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Protein

Cyclic AMP-responsive element-binding protein 3

Gene

CREB3

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

Functioni

Endoplasmic reticulum (ER)-bound transcription factor that plays a role in the unfolded protein response (UPR). Involved in cell proliferation and migration, tumor suppression and inflammatory gene expression. Plays also a role in the human immunodeficiency virus type 1 (HIV-1) virus protein expression and in the herpes simplex virus-1 (HSV-1) latent infection and reactivation from latency. Isoform 2 plays a role in the unfolded protein response (UPR). Isoform 2 acts as a positive regulator of LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell migration. Isoform 2 may play a role as a cellular tumor suppressor that is targeted by the hepatitis C virus (HSV) core protein. Isoform 2 represses the VP16-mediated transactivation of immediate early genes of the HSV-1 virus by sequestring host cell factor-1 HCFC1 in the ER membrane of sensory neurons, thereby preventing the initiation of the replicative cascade leading to latent infection. Isoform 3 functions as a negative transcriptional regulator in ligand-induced transcriptional activation of the glucocorticoid receptor NR3C1 by recruiting and activating histone deacetylases (HDAC1, HDAC2 and HDAC6). Isoform 3 decreases the acetylation level of histone H4. Isoform 3 does not promote the chemotactic activity of leukocyte cells.
Processed cyclic AMP-responsive element-binding protein 3: acts as a transcription factor that activates unfolded protein response (UPR) target genes during endoplasmic reticulum (ER) stress response. Promotes cell survival against ER stress-induced apoptotic cell death during UPR. Activates transcription from CRE and C/EBP-containing reporter genes. Induces transcriptional activation of chemokine receptors. Activates transcription of genes required for reactivation of the latent HSV-1 virus. Down-regulates Tat-dependent transcription of the HIV-1 LTR by interacting with HIV-1 Tat. It's transcriptional activity is inhibited by CREBZF in a HCFC1-dependent manner, by the viral transactivator protein VP16 and by the HCV core protein. Binds DNA to the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and C/EBP sequences present in many viral and cellular promoters. Binds to the unfolded protein respons element (UPRE) consensus sequences sites. Binds DNA to the 5'-CCAC[GA]-3'half of ERSE II (5'-ATTGG-N-CCACG-3'). Associates with chromatin to the HERPUD1 promoter.

GO - Molecular functioni

  • cAMP response element binding Source: InterPro
  • cAMP response element binding protein binding Source: UniProtKB
  • CCR1 chemokine receptor binding Source: UniProtKB
  • chromatin binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: ParkinsonsUK-UCL
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • chemotaxis Source: UniProtKB-KW
  • cytoplasmic sequestering of transcription factor Source: UniProtKB
  • establishment of viral latency Source: UniProtKB
  • induction of positive chemotaxis Source: UniProtKB
  • negative regulation of cell cycle Source: UniProtKB
  • negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  • negative regulation of ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • positive regulation of calcium ion transport Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of deacetylase activity Source: UniProtKB
  • positive regulation of defense response to virus by host Source: UniProtKB
  • positive regulation of monocyte chemotaxis Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response Source: ParkinsonsUK-UCL
  • regulation of cell growth Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • release from viral latency Source: UniProtKB
  • response to endoplasmic reticulum stress Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Chemotaxis, Host-virus interaction, Transcription, Transcription regulation, Unfolded protein response

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000107175-MONOMER.
SIGNORiO43889.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic AMP-responsive element-binding protein 3
Short name:
CREB-3
Short name:
cAMP-responsive element-binding protein 3
Alternative name(s):
Leucine zipper protein
Luman
Transcription factor LZIP-alpha
Cleaved into the following chain:
Processed cyclic AMP-responsive element-binding protein 3
Short name:
N-terminal Luman
Short name:
Transcriptionally active form
Gene namesi
Name:CREB3
Synonyms:LZIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:2347. CREB3.

Subcellular locationi

Isoform 2 :
  • Endoplasmic reticulum membrane; Single-pass type II membrane protein
  • Membrane

  • Note: Colocalizes with HCFC1 in neuronal cell bodies of the trigeminal ganglia (By similarity). Colocalizes with TM7SF4 in the ER membrane of immature dendritic cell (DC). Colocalizes with CANX, CCR1, HCFC1 in the ER membrane. Sequestred into the cytoplasm by the HCV core protein.By similarity
Isoform 3 :
Processed cyclic AMP-responsive element-binding protein 3 :
  • Nucleus

  • Note: Upon RIP activation the transcriptional active processed cyclic AMP-responsive element-binding protein 3 form translocates into the nucleus. Detected in the nucleus upon dendritic cell maturation and RIP activation. Colocalizes with CREBRF in nuclear foci. Colocalizes with CREBZF in promyelocytic leukemia protein nuclear bodies (PML-NB).

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 254CytoplasmicSequence analysisAdd BLAST254
Transmembranei255 – 271Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST17
Topological domaini272 – 395LumenalSequence analysisAdd BLAST124

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: ParkinsonsUK-UCL
  • endoplasmic reticulum membrane Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: UniProtKB
  • integral component of endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • nuclear body Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12 – 13LL → AA: Does not inhibit interaction with HCFC1. Reduces transcriptional activation. Inhibits strongly transcriptional activation; when associated with 56-A-A-57 and 78-A--A-81 (isoform 2). 1 Publication2
Mutagenesisi16 – 17LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 57-A-A-58 (isoform 3). 2 Publications2
Mutagenesisi57 – 58LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 16-A-A-17 (isoform 3). 1 Publication2
Mutagenesisi57 – 58LL → AA: Does not inhibit interaction with HCFC1. Reduces transcriptional activation. Inhibits strongly transcriptional activation; when associated with 12-A-A-13 and 78-A--A-81 (isoform 2). 1 Publication2
Mutagenesisi78 – 81DHTY → AAAA: Inhibits interaction with HCFC1. Reduces transcriptional activation. Inhibits strongly transcriptional activation; when associated with 12-A-A-13 and 56-A-A-57. Colocalizes with HCFC1 in the nucleus (isoform 2). 2 Publications4
Mutagenesisi81Y → A: Does not retain HCFC1 in the cytoplasm, does not interact with HCFC1, does not activate promoter and fail to protect cells from a productive infection by HSV-1. 1 Publication1
Mutagenesisi184N → G: Does not bind to DNA but retains its ability to interact with HCFC1. Reduces transcriptional activation of unfolded protein respons elements (UPRE)-containing promoter. Colocalizes with HCFC1 in the ER membrane. 1 Publication1
Mutagenesisi276R → A: Does not inhibit proteolytic cleavage and transcriptional activation. 1 Publication1
Mutagenesisi288R → G: Inhibits proteolytic cleavage and transcriptional activation. 1 Publication1
Mutagenesisi291R → G: Inhibits proteolytic cleavage and transcriptional activation. 1 Publication1

Organism-specific databases

DisGeNETi10488.
OpenTargetsiENSG00000107175.
PharmGKBiPA26865.

Polymorphism and mutation databases

BioMutaiCREB3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000766021 – 395Cyclic AMP-responsive element-binding protein 3Add BLAST395
ChainiPRO_00002962041 – ?Processed cyclic AMP-responsive element-binding protein 3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi331N-linked (GlcNAc...)Sequence analysis1
Glycosylationi372N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

The ER membrane embedded cyclic AMP-responsive element-binding protein 3 form is first proteolytically cleaved by site-1 protease (S1P) that generates membrane-associated N-terminus and a luminal C-terminus forms. The membrane-associated N-terminus form is further proteolytically processed probably by the site-2 protease (S2P) through a regulated intramembrane proteolysis (RIP), releasing the transcriptional active processed cyclic AMP-responsive element-binding protein 3 form, which is transported to the nucleus. The proteolytic cleavage is strongly induced during dendritic cell (DC) maturation and inhibited by TM7SF4.
The processed cyclic AMP-responsive element-binding protein 3 is rapidly degraded.
N-glycosylated.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei287 – 288Cleavage; by PS1Curated2
Sitei290 – 291Cleavage; by PS1Curated2

Keywords - PTMi

Glycoprotein

Proteomic databases

PeptideAtlasiO43889.
PRIDEiO43889.

PTM databases

iPTMnetiO43889.
PhosphoSitePlusiO43889.

Expressioni

Tissue specificityi

Expressed in dendritic cells (DC). Weakly expressed in monocytes (at protein level). Ubiquitous.5 Publications

Inductioni

Up-regulated upon differentiation of monocytes towards immature dendritic cells (DC). Down-regulated upon DC maturation. Up-regulated by endoplasmic reticulum stress triggered by thapsigargin (Tg) or tunicamycin (Tm). Up-regulated by CCR1-dependent chemokines in an immediate early response and biphasic manner and by NF-kappa-B.5 Publications

Gene expression databases

BgeeiENSG00000107175.
CleanExiHS_CREB3.
GenevisibleiO43889. HS.

Interactioni

Subunit structurei

Homodimer; homodimerization is prevented by the HCV core protein. Interacts with HCFC1; the interaction is required to stimulate CREB3 transcriptional activity. Isoform 2 interacts with CREBZF; the interaction occurs only in combination with HCFC1. Isoform 2 interacts (via central part and transmembrane region) with TM7SF4 (via C-terminus cytoplasmic domain). Isoform 2 interacts with OS9. Isoform 2 interacts (via leucine-zipper domain) with CREBRF (via leucine-zipper domain); the interaction occurs only after CREB3 activation and promotes CREB3 degradation. Isoform 2 interacts (via C-terminal domain) with CCR1. Isoform 2 interacts (via leucine-zipper and transmembrane domains) with HIV-1 ENV (via cytoplasmic domain). Isoform 2 interacts (via leucine-zipper and transmembrane domains) with HIV-1 TMgp41 (via cytoplasmic domain); the interaction reduces CREB3 stability. Interacts with the HCV core protein. Processed cyclic AMP-responsive element-binding protein 3 interacts with HIV-1 Tat.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P298468EBI-625022,EBI-909718From a different organism.
CCR1P322467EBI-625022,EBI-608322
CREB3L3Q68CJ92EBI-625002,EBI-852194
CREBRFQ8IUR64EBI-625022,EBI-1042699
DCSTAMPQ9H2956EBI-625022,EBI-6095316
HCFC1P516105EBI-625002,EBI-396176
JUNP054124EBI-625002,EBI-852823

GO - Molecular functioni

  • cAMP response element binding protein binding Source: UniProtKB
  • CCR1 chemokine receptor binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115751. 190 interactors.
DIPiDIP-33935N.
IntActiO43889. 132 interactors.
MINTiMINT-1446829.

Structurei

3D structure databases

ProteinModelPortaliO43889.
SMRiO43889.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini174 – 237bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 92Transcription activation (acidic)Add BLAST92
Regioni176 – 208Basic motifPROSITE-ProRule annotationAdd BLAST33
Regioni216 – 237Leucine-zipperPROSITE-ProRule annotationAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi13 – 17LXXLL motif 15
Motifi54 – 58LXXLL motif 25
Motifi78 – 81HCFC1-binding-motif (HBM)4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi340 – 385Pro-richAdd BLAST46

Sequence similaritiesi

Belongs to the bZIP family. ATF subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00520000055538.
HOGENOMiHOG000133026.
HOVERGENiHBG051114.
InParanoidiO43889.
KOiK09048.
PhylomeDBiO43889.
TreeFamiTF316079.

Family and domain databases

InterProiIPR004827. bZIP.
IPR029808. Luman.
[Graphical view]
PANTHERiPTHR22952:SF100. PTHR22952:SF100. 2 hits.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43889-1) [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
MELELDAGDQ DLLAFLLEES GDLGTAPDEA VRAPLDWALP LSEVPSDWEV
60 70 80 90 100
DDLLCSLLSP PASLNILSSS NPCLVHHDHT YSLPRETVSM DLGECEISLT
110 120 130 140 150
GRTGFMGLAI HTFPFAESES CRKEGTQMTP QHMEELAEQE IARLVLTDEE
160 170 180 190 200
KSLLEKEGLI LPETLPLTKT EEQILKRVRR KIRNKRSAQE SRRKKKVYVG
210 220 230 240 250
GLESRVLKYT AQNMELQNKV QLLEEQNLSL LDQLRKLQAM VIEISNKTSS
260 270 280 290 300
SSTCILVLLV SFCLLLVPAM YSSDTRGSLP AEHGVLSRQL RALPSEDPYQ
310 320 330 340 350
LELPALQSEV PKDSTHQWLD GSDCVLQAPG NTSCLLHYMP QAPSAEPPLE
360 370 380 390
WPFPDLFSEP LCRGPILPLQ ANLTRKGGWL PTGSPSVILQ DRYSG
Length:395
Mass (Da):43,917
Last modified:June 1, 1998 - v1
Checksum:i1C412AA0D51CB7B2
GO
Isoform 2 (identifier: O43889-2) [UniParc]FASTAAdd to basket
Also known as: LZIP

The sequence of this isoform differs from the canonical sequence as follows:
     93-116: Missing.

Show »
Length:371
Mass (Da):41,379
Checksum:i82152E496B924EEC
GO
Isoform 3 (identifier: O43889-3) [UniParc]FASTAAdd to basket
Also known as: smal LZIP, sLZIP

The sequence of this isoform differs from the canonical sequence as follows:
     93-116: Missing.
     253-269: Missing.

Note: Does not contain a helical transmembrane domain.
Show »
Length:354
Mass (Da):39,580
Checksum:iBC8F014103A52111
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21G → E in AAG43527 (Ref. 6) Curated1
Sequence conflicti254C → G in AAD09210 (PubMed:10675342).Curated1
Sequence conflicti270M → I in AAH09402 (PubMed:15489334).Curated1
Sequence conflicti286L → C in AAD09210 (PubMed:10675342).Curated1
Sequence conflicti357F → S in AAB69652 (PubMed:9271389).Curated1
Sequence conflicti362C → V in AAD09210 (PubMed:10675342).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01183893 – 116Missing in isoform 2 and isoform 3. 5 PublicationsAdd BLAST24
Alternative sequenceiVSP_043805253 – 269Missing in isoform 3. 1 PublicationAdd BLAST17

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009368 mRNA. Translation: AAB69652.1.
AF029674 mRNA. Translation: AAB84166.1.
U59629 Genomic DNA. Translation: AAD09210.1.
FJ263669 mRNA. Translation: ACN32251.1.
U88528 mRNA. Translation: AAC04325.1.
AF211847 Genomic DNA. Translation: AAG43527.1.
AF211848 mRNA. Translation: AAG43528.1.
AL133410 Genomic DNA. Translation: CAI10980.1.
BC009402 mRNA. Translation: AAH09402.1.
BC010158 mRNA. Translation: AAH10158.1.
CCDSiCCDS6588.1. [O43889-2]
RefSeqiNP_006359.3. NM_006368.4. [O43889-2]
UniGeneiHs.522110.

Genome annotation databases

EnsembliENST00000353704; ENSP00000342136; ENSG00000107175. [O43889-2]
GeneIDi10488.
KEGGihsa:10488.
UCSCiuc003zxv.4. human. [O43889-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009368 mRNA. Translation: AAB69652.1.
AF029674 mRNA. Translation: AAB84166.1.
U59629 Genomic DNA. Translation: AAD09210.1.
FJ263669 mRNA. Translation: ACN32251.1.
U88528 mRNA. Translation: AAC04325.1.
AF211847 Genomic DNA. Translation: AAG43527.1.
AF211848 mRNA. Translation: AAG43528.1.
AL133410 Genomic DNA. Translation: CAI10980.1.
BC009402 mRNA. Translation: AAH09402.1.
BC010158 mRNA. Translation: AAH10158.1.
CCDSiCCDS6588.1. [O43889-2]
RefSeqiNP_006359.3. NM_006368.4. [O43889-2]
UniGeneiHs.522110.

3D structure databases

ProteinModelPortaliO43889.
SMRiO43889.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115751. 190 interactors.
DIPiDIP-33935N.
IntActiO43889. 132 interactors.
MINTiMINT-1446829.

PTM databases

iPTMnetiO43889.
PhosphoSitePlusiO43889.

Polymorphism and mutation databases

BioMutaiCREB3.

Proteomic databases

PeptideAtlasiO43889.
PRIDEiO43889.

Protocols and materials databases

DNASUi10488.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353704; ENSP00000342136; ENSG00000107175. [O43889-2]
GeneIDi10488.
KEGGihsa:10488.
UCSCiuc003zxv.4. human. [O43889-1]

Organism-specific databases

CTDi10488.
DisGeNETi10488.
GeneCardsiCREB3.
HGNCiHGNC:2347. CREB3.
MIMi606443. gene.
neXtProtiNX_O43889.
OpenTargetsiENSG00000107175.
PharmGKBiPA26865.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00520000055538.
HOGENOMiHOG000133026.
HOVERGENiHBG051114.
InParanoidiO43889.
KOiK09048.
PhylomeDBiO43889.
TreeFamiTF316079.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000107175-MONOMER.
SIGNORiO43889.

Miscellaneous databases

ChiTaRSiCREB3. human.
GeneWikiiCREB3.
GenomeRNAii10488.
PROiO43889.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107175.
CleanExiHS_CREB3.
GenevisibleiO43889. HS.

Family and domain databases

InterProiIPR004827. bZIP.
IPR029808. Luman.
[Graphical view]
PANTHERiPTHR22952:SF100. PTHR22952:SF100. 2 hits.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCREB3_HUMAN
AccessioniPrimary (citable) accession number: O43889
Secondary accession number(s): D0PTW6
, O14671, O14919, Q5TCV1, Q96GK8, Q9H2W3, Q9UE77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: June 1, 1998
Last modified: November 30, 2016
This is version 157 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

Caution

All experiments concerning the proteolytic cleavage are done with isoform 2.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. 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.