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Protein

CUGBP Elav-like family member 1

Gene

CELF1

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

Functioni

RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB. Promotes exclusion of exon 11 of the INSR pre-mRNA. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Increases translation and controls the choice of translation initiation codon of CEBPB mRNA. Increases mRNA translation of CEBPB in aging liver (By similarity). Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3. Mediates rapid cytoplasmic mRNA deadenylation. Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation. Required for completion of spermatogenesis (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs). Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA. Binds to the 5'-region of CDKN1A and CEBPB mRNAs. Binds with the 5'-region of CEBPB mRNA in aging liver.By similarity8 Publications

GO - Molecular functioni

  • BRE binding Source: UniProtKB
  • mRNA binding Source: BHF-UCL
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • translation repressor activity, nucleic acid binding Source: UniProtKB

GO - Biological processi

  • embryo development Source: UniProtKB
  • germ cell development Source: UniProtKB
  • mRNA processing Source: ProtInc
  • mRNA splice site selection Source: UniProtKB
  • positive regulation of multicellular organism growth Source: Ensembl
  • regulation of RNA splicing Source: UniProtKB
  • RNA interference Source: UniProtKB
  • spermatid development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000149187-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
CUGBP Elav-like family member 1
Short name:
CELF-1
Alternative name(s):
50 kDa nuclear polyadenylated RNA-binding protein
Bruno-like protein 2
CUG triplet repeat RNA-binding protein 1
Short name:
CUG-BP1
CUG-BP- and ETR-3-like factor 1
Deadenylation factor CUG-BP
Embryo deadenylation element-binding protein homolog
Short name:
EDEN-BP homolog
RNA-binding protein BRUNOL-2
Gene namesi
Name:CELF1
Synonyms:BRUNOL2, CUGBP, CUGBP1, NAB50
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:2549. CELF1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi63F → L: Does not reduce RNA-binding; when associated with D-331 and F-472. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472. 1 Publication1
Mutagenesisi331G → D: Does not reduce RNA-binding; when associated with L-63 and F-472. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472. 1 Publication1
Mutagenesisi472L → F: Does not reduce RNA-binding; when associated with L-63 and D-331. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472. 1 Publication1

Organism-specific databases

DisGeNETi10658.
OpenTargetsiENSG00000149187.
PharmGKBiPA27045.

Polymorphism and mutation databases

BioMutaiCELF1.
DMDMi17374605.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000815381 – 486CUGBP Elav-like family member 1Add BLAST486

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei4PhosphothreonineCombined sources1
Modified residuei179PhosphoserineCombined sources1
Modified residuei302PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated. Its phosphorylation status increases in senescent cells.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ92879.
MaxQBiQ92879.
PaxDbiQ92879.
PeptideAtlasiQ92879.
PRIDEiQ92879.

PTM databases

iPTMnetiQ92879.
PhosphoSitePlusiQ92879.

Expressioni

Tissue specificityi

Ubiquitous.3 Publications

Inductioni

Up-regulated in myotonic dystrophy pathophysiology (DM).1 Publication

Gene expression databases

BgeeiENSG00000149187.
CleanExiHS_CUGBP1.
ExpressionAtlasiQ92879. baseline and differential.
GenevisibleiQ92879. HS.

Organism-specific databases

HPAiCAB016114.
HPA044597.

Interactioni

Subunit structurei

Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Associates with polysomes (By similarity). Interacts with HNRNPH1; the interaction in RNA-dependent. Interacts with PARN.By similarity3 Publications

Protein-protein interaction databases

BioGridi115901. 22 interactors.
IntActiQ92879. 19 interactors.
MINTiMINT-1382906.
STRINGi9606.ENSP00000435926.

Structurei

Secondary structure

1486
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 22Combined sources7
Helixi29 – 37Combined sources9
Beta strandi42 – 50Combined sources9
Beta strandi52 – 55Combined sources4
Beta strandi57 – 68Combined sources12
Helixi69 – 79Combined sources11
Turni80 – 82Combined sources3
Beta strandi93 – 96Combined sources4
Helixi98 – 100Combined sources3
Helixi105 – 107Combined sources3
Beta strandi108 – 114Combined sources7
Helixi121 – 128Combined sources8
Helixi129 – 131Combined sources3
Beta strandi134 – 141Combined sources8
Turni143 – 145Combined sources3
Beta strandi147 – 157Combined sources11
Helixi158 – 168Combined sources11
Turni169 – 171Combined sources3
Turni174 – 177Combined sources4
Beta strandi182 – 185Combined sources4
Helixi385 – 388Combined sources4
Beta strandi389 – 391Combined sources3
Turni399 – 401Combined sources3
Beta strandi403 – 407Combined sources5
Helixi414 – 421Combined sources8
Helixi422 – 424Combined sources3
Beta strandi428 – 434Combined sources7
Beta strandi436 – 438Combined sources3
Beta strandi440 – 448Combined sources9
Helixi452 – 462Combined sources11
Beta strandi473 – 475Combined sources3
Beta strandi482 – 484Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CPZNMR-A383-484[»]
2DHSNMR-A1-187[»]
2RQ4NMR-A383-484[»]
2RQCNMR-A383-484[»]
3NMRX-ray1.85A14-187[»]
3NNAX-ray1.90A14-187[»]
3NNCX-ray2.20A14-187[»]
3NNHX-ray2.75A/B/C/D14-100[»]
ProteinModelPortaliQ92879.
SMRiQ92879.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92879.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 99RRM 1PROSITE-ProRule annotationAdd BLAST84
Domaini108 – 188RRM 2PROSITE-ProRule annotationAdd BLAST81
Domaini401 – 479RRM 3PROSITE-ProRule annotationAdd BLAST79

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi287 – 308Ser-richAdd BLAST22

Domaini

RRM1 and RRM2 domains preferentially target UGU(U/G)-rich mRNA elements.1 Publication

Sequence similaritiesi

Belongs to the CELF/BRUNOL family.Curated
Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0146. Eukaryota.
ENOG410XNTW. LUCA.
GeneTreeiENSGT00560000076837.
HOGENOMiHOG000004754.
HOVERGENiHBG107646.
InParanoidiQ92879.
KOiK13207.
PhylomeDBiQ92879.
TreeFamiTF314924.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92879-1) [UniParc]FASTAAdd to basket
Also known as: LYLQ

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
MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINVLRD
60 70 80 90 100
RSQNPPQSKG CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE
110 120 130 140 150
KNNAVEDRKL FIGMISKKCT ENDIRVMFSS FGQIEECRIL RGPDGLSRGC
160 170 180 190 200
AFVTFTTRAM AQTAIKAMHQ AQTMEGCSSP MVVKFADTQK DKEQKRMAQQ
210 220 230 240 250
LQQQMQQISA ASVWGNLAGL NTLGPQYLAL YLQLLQQTAS SGNLNTLSSL
260 270 280 290 300
HPMGGLNAMQ LQNLAALAAA ASAAQNTPSG TNALTTSSSP LSVLTSSGSS
310 320 330 340 350
PSSSSSNSVN PIASLGALQT LAGATAGLNV GSLAGMAALN GGLGSSGLSN
360 370 380 390 400
GTGSTMEALT QAYSGIQQYA AAALPTLYNQ NLLTQQSIGA AGSQKEGPEG
410 420 430 440 450
ANLFIYHLPQ EFGDQDLLQM FMPFGNVVSA KVFIDKQTNL SKCFGFVSYD
460 470 480
NPVSAQAAIQ SMNGFQIGMK RLKVQLKRSK NDSKPY
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Length:486
Mass (Da):52,063
Last modified:October 18, 2001 - v2
Checksum:iC4C13D772273A01D
GO
Isoform 2 (identifier: Q92879-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     231-234: Missing.

Show »
Length:482
Mass (Da):51,546
Checksum:iAC0863DB01A22163
GO
Isoform 3 (identifier: Q92879-3) [UniParc]FASTAAdd to basket
Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     231-234: Missing.
     297-297: S → SA

Show »
Length:483
Mass (Da):51,617
Checksum:i0C8D6B707E157FD1
GO
Isoform 4 (identifier: Q92879-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAAFKLDFLPEMMVDHCSLNSSPVSKKM
     104-104: Missing.

Show »
Length:512
Mass (Da):55,001
Checksum:i2A099A7F4E0F5358
GO
Isoform 5 (identifier: Q92879-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.
     104-104: Missing.

Note: No experimental confirmation available.
Show »
Length:468
Mass (Da):50,130
Checksum:i7CD2C6BFBE344830
GO
Isoform 6 (identifier: Q92879-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     104-104: Missing.

Show »
Length:485
Mass (Da):51,992
Checksum:i37B0006E19EC012A
GO

Sequence cautioni

The sequence BAE06101 differs from that shown. Reason: Erroneous initiation.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0450431 – 17Missing in isoform 5. 1 PublicationAdd BLAST17
Alternative sequenceiVSP_0267871M → MAAFKLDFLPEMMVDHCSLN SSPVSKKM in isoform 4. 1 Publication1
Alternative sequenceiVSP_026788104Missing in isoform 4, isoform 5 and isoform 6. 2 Publications1
Alternative sequenceiVSP_005784231 – 234Missing in isoform 2 and isoform 3. 3 Publications4
Alternative sequenceiVSP_005785297S → SA in isoform 3. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63289 mRNA. Translation: AAC50895.1.
AF248648 mRNA. Translation: AAF86230.1.
AF267533 mRNA. Translation: AAF78955.1.
AF267534 mRNA. Translation: AAF78956.1.
AJ007988 mRNA. Translation: CAC20566.1.
AK304430 mRNA. Translation: BAG65257.1.
AB210019 mRNA. Translation: BAE06101.1. Different initiation.
AC090559 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW67909.1.
CH471064 Genomic DNA. Translation: EAW67912.1.
BC031079 mRNA. Translation: AAH31079.1.
CCDSiCCDS31482.1. [Q92879-1]
CCDS53622.1. [Q92879-6]
CCDS53623.1. [Q92879-4]
CCDS7938.1. [Q92879-2]
CCDS7939.1. [Q92879-3]
RefSeqiNP_001020767.1. NM_001025596.2. [Q92879-1]
NP_001166110.1. NM_001172639.1. [Q92879-4]
NP_001166111.1. NM_001172640.1. [Q92879-6]
NP_006551.1. NM_006560.3. [Q92879-2]
NP_941989.1. NM_198700.2. [Q92879-3]
XP_011518161.1. XM_011519859.1. [Q92879-3]
XP_016872613.1. XM_017017124.1. [Q92879-1]
XP_016872614.1. XM_017017125.1. [Q92879-1]
XP_016872615.1. XM_017017126.1. [Q92879-1]
XP_016872616.1. XM_017017127.1. [Q92879-1]
XP_016872617.1. XM_017017128.1. [Q92879-1]
XP_016872618.1. XM_017017129.1. [Q92879-1]
XP_016872619.1. XM_017017130.1. [Q92879-1]
XP_016872620.1. XM_017017131.1. [Q92879-1]
XP_016872621.1. XM_017017132.1. [Q92879-1]
XP_016872622.1. XM_017017133.1. [Q92879-3]
XP_016872623.1. XM_017017134.1. [Q92879-3]
XP_016872624.1. XM_017017135.1. [Q92879-2]
UniGeneiHs.595333.

Genome annotation databases

EnsembliENST00000310513; ENSP00000308386; ENSG00000149187. [Q92879-2]
ENST00000358597; ENSP00000351409; ENSG00000149187. [Q92879-1]
ENST00000361904; ENSP00000354639; ENSG00000149187. [Q92879-3]
ENST00000395290; ENSP00000378705; ENSG00000149187. [Q92879-6]
ENST00000395292; ENSP00000378706; ENSG00000149187. [Q92879-3]
ENST00000532048; ENSP00000435926; ENSG00000149187. [Q92879-4]
GeneIDi10658.
KEGGihsa:10658.
UCSCiuc001nfk.3. human. [Q92879-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63289 mRNA. Translation: AAC50895.1.
AF248648 mRNA. Translation: AAF86230.1.
AF267533 mRNA. Translation: AAF78955.1.
AF267534 mRNA. Translation: AAF78956.1.
AJ007988 mRNA. Translation: CAC20566.1.
AK304430 mRNA. Translation: BAG65257.1.
AB210019 mRNA. Translation: BAE06101.1. Different initiation.
AC090559 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW67909.1.
CH471064 Genomic DNA. Translation: EAW67912.1.
BC031079 mRNA. Translation: AAH31079.1.
CCDSiCCDS31482.1. [Q92879-1]
CCDS53622.1. [Q92879-6]
CCDS53623.1. [Q92879-4]
CCDS7938.1. [Q92879-2]
CCDS7939.1. [Q92879-3]
RefSeqiNP_001020767.1. NM_001025596.2. [Q92879-1]
NP_001166110.1. NM_001172639.1. [Q92879-4]
NP_001166111.1. NM_001172640.1. [Q92879-6]
NP_006551.1. NM_006560.3. [Q92879-2]
NP_941989.1. NM_198700.2. [Q92879-3]
XP_011518161.1. XM_011519859.1. [Q92879-3]
XP_016872613.1. XM_017017124.1. [Q92879-1]
XP_016872614.1. XM_017017125.1. [Q92879-1]
XP_016872615.1. XM_017017126.1. [Q92879-1]
XP_016872616.1. XM_017017127.1. [Q92879-1]
XP_016872617.1. XM_017017128.1. [Q92879-1]
XP_016872618.1. XM_017017129.1. [Q92879-1]
XP_016872619.1. XM_017017130.1. [Q92879-1]
XP_016872620.1. XM_017017131.1. [Q92879-1]
XP_016872621.1. XM_017017132.1. [Q92879-1]
XP_016872622.1. XM_017017133.1. [Q92879-3]
XP_016872623.1. XM_017017134.1. [Q92879-3]
XP_016872624.1. XM_017017135.1. [Q92879-2]
UniGeneiHs.595333.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CPZNMR-A383-484[»]
2DHSNMR-A1-187[»]
2RQ4NMR-A383-484[»]
2RQCNMR-A383-484[»]
3NMRX-ray1.85A14-187[»]
3NNAX-ray1.90A14-187[»]
3NNCX-ray2.20A14-187[»]
3NNHX-ray2.75A/B/C/D14-100[»]
ProteinModelPortaliQ92879.
SMRiQ92879.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115901. 22 interactors.
IntActiQ92879. 19 interactors.
MINTiMINT-1382906.
STRINGi9606.ENSP00000435926.

PTM databases

iPTMnetiQ92879.
PhosphoSitePlusiQ92879.

Polymorphism and mutation databases

BioMutaiCELF1.
DMDMi17374605.

Proteomic databases

EPDiQ92879.
MaxQBiQ92879.
PaxDbiQ92879.
PeptideAtlasiQ92879.
PRIDEiQ92879.

Protocols and materials databases

DNASUi10658.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310513; ENSP00000308386; ENSG00000149187. [Q92879-2]
ENST00000358597; ENSP00000351409; ENSG00000149187. [Q92879-1]
ENST00000361904; ENSP00000354639; ENSG00000149187. [Q92879-3]
ENST00000395290; ENSP00000378705; ENSG00000149187. [Q92879-6]
ENST00000395292; ENSP00000378706; ENSG00000149187. [Q92879-3]
ENST00000532048; ENSP00000435926; ENSG00000149187. [Q92879-4]
GeneIDi10658.
KEGGihsa:10658.
UCSCiuc001nfk.3. human. [Q92879-1]

Organism-specific databases

CTDi10658.
DisGeNETi10658.
GeneCardsiCELF1.
HGNCiHGNC:2549. CELF1.
HPAiCAB016114.
HPA044597.
MIMi601074. gene.
neXtProtiNX_Q92879.
OpenTargetsiENSG00000149187.
PharmGKBiPA27045.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0146. Eukaryota.
ENOG410XNTW. LUCA.
GeneTreeiENSGT00560000076837.
HOGENOMiHOG000004754.
HOVERGENiHBG107646.
InParanoidiQ92879.
KOiK13207.
PhylomeDBiQ92879.
TreeFamiTF314924.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000149187-MONOMER.

Miscellaneous databases

ChiTaRSiCELF1. human.
EvolutionaryTraceiQ92879.
GeneWikiiCUGBP1.
GenomeRNAii10658.
PROiQ92879.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149187.
CleanExiHS_CUGBP1.
ExpressionAtlasiQ92879. baseline and differential.
GenevisibleiQ92879. HS.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCELF1_HUMAN
AccessioniPrimary (citable) accession number: Q92879
Secondary accession number(s): B4E2U5
, D3DQS0, F8W940, Q4LE52, Q9NP83, Q9NR06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 18, 2001
Last modified: November 2, 2016
This is version 167 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.