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Q15796

- SMAD2_HUMAN

UniProt

Q15796 - SMAD2_HUMAN

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Protein

Mothers against decapentaplegic homolog 2

Gene

SMAD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi74 – 741ZincBy similarity
Metal bindingi149 – 1491ZincBy similarity
Metal bindingi161 – 1611ZincBy similarity
Metal bindingi166 – 1661ZincBy similarity

GO - Molecular functioni

  1. activating transcription factor binding Source: UniProtKB
  2. chromatin binding Source: Ensembl
  3. co-SMAD binding Source: BHF-UCL
  4. double-stranded DNA binding Source: UniProtKB
  5. enhancer binding Source: BHF-UCL
  6. I-SMAD binding Source: BHF-UCL
  7. metal ion binding Source: UniProtKB-KW
  8. phosphatase binding Source: UniProtKB
  9. R-SMAD binding Source: BHF-UCL
  10. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  11. SMAD binding Source: UniProtKB
  12. transcription factor binding Source: UniProtKB
  13. transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity Source: BHF-UCL
  14. transforming growth factor beta receptor binding Source: BHF-UCL
  15. type I transforming growth factor beta receptor binding Source: BHF-UCL
  16. ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  1. activin receptor signaling pathway Source: BHF-UCL
  2. anterior/posterior pattern specification Source: UniProtKB
  3. cell fate commitment Source: UniProtKB
  4. common-partner SMAD protein phosphorylation Source: MGI
  5. developmental growth Source: Ensembl
  6. embryonic cranial skeleton morphogenesis Source: Ensembl
  7. embryonic foregut morphogenesis Source: Ensembl
  8. endoderm formation Source: Ensembl
  9. gastrulation Source: BHF-UCL
  10. gene expression Source: Reactome
  11. insulin secretion Source: Ensembl
  12. intracellular signal transduction Source: UniProtKB
  13. in utero embryonic development Source: Ensembl
  14. lung development Source: Ensembl
  15. mesoderm formation Source: UniProtKB
  16. negative regulation of cell proliferation Source: Ensembl
  17. negative regulation of transcription, DNA-templated Source: BHF-UCL
  18. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
  19. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
  20. nodal signaling pathway Source: BHF-UCL
  21. organ growth Source: Ensembl
  22. palate development Source: BHF-UCL
  23. pancreas development Source: Ensembl
  24. paraxial mesoderm morphogenesis Source: UniProtKB
  25. pericardium development Source: Ensembl
  26. positive regulation of BMP signaling pathway Source: BHF-UCL
  27. positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  28. positive regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry Source: BHF-UCL
  29. positive regulation of transcription, DNA-templated Source: UniProtKB
  30. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  31. post-embryonic development Source: Ensembl
  32. primary miRNA processing Source: BHF-UCL
  33. regulation of binding Source: UniProtKB
  34. regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  35. response to cholesterol Source: BHF-UCL
  36. response to glucose Source: Ensembl
  37. signal transduction involved in regulation of gene expression Source: Ensembl
  38. SMAD protein complex assembly Source: BHF-UCL
  39. transcription, DNA-templated Source: Reactome
  40. transcription initiation from RNA polymerase II promoter Source: Reactome
  41. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  42. ureteric bud development Source: Ensembl
  43. zygotic specification of dorsal/ventral axis Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_111057. Signaling by NODAL.
REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_120850. TGF-beta receptor signaling activates SMADs.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_150238. Signaling by Activin.
REACT_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_169107. SMAD4 MH2 Domain Mutants in Cancer.
REACT_169165. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_169263. TGFBR1 KD Mutants in Cancer.
REACT_200812. Transcriptional regulation of pluripotent stem cells.
SignaLinkiQ15796.

Names & Taxonomyi

Protein namesi
Recommended name:
Mothers against decapentaplegic homolog 2
Short name:
MAD homolog 2
Short name:
Mothers against DPP homolog 2
Alternative name(s):
JV18-1
Mad-related protein 2
Short name:
hMAD-2
SMAD family member 2
Short name:
SMAD 2
Short name:
Smad2
Short name:
hSMAD2
Gene namesi
Name:SMAD2
Synonyms:MADH2, MADR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:6768. SMAD2.

Subcellular locationi

Cytoplasm. Nucleus
Note: Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4. On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1.

GO - Cellular componenti

  1. activin responsive factor complex Source: BHF-UCL
  2. cytoplasm Source: BHF-UCL
  3. cytosol Source: Reactome
  4. nuclear chromatin Source: BHF-UCL
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProtKB
  7. SMAD2-SMAD3 protein complex Source: BHF-UCL
  8. SMAD protein complex Source: UniProtKB
  9. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191K → R: Loss of acetylation. 1 Publication
Mutagenesisi20 – 201K → R: No effect on acetylation. 1 Publication
Mutagenesisi221 – 2255Missing: Loss of binding to SMURF2. 1 Publication
Mutagenesisi368 – 3681W → A: Loss of interaction with PMEPA1. 1 Publication
Mutagenesisi381 – 3811N → S: Loss of binding to SARA. 1 Publication
Mutagenesisi398 – 3981V → R: Increased binding to PPM1A. 1 Publication
Mutagenesisi464 – 4641S → A: Loss of phosphorylation by TGFBR1; when associated with A-465 and A-467. 1 Publication
Mutagenesisi465 – 4673SMS → AMA: Binds RANBP3. 1 Publication
Mutagenesisi465 – 4673SMS → DMD: Greatly reduced RANBP2 binding. 1 Publication
Mutagenesisi465 – 4651S → A: No change in binding to PPM1A. Loss of phosphorylation by TGFBR1; when associated with A-464 and A-467. 2 Publications
Mutagenesisi465 – 4651S → D: No change in binding to PPM1A. 2 Publications
Mutagenesisi467 – 4671S → A: No change in binding to PPM1A. Loss of phosphorylation by TGFBR1; when associated with A-464 and A-465. 2 Publications
Mutagenesisi467 – 4671S → D: No change in binding to PPM1A. 2 Publications

Organism-specific databases

PharmGKBiPA134959722.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 467466Mothers against decapentaplegic homolog 2PRO_0000090852Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine5 Publications
Modified residuei8 – 81Phosphothreonine; by MAPK33 Publications
Modified residuei19 – 191N6-acetyllysine1 Publication
Modified residuei220 – 2201Phosphothreonine1 Publication
Modified residuei240 – 2401Phosphoserine; by CAMK21 PublicationPROSITE-ProRule annotation
Modified residuei245 – 2451Phosphoserine1 Publication
Modified residuei250 – 2501Phosphoserine1 Publication
Modified residuei255 – 2551Phosphoserine1 Publication
Modified residuei458 – 4581Phosphoserine2 PublicationsPROSITE-ProRule annotation
Modified residuei460 – 4601Phosphoserine1 PublicationPROSITE-ProRule annotation
Modified residuei464 – 4641Phosphoserine1 PublicationPROSITE-ProRule annotation
Modified residuei465 – 4651Phosphoserine; by TGFBR14 PublicationsPROSITE-ProRule annotation
Modified residuei467 – 4671Phosphoserine; by TGFBR14 PublicationsPROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated on one or several of Thr-220, Ser-245, Ser-250, and Ser-255. In response to TGF-beta, phosphorylated on Ser-465/467 by TGF-beta and activin type 1 receptor kinases. TGF-beta-induced Ser-465/467 phosphorylation declines progressively in a SETD8-dependent manner. Able to interact with SMURF2 when phosphorylated on Ser-465/467, recruiting other proteins, such as SNON, for degradation. In response to decorin, the naturally occurring inhibitor of TGF-beta signaling, phosphorylated on Ser-240 by CaMK2. Phosphorylated by MAPK3 upon EGF stimulation; which increases transcriptional activity and stability, and is blocked by calmodulin. Phosphorylated by PDPK1.11 Publications
In response to TGF-beta, ubiquitinated by NEDD4L; which promotes its degradation (By similarity). Monoubiquitinated, leading to prevent DNA-binding. Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes.By similarity1 Publication
Acetylated on Lys-19 by coactivators in response to TGF-beta signaling, which increases transcriptional activity. Isoform short: Acetylation increases DNA binding activity in vitro and enhances its association with target promoters in vivo. Acetylation in the nucleus by EP300 is enhanced by TGF-beta.7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15796.
PaxDbiQ15796.
PRIDEiQ15796.

PTM databases

PhosphoSiteiQ15796.

Expressioni

Tissue specificityi

Expressed at high levels in skeletal muscle, endothelial cells, heart and placenta.1 Publication

Gene expression databases

BgeeiQ15796.
CleanExiHS_SMAD2.
ExpressionAtlasiQ15796. baseline and differential.
GenevestigatoriQ15796.

Organism-specific databases

HPAiCAB025507.

Interactioni

Subunit structurei

Momomer; the absence of TGF-beta. Heterodimer; in the presence of TGF-beta. Forms a heterodimer with co-SMAD, SMAD4, in the nucleus to form the transactivation complex SMAD2/SMAD4. Interacts with AIP1, HGS, PML and WWP1 (By similarity). Interacts with NEDD4L in response to TGF-beta (By similarity). Found in a complex with SMAD3 and TRIM33 upon addition of TGF-beta. Interacts with ACVR1B, SMAD3 and TRIM33. Interacts (via the MH2 domain) with ZFYVE9; may form trimers with the SMAD4 co-SMAD. Interacts with FOXH1, homeobox protein TGIF, PEBP2-alpha subunit, CREB-binding protein (CBP), EP300, SKI and SNW1. Interacts with SNON; when phosphorylated at Ser-465/467. Interacts with SKOR1 and SKOR2. Interacts with PRDM16. Interacts (via MH2 domain) with LEMD3. Interacts with RBPMS. Interacts with WWP1. Interacts (dephosphorylated form, via the MH1 and MH2 domains) with RANBP3 (via its C-terminal R domain); the interaction results in the export of dephosphorylated SMAD3 out of the nucleus and termination of the TGF-beta signaling. Interacts with PDPK1 (via PH domain). Interacts with DAB2; the interactions are enhanced upon TGF-beta stimulation. Interacts with USP15. Interacts with PPP5C. Interacts with ZNF580. Interacts with LDLRAD4 (via the SMAD interaction motif). Interacts (via MH2 domain) with PMEPA1 (via the SMAD interaction motif).By similarity26 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANK3Q129552EBI-1040141,EBI-2691178
CHGBP050602EBI-1040141,EBI-712619
DAB2P980824EBI-1040141,EBI-1171238
DOCK9Q9BZ293EBI-1040141,EBI-2695893
MTMR4Q9NYA43EBI-1040141,EBI-1052346
NEFMP071973EBI-1040141,EBI-1105035
OLIG1Q8TAK62EBI-1040141,EBI-3867416
PPM1AP358132EBI-1040141,EBI-989143
RANBP3Q9H6Z42EBI-1040141,EBI-992681
RHOAP615862EBI-1040141,EBI-446668
SMAD3P840222EBI-1040141,EBI-347161
SMAD4Q1348518EBI-1040141,EBI-347263
SMURF2Q9HAU45EBI-1040141,EBI-396727
SNW1Q135733EBI-1040141,EBI-632715
TP53P046374EBI-1040141,EBI-366083
TP63Q9H3D43EBI-1040141,EBI-2337775
TRIM33Q9UPN96EBI-1040141,EBI-2214398
WWP2O003084EBI-1040141,EBI-743923
ZFRQ96KR12EBI-1040141,EBI-2513582
ZFYVE9O954052EBI-1040141,EBI-296817

Protein-protein interaction databases

BioGridi110262. 257 interactions.
DIPiDIP-29716N.
IntActiQ15796. 207 interactions.
MINTiMINT-5006109.
STRINGi9606.ENSP00000262160.

Structurei

Secondary structure

1
467
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi264 – 2674Combined sources
Beta strandi274 – 2818Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi294 – 3029Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi310 – 3123Combined sources
Helixi313 – 3153Combined sources
Helixi323 – 3297Combined sources
Turni330 – 3345Combined sources
Beta strandi336 – 3416Combined sources
Beta strandi344 – 3496Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi355 – 3584Combined sources
Helixi360 – 3656Combined sources
Beta strandi374 – 3763Combined sources
Beta strandi381 – 3866Combined sources
Helixi387 – 39711Combined sources
Helixi398 – 4003Combined sources
Helixi402 – 4065Combined sources
Helixi407 – 4126Combined sources
Beta strandi413 – 4197Combined sources
Beta strandi423 – 4275Combined sources
Helixi431 – 4333Combined sources
Beta strandi434 – 4429Combined sources
Helixi443 – 45311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEVX-ray2.20A/C261-456[»]
1KHXX-ray1.80A241-467[»]
1U7VX-ray2.70A/C270-467[»]
2LB3NMR-B217-224[»]
ProteinModelPortaliQ15796.
SMRiQ15796. Positions 7-172, 265-467.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15796.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 176167MH1PROSITE-ProRule annotationAdd
BLAST
Domaini274 – 467194MH2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi221 – 2255PY-motif

Sequence similaritiesi

Belongs to the dwarfin/SMAD family.Curated
Contains 1 MH1 (MAD homology 1) domain.PROSITE-ProRule annotation
Contains 1 MH2 (MAD homology 2) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG320700.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000286018.
HOVERGENiHBG053353.
InParanoidiQ15796.
KOiK04500.
OMAiMNQSMDT.
OrthoDBiEOG7W1540.
PhylomeDBiQ15796.
TreeFamiTF314923.

Family and domain databases

Gene3Di2.60.200.10. 1 hit.
3.90.520.10. 1 hit.
InterProiIPR013790. Dwarfin.
IPR003619. MAD_homology1_Dwarfin-type.
IPR013019. MAD_homology_MH1.
IPR017855. SMAD_dom-like.
IPR001132. SMAD_dom_Dwarfin-type.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR13703. PTHR13703. 1 hit.
PfamiPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTiSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 2 hits.
PROSITEiPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: Q15796-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK
60 70 80 90 100
KLKKTGRLDE LEKAITTQNC NTKCVTIPST CSEIWGLSTP NTIDQWDTTG
110 120 130 140 150
LYSFSEQTRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELKAIENCE
160 170 180 190 200
YAFNLKKDEV CVNPYHYQRV ETPVLPPVLV PRHTEILTEL PPLDDYTHSI
210 220 230 240 250
PENTNFPAGI EPQSNYIPET PPPGYISEDG ETSDQQLNQS MDTGSPAELS
260 270 280 290 300
PTTLSPVNHS LDLQPVTYSE PAFWCSIAYY ELNQRVGETF HASQPSLTVD
310 320 330 340 350
GFTDPSNSER FCLGLLSNVN RNATVEMTRR HIGRGVRLYY IGGEVFAECL
360 370 380 390 400
SDSAIFVQSP NCNQRYGWHP ATVCKIPPGC NLKIFNNQEF AALLAQSVNQ
410 420 430 440 450
GFEAVYQLTR MCTIRMSFVK GWGAEYRRQT VTSTPCWIEL HLNGPLQWLD
460
KVLTQMGSPS VRCSSMS
Length:467
Mass (Da):52,306
Last modified:November 1, 1996 - v1
Checksum:i95406DB5FC0AA4C9
GO
Isoform Short (identifier: Q15796-2) [UniParc]FASTAAdd to Basket

Also known as: Smad2Deltaexon3

The sequence of this isoform differs from the canonical sequence as follows:
     79-108: Missing.

Show »
Length:437
Mass (Da):48,956
Checksum:i0E2FF38B009D2F9E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti133 – 1331R → C in a colorectal carcinoma sample. 1 Publication
VAR_011375
Natural varianti300 – 3001D → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036473
Natural varianti344 – 35815Missing in a colorectal carcinoma sample. 1 Publication
VAR_011376Add
BLAST
Natural varianti440 – 4401L → R in a colorectal carcinoma sample. 1 Publication
VAR_011377
Natural varianti445 – 4451P → H in a colorectal carcinoma sample. 1 Publication
VAR_011378
Natural varianti450 – 4501D → E in a colorectal carcinoma sample. 1 Publication
VAR_011379

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei79 – 10830Missing in isoform Short. CuratedVSP_006178Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59911 mRNA. Translation: AAC50789.1.
U68018 mRNA. Translation: AAB17087.1.
U65019 mRNA. Translation: AAB17054.1.
AF027964 mRNA. Translation: AAC51918.1.
U78733
, U78727, U78728, U78729, U78730, U78731, U78732 Genomic DNA. Translation: AAC39657.1.
BC014840 mRNA. Translation: AAH14840.1.
BC025699 mRNA. Translation: AAH25699.1.
CCDSiCCDS11934.1. [Q15796-1]
PIRiS71797.
RefSeqiNP_001003652.1. NM_001003652.3. [Q15796-1]
NP_005892.1. NM_005901.5. [Q15796-1]
XP_005258316.1. XM_005258259.1. [Q15796-1]
XP_006722514.1. XM_006722451.1. [Q15796-1]
UniGeneiHs.12253.
Hs.705764.
Hs.741342.

Genome annotation databases

EnsembliENST00000262160; ENSP00000262160; ENSG00000175387. [Q15796-1]
ENST00000356825; ENSP00000349282; ENSG00000175387. [Q15796-2]
ENST00000402690; ENSP00000384449; ENSG00000175387. [Q15796-1]
ENST00000586040; ENSP00000466193; ENSG00000175387. [Q15796-2]
GeneIDi4087.
KEGGihsa:4087.
UCSCiuc002lcy.4. human. [Q15796-1]
uc010xdc.3. human. [Q15796-2]

Polymorphism databases

DMDMi13633914.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59911 mRNA. Translation: AAC50789.1 .
U68018 mRNA. Translation: AAB17087.1 .
U65019 mRNA. Translation: AAB17054.1 .
AF027964 mRNA. Translation: AAC51918.1 .
U78733
, U78727 , U78728 , U78729 , U78730 , U78731 , U78732 Genomic DNA. Translation: AAC39657.1 .
BC014840 mRNA. Translation: AAH14840.1 .
BC025699 mRNA. Translation: AAH25699.1 .
CCDSi CCDS11934.1. [Q15796-1 ]
PIRi S71797.
RefSeqi NP_001003652.1. NM_001003652.3. [Q15796-1 ]
NP_005892.1. NM_005901.5. [Q15796-1 ]
XP_005258316.1. XM_005258259.1. [Q15796-1 ]
XP_006722514.1. XM_006722451.1. [Q15796-1 ]
UniGenei Hs.12253.
Hs.705764.
Hs.741342.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DEV X-ray 2.20 A/C 261-456 [» ]
1KHX X-ray 1.80 A 241-467 [» ]
1U7V X-ray 2.70 A/C 270-467 [» ]
2LB3 NMR - B 217-224 [» ]
ProteinModelPortali Q15796.
SMRi Q15796. Positions 7-172, 265-467.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110262. 257 interactions.
DIPi DIP-29716N.
IntActi Q15796. 207 interactions.
MINTi MINT-5006109.
STRINGi 9606.ENSP00000262160.

Chemistry

ChEMBLi CHEMBL2396512.

PTM databases

PhosphoSitei Q15796.

Polymorphism databases

DMDMi 13633914.

Proteomic databases

MaxQBi Q15796.
PaxDbi Q15796.
PRIDEi Q15796.

Protocols and materials databases

DNASUi 4087.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262160 ; ENSP00000262160 ; ENSG00000175387 . [Q15796-1 ]
ENST00000356825 ; ENSP00000349282 ; ENSG00000175387 . [Q15796-2 ]
ENST00000402690 ; ENSP00000384449 ; ENSG00000175387 . [Q15796-1 ]
ENST00000586040 ; ENSP00000466193 ; ENSG00000175387 . [Q15796-2 ]
GeneIDi 4087.
KEGGi hsa:4087.
UCSCi uc002lcy.4. human. [Q15796-1 ]
uc010xdc.3. human. [Q15796-2 ]

Organism-specific databases

CTDi 4087.
GeneCardsi GC18M045357.
HGNCi HGNC:6768. SMAD2.
HPAi CAB025507.
MIMi 601366. gene.
neXtProti NX_Q15796.
PharmGKBi PA134959722.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG320700.
GeneTreei ENSGT00760000119091.
HOGENOMi HOG000286018.
HOVERGENi HBG053353.
InParanoidi Q15796.
KOi K04500.
OMAi MNQSMDT.
OrthoDBi EOG7W1540.
PhylomeDBi Q15796.
TreeFami TF314923.

Enzyme and pathway databases

Reactomei REACT_111057. Signaling by NODAL.
REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_120850. TGF-beta receptor signaling activates SMADs.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_150238. Signaling by Activin.
REACT_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_169107. SMAD4 MH2 Domain Mutants in Cancer.
REACT_169165. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_169263. TGFBR1 KD Mutants in Cancer.
REACT_200812. Transcriptional regulation of pluripotent stem cells.
SignaLinki Q15796.

Miscellaneous databases

ChiTaRSi SMAD2. human.
EvolutionaryTracei Q15796.
GeneWikii Mothers_against_decapentaplegic_homolog_2.
GenomeRNAii 4087.
NextBioi 16020.
PROi Q15796.
SOURCEi Search...

Gene expression databases

Bgeei Q15796.
CleanExi HS_SMAD2.
ExpressionAtlasi Q15796. baseline and differential.
Genevestigatori Q15796.

Family and domain databases

Gene3Di 2.60.200.10. 1 hit.
3.90.520.10. 1 hit.
InterProi IPR013790. Dwarfin.
IPR003619. MAD_homology1_Dwarfin-type.
IPR013019. MAD_homology_MH1.
IPR017855. SMAD_dom-like.
IPR001132. SMAD_dom_Dwarfin-type.
IPR008984. SMAD_FHA_domain.
[Graphical view ]
PANTHERi PTHR13703. PTHR13703. 1 hit.
Pfami PF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view ]
SMARTi SM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 2 hits.
PROSITEi PS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT 344-GLU--GLN-358 DEL.
  2. "Receptor-associated Mad homologues synergize as effectors of the TGF-beta response."
    Zhang Y., Feng X.-H., Wu R.-Y., Derynck R.
    Nature 383:168-172(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    Tissue: Placenta.
  3. "MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma."
    Eppert K., Scherer S.W., Ozcelik H., Pirone R., Hoodless P., Kim H., Tsui L.-C., Bapat B., Gallinger S., Andrulis I.L., Thomsen G.H., Wrana J.L., Attisano L.
    Cell 86:543-552(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PHOSPHORYLATION BY TGFBR1, VARIANTS CYS-133; ARG-440; HIS-445 AND GLU-450.
    Tissue: Kidney.
  4. "Dual role of the Smad4/DPC4 tumor suppressor in TGFbeta-inducible transcriptional complexes."
    Liu F., Pouponnot C., Massague J.
    Genes Dev. 11:3157-3167(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  5. "Characterization of the MADH2/Smad2 gene, a human Mad homolog responsible for the transforming growth factor-beta and activin signal transduction pathway."
    Takenoshita S., Mogi A., Nagashima M., Yang K., Yagi K., Hanyu A., Nagamachi Y., Miyazono K., Hagiwara K.
    Genomics 48:1-11(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
  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 LONG).
    Tissue: Kidney, Pancreas and Spleen.
  7. Bienvenut W.V., von Kriegsheim A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14 AND 170-182, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Chronic myeloid leukemia cell.
  8. "MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling."
    Macias-Silva M., Abdollah S., Hoodless P.A., Pirone R., Attisano L., Wrana J.L.
    Cell 87:1215-1224(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFBR1, PHOSPHORYLATION AT SER-464; SER-465 AND SER-467, MUTAGENESIS OF SER-464; SER-465 AND SER-467.
  9. "SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor."
    Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.
    Cell 95:779-791(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZFYVE9, SUBCELLULAR LOCATION.
  10. "Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors."
    Kawabata M., Inoue H., Hanyu A., Imamura T., Miyazono K.
    EMBO J. 17:4056-4065(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  11. "Alternatively spliced variant of Smad2 lacking exon 3. Comparison with wild-type Smad2 and Smad3."
    Yagi K., Goto D., Hamamoto T., Takenoshita S., Kato M., Miyazono K.
    J. Biol. Chem. 274:703-709(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS LONG AND SHORT).
  12. "The TGF-beta family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase."
    Kretzschmar M., Liu F., Hata A., Doody J., Massague J.
    Genes Dev. 11:984-995(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-465 AND SER-467.
  13. "TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling."
    Abdollah S., Macias-Silva M., Tsukazaki T., Hayashi H., Attisano L., Wrana J.L.
    J. Biol. Chem. 272:27678-27685(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-465 AND SER-467 BY TGFBR1.
  14. "Characterization of human FAST-1, a TGF beta and activin signal transducer."
    Zhou S., Zawel L., Lengauer C., Kinzler K.W., Vogelstein B.
    Mol. Cell 2:121-127(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FOXH1.
    Tissue: Colon adenocarcinoma.
  15. "Roles of pathway-specific and inhibitory Smads in activin receptor signaling."
    Lebrun J.J., Takabe K., Chen Y., Vale W.
    Mol. Endocrinol. 13:15-23(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACVR1B, FUNCTION.
  16. "The adaptor molecule Disabled-2 links the transforming growth factor beta receptors to the Smad pathway."
    Hocevar B.A., Smine A., Xu X.X., Howe P.H.
    EMBO J. 20:2789-2801(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2.
  17. "Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription."
    Leong G.M., Subramaniam N., Figueroa J., Flanagan J.L., Hayman M.J., Eisman J.A., Kouzmenko A.P.
    J. Biol. Chem. 276:18243-18248(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNW1.
  18. "TGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation."
    Bonni S., Wang H.R., Causing C.G., Kavsak P., Stroschein S.L., Luo K., Wrana J.L.
    Nat. Cell Biol. 3:587-595(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMURF2, MUTAGENESIS OF 221-PRO--TYR-225.
  19. "Decorin suppresses transforming growth factor-beta-induced expression of plasminogen activator inhibitor-1 in human mesangial cells through a mechanism that involves Ca2+-dependent phosphorylation of Smad2 at serine-240."
    Abdel-Wahab N., Wicks S.J., Mason R.M., Chantry A.
    Biochem. J. 362:643-649(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-240.
  20. "Modulation of Smad2-mediated signaling by extracellular signal-regulated kinase."
    Funaba M., Zimmerman C.M., Mathews L.S.
    J. Biol. Chem. 277:41361-41368(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-8; THR-220; SER-245; SER-250 AND SER-255.
  21. "MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling."
    Lin F., Morrison J.M., Wu W., Worman H.J.
    Hum. Mol. Genet. 14:437-445(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LEMD3.
  22. "The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines."
    Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S., Luo K.
    J. Biol. Chem. 280:15992-16001(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LEMD3.
  23. "Cloning and functional characterization of a new Ski homolog, Fussel-18, specifically expressed in neuronal tissues."
    Arndt S., Poser I., Schubert T., Moser M., Bosserhoff A.-K.
    Lab. Invest. 85:1330-1341(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKOR2.
  24. Cited for: INTERACTION WITH PPM1A, DEPHOSPHORYLATION, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-398; SER-465 AND SER-467.
  25. "Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of the TGFbeta pathway."
    He W., Dorn D.C., Erdjument-Bromage H., Tempst P., Moore M.A., Massague J.
    Cell 125:929-941(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH SMAD3 AND TRIM33, INTERACTION WITH TRIM33.
  26. "The DNA binding activities of Smad2 and Smad3 are regulated by coactivator-mediated acetylation."
    Simonsson M., Kanduri M., Gronroos E., Heldin C.H., Ericsson J.
    J. Biol. Chem. 281:39870-39880(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-19, MUTAGENESIS OF LYS-19 AND LYS-20.
  27. "Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS."
    Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H., Ye Q.
    Nucleic Acids Res. 34:6314-6326(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBPMS.
  28. "3-Phosphoinositide-dependent PDK1 negatively regulates transforming growth factor-beta-induced signaling in a kinase-dependent manner through physical interaction with Smad proteins."
    Seong H.A., Jung H., Kim K.T., Ha H.
    J. Biol. Chem. 282:12272-12289(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY PDPK1, INTERACTION WITH PDPK1.
  29. "Fussel-15, a novel Ski/Sno homolog protein, antagonizes BMP signaling."
    Arndt S., Poser I., Moser M., Bosserhoff A.-K.
    Mol. Cell. Neurosci. 34:603-611(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKOR1.
  30. "Smad3 is acetylated by p300/CBP to regulate its transactivation activity."
    Inoue Y., Itoh Y., Abe K., Okamoto T., Daitoku H., Fukamizu A., Onozaki K., Hayashi H.
    Oncogene 26:500-508(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION, FUNCTION.
  31. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  32. "TAZ controls Smad nucleocytoplasmic shuttling and regulates human embryonic stem-cell self-renewal."
    Varelas X., Sakuma R., Samavarchi-Tehrani P., Peerani R., Rao B.M., Dembowy J., Yaffe M.B., Zandstra P.W., Wrana J.L.
    Nat. Cell Biol. 10:837-848(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WWTR1.
  33. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  34. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling."
    Dai F., Lin X., Chang C., Feng X.H.
    Dev. Cell 16:345-357(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP3, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF 465-SER--SER-467.
  36. Cited for: INTERACTION WITH PRDM16.
  37. "TMEPAI, a transmembrane TGF-beta-inducible protein, sequesters Smad proteins from active participation in TGF-beta signaling."
    Watanabe Y., Itoh S., Goto T., Ohnishi E., Inamitsu M., Itoh F., Satoh K., Wiercinska E., Yang W., Shi L., Tanaka A., Nakano N., Mommaas A.M., Shibuya H., Ten Dijke P., Kato M.
    Mol. Cell 37:123-134(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PMEPA1, MUTAGENESIS OF TRP-368.
  38. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-458 AND SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. "ZNF580, a novel C2H2 zinc-finger transcription factor, interacts with the TGF-beta signal molecule Smad2."
    Luo Y., Hu W., Xu R., Hou B., Zhang L., Zhang W.
    Cell Biol. Int. 35:1153-1157(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF580, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  41. Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP15, DNA-BINDING, INTERACTION WITH USP15.
  42. "Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway."
    Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.
    Cell. Signal. 24:1999-2006(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP5C, SUBCELLULAR LOCATION.
  43. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  44. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  45. "CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration."
    Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.
    Mol. Cell 49:1147-1158(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-465 AND SER-467.
  46. Cited for: INTERACTION WITH LDLRAD4.
  47. Cited for: REVIEW.
  48. "Remarkable versatility of Smad proteins in the nucleus of transforming growth factor-beta activated cells."
    Verschueren K., Huylebroeck D.
    Cytokine Growth Factor Rev. 10:187-199(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  49. Cited for: REVIEW.
  50. Cited for: REVIEW.
  51. "Structural basis of Smad2 recognition by the Smad anchor for receptor activation."
    Wu G., Chen Y.-G., Ozdamar B., Gyuricza C.A., Chong P.A., Wrana J.L., Massague J., Shi Y.
    Science 287:92-97(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 261-456 IN COMPLEX WITH ZFYVE9, INTERACTION WITH SARA, MUTAGENESIS OF ASN-381.
  52. "Structural basis of heteromeric smad protein assembly in TGF-beta signaling."
    Chacko B.M., Qin B.Y., Tiwari A., Shi G., Lam S., Hayward L.J., De Caestecker M., Lin K.
    Mol. Cell 15:813-823(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 270-466 IN COMPLEX WITH SMAD4, SUBUNIT.
  53. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-300.

Entry informationi

Entry nameiSMAD2_HUMAN
AccessioniPrimary (citable) accession number: Q15796
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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