H., Hwang E.S., Jung H.S., Park S.-H., Bae I., Lee I.K., Choi H.-S., Shong M.
Mol. Endocrinol. 19:12-24(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GADD45GIP1.
[10]"RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation."
Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J., Sonenberg N., Blenis J.
J. Biol. Chem. 282:14056-14064(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-351.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D49728 mRNA. Translation: BAA08565.1.
L13740 mRNA. Translation: AAA36763.1.
AK297526 mRNA. Translation: BAG59929.1.
AC025259 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58222.1.
BC016147 mRNA. Translation: AAH16147.1.
IPIIPI00743108.
IPI01011914.
PIRA37251.
RefSeqNP_001189162.1. NM_001202233.1.
NP_002126.2. NM_002135.4.
NP_775180.1. NM_173157.2.
UniGeneHs.524430.
Hs.670088.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QW4X-ray2.80A/B/C/D347-598[»]
3V3EX-ray2.06A/B351-598[»]
3V3QX-ray2.22A/B351-598[»]
ProteinModelPortalP22736.
ModBaseSearch...

Protein-protein interaction databases

IntActP22736. 58 interactions.
MINTMINT-2859679.
STRING9606.ENSP00000243050.

PTM databases

PhosphoSiteP22736.

Polymorphism databases

DMDM127819.

Proteomic databases

PaxDbP22736.
PRIDEP22736.

Protocols and materials databases

DNASU3164.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000243050; ENSP00000243050; ENSG00000123358.
ENST00000360284; ENSP00000353427; ENSG00000123358.
ENST00000394824; ENSP00000378301; ENSG00000123358.
ENST00000394825; ENSP00000378302; ENSG00000123358.
ENST00000550082; ENSP00000449539; ENSG00000123358.
GeneID3164.
KEGGhsa:3164.
UCSCuc001rzs.3. human.

Organism-specific databases

CTD3164.
GeneCardsGC12P052416.
H-InvDBHIX0171621.
HGNCHGNC:7980. NR4A1.
MIM139139. gene.
neXtProtNX_P22736.
PharmGKBPA31761.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245120.
HOGENOMHOG000230925.
HOVERGENHBG052663.
InParanoidP22736.
KOK04465.
OrthoDBEOG4VMFF7.
PhylomeDBP22736.

Enzyme and pathway databases

Pathway_Interaction_DBnfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP22736.
BgeeP22736.
CleanExHS_NR4A1.
GenevestigatorP22736.
GermOnlineENSG00000123358. Homo sapiens.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR003071. Nuc_orp_HMR_rcpt.
IPR003070. Nuc_orph_rcpt.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR01285. HMRNUCRECPTR.
PR01284. NUCLEARECPTR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. Str_ncl_receptor. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP22736.
ChEMBLCHEMBL1293229.
ChiTaRSNR4A1. human.
EvolutionaryTraceP22736.
GenomeRNAi3164.
NextBio12546.
SOURCESearch...

Entry information

Entry nameNR4A1_HUMAN
AccessionPrimary (citable) accession number: P22736
Secondary accession number(s): B4DML7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: May 1, 2013
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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 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

SIMILARITY comments

Index of protein domains and families