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Protein

Mothers against decapentaplegic homolog 1

Gene

SMAD1

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

Functioni

Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64ZincBy similarity1
Metal bindingi109ZincBy similarity1
Metal bindingi121ZincBy similarity1
Metal bindingi126ZincBy similarity1

GO - Molecular functioni

  • co-SMAD binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • I-SMAD binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • primary miRNA binding Source: Ensembl
  • protein kinase binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  • signal transducer activity, downstream of receptor Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription factor activity, sequence-specific DNA binding Source: BHF-UCL
  • transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170365-MONOMER.
ReactomeiR-HSA-201451. Signaling by BMP.
R-HSA-5689880. Ub-specific processing proteases.
SignaLinkiQ15797.
SIGNORiQ15797.

Names & Taxonomyi

Protein namesi
Recommended name:
Mothers against decapentaplegic homolog 1
Short name:
MAD homolog 1
Short name:
Mothers against DPP homolog 1
Alternative name(s):
JV4-1
Mad-related protein 1
SMAD family member 1
Short name:
SMAD 1
Short name:
Smad1
Short name:
hSMAD1
Transforming growth factor-beta-signaling protein 1
Short name:
BSP-1
Gene namesi
Name:SMAD1
Synonyms:BSP1, MADH1, MADR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:6767. SMAD1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • integral component of membrane Source: UniProtKB
  • intracellular Source: UniProtKB
  • nuclear inner membrane Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein complex Source: MGI
  • SMAD protein complex Source: BHF-UCL
  • transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

SMAD1 variants may be associated with susceptibility to pulmonary hypertension, a disorder characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure, and death. The disease can occur from infancy throughout life and it has a mean age at onset of 36 years. Penetrance is reduced. Although familial pulmonary hypertension is rare, cases secondary to known etiologies are more common and include those associated with the appetite-suppressant drugs.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi297D → H: Reduced trimerization. 1 Publication1
Mutagenesisi317V → D: Reduced trimerization. 1 Publication1
Mutagenesisi373K → S: Reduced trimerization. 1 Publication1
Mutagenesisi418K → S: Reduced trimerization. 1 Publication1
Mutagenesisi419G → S: Loss of phosphorylation. 1 Publication1
Mutagenesisi424Y → F: Reduced trimerization. 1 Publication1
Mutagenesisi426R → S: Reduced trimerization. 1 Publication1
Mutagenesisi448D → H: Reduced trimerization. 1 Publication1

Organism-specific databases

DisGeNETi4086.
MalaCardsiSMAD1.
OpenTargetsiENSG00000170365.
PharmGKBiPA30524.

Polymorphism and mutation databases

BioMutaiSMAD1.
DMDMi13633915.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000908471 – 465Mothers against decapentaplegic homolog 1Add BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei322Phosphothreonine; by MINK1, TNIK and MAP4K41 Publication1
Modified residuei463PhosphoserinePROSITE-ProRule annotation2 Publications1
Modified residuei465PhosphoserinePROSITE-ProRule annotation2 Publications1

Post-translational modificationi

Phosphorylation of the C-terminal SVS motif by BMP type 1 receptor kinase activates SMAD1 by promoting dissociation from the receptor and trimerization with SMAD4.3 Publications
Ubiquitinated by SMAD-specific E3 ubiquitin ligase SMURF1, leading to its degradation. Monoubiquitinated, leading to prevent DNA-binding. Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ15797.
MaxQBiQ15797.
PaxDbiQ15797.
PeptideAtlasiQ15797.
PRIDEiQ15797.

PTM databases

iPTMnetiQ15797.
PhosphoSitePlusiQ15797.

Expressioni

Tissue specificityi

Ubiquitous. Highest expression seen in the heart and skeletal muscle.

Gene expression databases

BgeeiENSG00000170365.
CleanExiHS_SMAD1.
ExpressionAtlasiQ15797. baseline and differential.
GenevisibleiQ15797. HS.

Organism-specific databases

HPAiCAB005389.
CAB069411.

Interactioni

Subunit structurei

Found in a complex with SMAD4 and YY1. Interacts with HGS, NANOG and ZCCHC12 (By similarity). Upon C-terminus phosphorylation: forms trimers with another SMAD1 and the co-SMAD SMAD4. Interacts with PEBP2-alpha subunit, CREB-binding protein (CBP), p300, SMURF1, SMURF2, USP15 and HOXC8. Associates with ZNF423 or ZNF521 in response to BMP2 leading to activate transcription of BMP target genes. Interacts with SKOR1. Interacts (via MH2 domain) with LEMD3. Binding to LEMD3 results in at least a partial reduction of receptor-mediated phosphorylation. Forms a ternary complex with PSMB4 and OAZ1 before PSMB4 is incorporated into the 20S proteasome. Found in a macromolecular complex with FAM83G. Interacts (via MH2 domain) with FAM83G (via MH2 domain); in a SMAD4-independent manner. Interacts with ZC3H3 (By similarity). Interacts with TMEM119 (By similarity). Interacts (via MH1 and MH2 domains) with ZNF8 (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-1567153,EBI-1567153
ARP102756EBI-1567153,EBI-608057
GSK3BP498412EBI-1567153,EBI-373586
LEMD3Q9Y2U83EBI-1567153,EBI-2561428
SMAD4Q134859EBI-1567153,EBI-347263
SMAD6O435414EBI-1567153,EBI-976374
SMURF1Q9HCE72EBI-1567153,EBI-976466
SMURF1Q9HCE7-22EBI-1567153,EBI-9845742
SMURF2Q9HAU43EBI-1567153,EBI-396727
UCHL3P153742EBI-1567153,EBI-954554
YAP1P469373EBI-1567153,EBI-1044059

GO - Molecular functioni

  • co-SMAD binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • I-SMAD binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110261. 119 interactors.
DIPiDIP-38538N.
IntActiQ15797. 74 interactors.
MINTiMINT-244113.
STRINGi9606.ENSP00000305769.

Structurei

Secondary structure

1465
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi272 – 278Combined sources7
Beta strandi291 – 299Combined sources9
Beta strandi305 – 310Combined sources6
Helixi321 – 327Combined sources7
Beta strandi334 – 338Combined sources5
Beta strandi340 – 347Combined sources8
Beta strandi349 – 351Combined sources3
Beta strandi353 – 356Combined sources4
Helixi358 – 363Combined sources6
Beta strandi372 – 374Combined sources3
Beta strandi379 – 384Combined sources6
Helixi385 – 393Combined sources9
Turni394 – 398Combined sources5
Helixi400 – 404Combined sources5
Helixi405 – 410Combined sources6
Beta strandi411 – 417Combined sources7
Helixi429 – 431Combined sources3
Beta strandi432 – 440Combined sources9
Helixi441 – 451Combined sources11
Beta strandi461 – 463Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KHUX-ray2.50A/B/C/D248-465[»]
2LAWNMR-B222-233[»]
2LAXNMR-B201-209[»]
2LAYNMR-B201-209[»]
2LAZNMR-B210-217[»]
2LB0NMR-B208-217[»]
2LB1NMR-B220-233[»]
3Q47X-ray1.70C456-464[»]
3Q4AX-ray1.54C456-465[»]
ProteinModelPortaliQ15797.
SMRiQ15797.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 136MH1PROSITE-ProRule annotationAdd BLAST125
Domaini271 – 465MH2PROSITE-ProRule annotationAdd BLAST195

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni418 – 428L3 loop1 PublicationAdd BLAST11

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi39 – 45Poly-Lys7
Compositional biasi198 – 201Poly-Ser4

Domaini

The MH2 domain mediates phosphorylation-dependent trimerization through L3 loop binding of phosphoserines in the adjacent subunit.1 Publication

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

eggNOGiKOG3701. Eukaryota.
ENOG410XQKU. LUCA.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000286019.
HOVERGENiHBG053353.
InParanoidiQ15797.
KOiK04676.
OMAiMTHDTSQ.
OrthoDBiEOG091G082C.
PhylomeDBiQ15797.
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. 1 hit.
PROSITEiPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15797-1) [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
MNVTSLFSFT SPAVKRLLGW KQGDEEEKWA EKAVDALVKK LKKKKGAMEE
60 70 80 90 100
LEKALSCPGQ PSNCVTIPRS LDGRLQVSHR KGLPHVIYCR VWRWPDLQSH
110 120 130 140 150
HELKPLECCE FPFGSKQKEV CINPYHYKRV ESPVLPPVLV PRHSEYNPQH
160 170 180 190 200
SLLAQFRNLG QNEPHMPLNA TFPDSFQQPN SHPFPHSPNS SYPNSPGSSS
210 220 230 240 250
STYPHSPTSS DPGSPFQMPA DTPPPAYLPP EDPMTQDGSQ PMDTNMMAPP
260 270 280 290 300
LPSEINRGDV QAVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT
310 320 330 340 350
DPSNNKNRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD
360 370 380 390 400
SSIFVQSRNC NYHHGFHPTT VCKIPSGCSL KIFNNQEFAQ LLAQSVNHGF
410 420 430 440 450
ETVYELTKMC TIRMSFVKGW GAEYHRQDVT STPCWIEIHL HGPLQWLDKV
460
LTQMGSPHNP ISSVS
Length:465
Mass (Da):52,260
Last modified:November 1, 1996 - v1
Checksum:i2DD34B7F434DBC7E
GO
Isoform 2 (identifier: Q15797-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MNVTSLFSFTSP → MFVLLFFPFLFL
     13-133: Missing.
     220-258: ADTPPPAYLP...PPLPSEINRG → GRLECSVMFC...EGGFQPWYMT
     259-465: Missing.

Note: No experimental confirmation available.
Show »
Length:137
Mass (Da):15,406
Checksum:iA43324EACCA53062
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0668693V → A Found in a patient with primary pulmonary hypertension; unknown pathological significance; affects SMAD-mediated signaling. 1 PublicationCorresponds to variant rs587777018dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0571631 – 12MNVTS…SFTSP → MFVLLFFPFLFL in isoform 2. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_05716413 – 133Missing in isoform 2. 1 PublicationAdd BLAST121
Alternative sequenceiVSP_057165220 – 258ADTPP…EINRG → GRLECSVMFCSHIRQCYHSV TEKLGQPAVEGGFQPWYMT in isoform 2. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_057166259 – 465Missing in isoform 2. 1 PublicationAdd BLAST207

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59912 mRNA. Translation: AAC50790.1.
U59423 mRNA. Translation: AAB06852.1.
U54826 mRNA. Translation: AAC50493.1.
U57456 mRNA. Translation: AAC50621.1.
BT007386 mRNA. Translation: AAP36050.1.
AK293055 mRNA. Translation: BAF85744.1.
AL117396 Genomic DNA. Translation: CAB55898.1.
CH471056 Genomic DNA. Translation: EAX05037.1.
CH471056 Genomic DNA. Translation: EAX05038.1.
CH471056 Genomic DNA. Translation: EAX05039.1.
CH471056 Genomic DNA. Translation: EAX05040.1.
BC001878 mRNA. Translation: AAH01878.1.
CCDSiCCDS3765.1. [Q15797-1]
PIRiS68987.
RefSeqiNP_001003688.1. NM_001003688.1. [Q15797-1]
NP_005891.1. NM_005900.2. [Q15797-1]
XP_005263049.1. XM_005262992.3. [Q15797-1]
XP_006714280.1. XM_006714217.2. [Q15797-1]
XP_011530263.1. XM_011531961.1. [Q15797-1]
XP_011530264.1. XM_011531962.1. [Q15797-1]
XP_011530265.1. XM_011531963.1. [Q15797-1]
XP_011530266.1. XM_011531964.1. [Q15797-1]
UniGeneiHs.604588.

Genome annotation databases

EnsembliENST00000302085; ENSP00000305769; ENSG00000170365. [Q15797-1]
ENST00000394092; ENSP00000377652; ENSG00000170365. [Q15797-1]
ENST00000515385; ENSP00000426568; ENSG00000170365. [Q15797-1]
GeneIDi4086.
KEGGihsa:4086.
UCSCiuc003ikc.4. human. [Q15797-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59912 mRNA. Translation: AAC50790.1.
U59423 mRNA. Translation: AAB06852.1.
U54826 mRNA. Translation: AAC50493.1.
U57456 mRNA. Translation: AAC50621.1.
BT007386 mRNA. Translation: AAP36050.1.
AK293055 mRNA. Translation: BAF85744.1.
AL117396 Genomic DNA. Translation: CAB55898.1.
CH471056 Genomic DNA. Translation: EAX05037.1.
CH471056 Genomic DNA. Translation: EAX05038.1.
CH471056 Genomic DNA. Translation: EAX05039.1.
CH471056 Genomic DNA. Translation: EAX05040.1.
BC001878 mRNA. Translation: AAH01878.1.
CCDSiCCDS3765.1. [Q15797-1]
PIRiS68987.
RefSeqiNP_001003688.1. NM_001003688.1. [Q15797-1]
NP_005891.1. NM_005900.2. [Q15797-1]
XP_005263049.1. XM_005262992.3. [Q15797-1]
XP_006714280.1. XM_006714217.2. [Q15797-1]
XP_011530263.1. XM_011531961.1. [Q15797-1]
XP_011530264.1. XM_011531962.1. [Q15797-1]
XP_011530265.1. XM_011531963.1. [Q15797-1]
XP_011530266.1. XM_011531964.1. [Q15797-1]
UniGeneiHs.604588.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KHUX-ray2.50A/B/C/D248-465[»]
2LAWNMR-B222-233[»]
2LAXNMR-B201-209[»]
2LAYNMR-B201-209[»]
2LAZNMR-B210-217[»]
2LB0NMR-B208-217[»]
2LB1NMR-B220-233[»]
3Q47X-ray1.70C456-464[»]
3Q4AX-ray1.54C456-465[»]
ProteinModelPortaliQ15797.
SMRiQ15797.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110261. 119 interactors.
DIPiDIP-38538N.
IntActiQ15797. 74 interactors.
MINTiMINT-244113.
STRINGi9606.ENSP00000305769.

PTM databases

iPTMnetiQ15797.
PhosphoSitePlusiQ15797.

Polymorphism and mutation databases

BioMutaiSMAD1.
DMDMi13633915.

Proteomic databases

EPDiQ15797.
MaxQBiQ15797.
PaxDbiQ15797.
PeptideAtlasiQ15797.
PRIDEiQ15797.

Protocols and materials databases

DNASUi4086.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302085; ENSP00000305769; ENSG00000170365. [Q15797-1]
ENST00000394092; ENSP00000377652; ENSG00000170365. [Q15797-1]
ENST00000515385; ENSP00000426568; ENSG00000170365. [Q15797-1]
GeneIDi4086.
KEGGihsa:4086.
UCSCiuc003ikc.4. human. [Q15797-1]

Organism-specific databases

CTDi4086.
DisGeNETi4086.
GeneCardsiSMAD1.
HGNCiHGNC:6767. SMAD1.
HPAiCAB005389.
CAB069411.
MalaCardsiSMAD1.
MIMi601595. gene.
neXtProtiNX_Q15797.
OpenTargetsiENSG00000170365.
PharmGKBiPA30524.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3701. Eukaryota.
ENOG410XQKU. LUCA.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000286019.
HOVERGENiHBG053353.
InParanoidiQ15797.
KOiK04676.
OMAiMTHDTSQ.
OrthoDBiEOG091G082C.
PhylomeDBiQ15797.
TreeFamiTF314923.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170365-MONOMER.
ReactomeiR-HSA-201451. Signaling by BMP.
R-HSA-5689880. Ub-specific processing proteases.
SignaLinkiQ15797.
SIGNORiQ15797.

Miscellaneous databases

EvolutionaryTraceiQ15797.
GeneWikiiMothers_against_decapentaplegic_homolog_1.
GenomeRNAii4086.
PROiQ15797.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000170365.
CleanExiHS_SMAD1.
ExpressionAtlasiQ15797. baseline and differential.
GenevisibleiQ15797. HS.

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. 1 hit.
PROSITEiPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSMAD1_HUMAN
AccessioniPrimary (citable) accession number: Q15797
Secondary accession number(s): A8KAJ0
, D3DNZ9, Q16636, Q9UFT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 188 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 4
    Human chromosome 4: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.