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Protein

Large proline-rich protein BAG6

Gene

BAG6

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

Functioni

Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane. Moreover, it regulates the stability and the degradation of proteins by the proteasome. For instance, it is required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno-proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. It is also involved in ubiquitin-mediated proteasomal degradation of proteins of the secretory pathway that are mislocalized to the cytosol. Binds the mislocalized proteins, preventing their aggregation in the cytosol, and promotes their ubiquitination. Participates in endoplasmic reticulum stress-induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2.4 Publications
Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).2 Publications
Can be released from tumor and dendritic cells in membrane vesicles or exosomes, and engage NCR3 thereby promoting natural killer cells (NK) activation and cytotoxicity.2 Publications

GO - Molecular functioni

  • misfolded protein binding Source: ParkinsonsUK-UCL
  • polyubiquitin binding Source: UniProtKB
  • proteasome binding Source: UniProtKB
  • ribosome binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-specific protease binding Source: ParkinsonsUK-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator

Keywords - Biological processi

Apoptosis, Differentiation, Immunity, Spermatogenesis, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Large proline-rich protein BAG6
Alternative name(s):
BAG family molecular chaperone regulator 6
BCL2-associated athanogene 6
Short name:
BAG-6
Short name:
BAG6
HLA-B-associated transcript 3
Protein G3
Protein Scythe
Gene namesi
Name:BAG6
Synonyms:BAT3, G3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:13919. BAG6.

Subcellular locationi

  • Cytoplasmcytosol
  • Nucleus

  • Note: The C-terminal fragment generated by caspase-3 is cytoplasmic. Also found in extracellular vesicular exosomes in some tumor cells.

GO - Cellular componenti

  • BAT3 complex Source: UniProtKB
  • cytoplasm Source: ParkinsonsUK-UCL
  • cytosol Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: ParkinsonsUK-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1001 – 10011D → A: Abolishes cleavage by caspase-3. 1 Publication

Organism-specific databases

PharmGKBiPA25264.

Polymorphism and mutation databases

BioMutaiBAG6.
DMDMi76800648.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11321132Large proline-rich protein BAG6PRO_0000114897Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei117 – 1171PhosphothreonineCombined sources
Modified residuei350 – 3501PhosphothreonineCombined sources
Modified residuei964 – 9641PhosphoserineCombined sources
Modified residuei973 – 9731PhosphoserineCombined sources
Modified residuei1081 – 10811PhosphoserineCombined sources
Modified residuei1117 – 11171PhosphoserineCombined sources
Isoform 4 (identifier: P46379-4)
Modified residuei832 – 8321PhosphoserineCombined sources

Post-translational modificationi

Cleavage by caspase-3 releases a C-terminal peptide that plays a role in ricin-induced apoptosis.1 Publication
In case of infection by L.pneumophila, ubiquitinated by the SCF(LegU1) complex.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1001 – 10022Cleavage; by caspase-3

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP46379.
MaxQBiP46379.
PaxDbiP46379.
PRIDEiP46379.

PTM databases

iPTMnetiP46379.
PhosphoSiteiP46379.

Miscellaneous databases

PMAP-CutDBB0UX84.

Expressioni

Gene expression databases

BgeeiP46379.
ExpressionAtlasiP46379. baseline and differential.
GenevisibleiP46379. HS.

Organism-specific databases

HPAiCAB020704.
HPA045116.
HPA053291.

Interactioni

Subunit structurei

Component of the BAT3 complex, at least composed of BAG6/BAT3, UBL4A and GET4/TRC35. Interacts with AIFM1, CTCFL, HSPA2 and p300/EP300. Interacts with ricin A chain. Interacts with L.pneumophila proteins Lpg2160 and LegU1. Interacts with NCR3. Interacts (via ubiquitin-like domain) with RNF126; required for BAG6-dependent ubiquitination of proteins mislocalized to the cytosol.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EFEMP1Q128053EBI-347552,EBI-536772
FAM9BQ8IZU03EBI-347552,EBI-10175124
KLHL12Q53G594EBI-347552,EBI-740929
MAVSQ7Z4342EBI-347552,EBI-995373
RNF126Q9BV684EBI-347552,EBI-357322
SGTAO437655EBI-347552,EBI-347996
TFCP2Q128003EBI-347552,EBI-717422

GO - Molecular functioni

  • misfolded protein binding Source: ParkinsonsUK-UCL
  • polyubiquitin binding Source: UniProtKB
  • proteasome binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-specific protease binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi113647. 261 interactions.
DIPiDIP-31191N.
IntActiP46379. 240 interactions.
MINTiMINT-1032268.
STRINGi9606.ENSP00000365131.

Structurei

Secondary structure

1
1132
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 238Combined sources
Beta strandi28 – 347Combined sources
Helixi39 – 5012Combined sources
Helixi54 – 563Combined sources
Beta strandi57 – 615Combined sources
Beta strandi68 – 714Combined sources
Helixi72 – 754Combined sources
Beta strandi80 – 867Combined sources
Helixi1063 – 107412Combined sources
Helixi1082 – 10898Combined sources
Helixi1092 – 111019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WX9NMR-A17-89[»]
4DWFX-ray1.80A/B13-101[»]
4EEWX-ray1.30A/B1-87[»]
4WWRX-ray2.00A/C/E/G1060-1111[»]
4X86X-ray1.85B1048-1123[»]
ProteinModelPortaliP46379.
SMRiP46379. Positions 13-87, 1057-1112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46379.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 9276Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Repeati242 – 270291Add
BLAST
Repeati415 – 443292Add
BLAST
Repeati574 – 602293Add
BLAST
Repeati608 – 636294Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni242 – 6363954 X 29 AA approximate repeatsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi195 – 27379Pro-richAdd
BLAST
Compositional biasi394 – 681288Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4248. Eukaryota.
ENOG410XS9P. LUCA.
GeneTreeiENSGT00390000016199.
HOVERGENiHBG002193.
InParanoidiP46379.
OMAiPFIERTH.
PhylomeDBiP46379.
TreeFamiTF328437.

Family and domain databases

InterProiIPR021925. DUF3538.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF12057. DUF3538. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P46379-1) [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
MEPNDSTSTA VEEPDSLEVL VKTLDSQTRT FIVGAQMNVK EFKEHIAASV
60 70 80 90 100
SIPSEKQRLI YQGRVLQDDK KLQEYNVGGK VIHLVERAPP QTHLPSGASS
110 120 130 140 150
GTGSASATHG GGSPPGTRGP GASVHDRNAN SYVMVGTFNL PSDGSAVDVH
160 170 180 190 200
INMEQAPIQS EPRVRLVMAQ HMIRDIQTLL SRMETLPYLQ CRGGPQPQHS
210 220 230 240 250
QPPPQPPAVT PEPVALSSQT SEPVESEAPP REPMEAEEVE ERAPAQNPEL
260 270 280 290 300
TPGPAPAGPT PAPETNAPNH PSPAEYVEVL QELQRLESRL QPFLQRYYEV
310 320 330 340 350
LGAAATTDYN NNHEGREEDQ RLINLVGESL RLLGNTFVAL SDLRCNLACT
360 370 380 390 400
PPRHLHVVRP MSHYTTPMVL QQAAIPIQIN VGTTVTMTGN GTRPPPTPNA
410 420 430 440 450
EAPPPGPGQA SSVAPSSTNV ESSAEGAPPP GPAPPPATSH PRVIRISHQS
460 470 480 490 500
VEPVVMMHMN IQDSGTQPGG VPSAPTGPLG PPGHGQTLGQ QVPGFPTAPT
510 520 530 540 550
RVVIARPTPP QARPSHPGGP PVSGTLQGAG LGTNASLAQM VSGLVGQLLM
560 570 580 590 600
QPVLVAQGTP GMAPPPAPAT ASASAGTTNT ATTAGPAPGG PAQPPPTPQP
610 620 630 640 650
SMADLQFSQL LGNLLGPAGP GAGGSGVASP TITVAMPGVP AFLQGMTDFL
660 670 680 690 700
QATQTAPPPP PPPPPPPPAP EQQTMPPPGS PSGGAGSPGG LGLESLSPEF
710 720 730 740 750
FTSVVQGVLS SLLGSLGARA GSSESIAAFI QRLSGSSNIF EPGADGALGF
760 770 780 790 800
FGALLSLLCQ NFSMVDVVML LHGHFQPLQR LQPQLRSFFH QHYLGGQEPT
810 820 830 840 850
PSNIRMATHT LITGLEEYVR ESFSLVQVQP GVDIIRTNLE FLQEQFNSIA
860 870 880 890 900
AHVLHCTDSG FGARLLELCN QGLFECLALN LHCLGGQQME LAAVINGRIR
910 920 930 940 950
RMSRGVNPSL VSWLTTMMGL RLQVVLEHMP VGPDAILRYV RRVGDPPQPL
960 970 980 990 1000
PEEPMEVQGA ERASPEPQRE NASPAPGTTA EEAMSRGPPP APEGGSRDEQ
1010 1020 1030 1040 1050
DGASAETEPW AAAVPPEWVP IIQQDIQSQR KVKPQPPLSD AYLSGMPAKR
1060 1070 1080 1090 1100
RKTMQGEGPQ LLLSEAVSRA AKAAGARPLT SPESLSRDLE APEVQESYRQ
1110 1120 1130
QLRSDIQKRL QEDPNYSPQR FPNAQRAFAD DP
Length:1,132
Mass (Da):119,409
Last modified:September 27, 2005 - v2
Checksum:i625B5F86321367ED
GO
Isoform 2 (identifier: P46379-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     185-190: Missing.

Show »
Length:1,126
Mass (Da):118,693
Checksum:i8A67290BC8176ABA
GO
Isoform 3 (identifier: P46379-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     185-190: Missing.
     489-489: G → GSTLIQLPSLPPEFMHAVAHQITHQAMVAAVASAAAG

Note: No experimental confirmation available.
Show »
Length:1,162
Mass (Da):122,342
Checksum:iFE67886ACE6F6432
GO
Isoform 4 (identifier: P46379-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     185-190: Missing.
     527-527: Missing.
     561-685: Missing.
     969-1016: Missing.
     1053-1101: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:903
Mass (Da):96,800
Checksum:i71B4D33EB924A0EA
GO
Isoform 5 (identifier: P46379-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     185-190: Missing.
     1053-1101: Missing.

Note: No experimental confirmation available.
Show »
Length:1,077
Mass (Da):113,456
Checksum:iCB94D1C58A1E3D21
GO

Sequence cautioni

The sequence AAD18085.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB63390.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI18318.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431K → R in BAG65616 (PubMed:14702039).Curated
Sequence conflicti47 – 471A → R in AAA35587 (PubMed:2156268).Curated
Sequence conflicti150 – 1501H → D in BAG65616 (PubMed:14702039).Curated
Sequence conflicti511 – 5111Q → R in BAG65616 (PubMed:14702039).Curated
Sequence conflicti561 – 5611G → D in BAG65616 (PubMed:14702039).Curated
Sequence conflicti617 – 6171P → L in BAG65616 (PubMed:14702039).Curated
Sequence conflicti679 – 6791G → R in BAG65616 (PubMed:14702039).Curated
Sequence conflicti839 – 8391L → R in BAG63924 (PubMed:14702039).Curated
Sequence conflicti842 – 8421L → P in BAG63924 (PubMed:14702039).Curated
Sequence conflicti853 – 8531V → M in CAI46045 (PubMed:17974005).Curated
Sequence conflicti854 – 8541L → Q in BAG65616 (PubMed:14702039).Curated
Sequence conflicti927 – 9271E → D in BAG65616 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti625 – 6251S → P.5 Publications
Corresponds to variant rs1052486 [ dbSNP | Ensembl ].
VAR_023531
Natural varianti728 – 7281A → V.
Corresponds to variant rs11548856 [ dbSNP | Ensembl ].
VAR_037150

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei185 – 1906Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_015695
Alternative sequencei489 – 4891G → GSTLIQLPSLPPEFMHAVAH QITHQAMVAAVASAAAG in isoform 3. CuratedVSP_030519
Alternative sequencei527 – 5271Missing in isoform 4. 1 PublicationVSP_045910
Alternative sequencei561 – 685125Missing in isoform 4. 1 PublicationVSP_045911Add
BLAST
Alternative sequencei969 – 101648Missing in isoform 4. 1 PublicationVSP_045912Add
BLAST
Alternative sequencei1053 – 110149Missing in isoform 4 and isoform 5. 1 PublicationVSP_045913Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33519 mRNA. Translation: AAA35587.1.
M33521, M33520 Genomic DNA. Translation: AAA35588.1.
BX647244 mRNA. Translation: CAI46045.1.
AK302695 mRNA. Translation: BAG63924.1.
AK304879 mRNA. Translation: BAG65616.1.
AF129756 Genomic DNA. Translation: AAD18085.1. Different initiation.
BA000025 Genomic DNA. Translation: BAB63390.1. Different initiation.
AL662801 Genomic DNA. Translation: CAI18314.1.
AL662801 Genomic DNA. Translation: CAI18315.1.
AL662801 Genomic DNA. Translation: CAI18316.2.
AL662801 Genomic DNA. Translation: CAI18318.2. Sequence problems.
AL662847, AL670886 Genomic DNA. Translation: CAI17658.1.
AL662847, AL670886 Genomic DNA. Translation: CAI17659.1.
AL670886, AL662847 Genomic DNA. Translation: CAI17784.1.
AL670886, AL662847 Genomic DNA. Translation: CAI17785.1.
AL670886, AL662847 Genomic DNA. Translation: CAI17786.1.
AL805934 Genomic DNA. Translation: CAI18501.1.
AL805934 Genomic DNA. Translation: CAI18504.1.
AL805934 Genomic DNA. Translation: CAI18508.2.
AL805934 Genomic DNA. Translation: CAI18509.1.
AL670886, AL662847 Genomic DNA. Translation: CAM25014.1.
BX511262 Genomic DNA. Translation: CAM45799.1.
BX511262 Genomic DNA. Translation: CAM45800.1.
BX511262 Genomic DNA. Translation: CAM45801.1.
AL662847, AL670886 Genomic DNA. Translation: CAO72072.1.
CR753842, CR753892 Genomic DNA. Translation: CAQ06558.1.
CR753892, CR753842 Genomic DNA. Translation: CAQ06931.1.
CR354443 Genomic DNA. Translation: CAQ06977.1.
CR759761 Genomic DNA. Translation: CAQ10854.1.
CH471081 Genomic DNA. Translation: EAX03455.1.
BC003133 mRNA. Translation: AAH03133.1.
CCDSiCCDS4709.1. [P46379-2]
CCDS47403.1. [P46379-1]
CCDS56414.1. [P46379-4]
CCDS56415.1. [P46379-5]
PIRiA35098.
RefSeqiNP_001092004.1. NM_001098534.1. [P46379-2]
NP_001186626.1. NM_001199697.1. [P46379-4]
NP_001186627.1. NM_001199698.1. [P46379-5]
NP_004630.3. NM_004639.3. [P46379-1]
NP_542433.1. NM_080702.2. [P46379-2]
NP_542434.1. NM_080703.2. [P46379-2]
XP_006715255.1. XM_006715192.1. [P46379-3]
XP_006725572.1. XM_006725509.1. [P46379-3]
XP_006726088.1. XM_006726025.1. [P46379-3]
XP_006726176.1. XM_006726113.1. [P46379-3]
XP_011513208.1. XM_011514906.1. [P46379-5]
XP_011545610.1. XM_011547308.1. [P46379-5]
XP_011546596.1. XM_011548294.1. [P46379-5]
XP_011546784.1. XM_011548482.1. [P46379-5]
UniGeneiHs.440900.

Genome annotation databases

EnsembliENST00000211379; ENSP00000211379; ENSG00000204463. [P46379-2]
ENST00000361076; ENSP00000354368; ENSG00000096155. [P46379-1]
ENST00000362049; ENSP00000354875; ENSG00000204463. [P46379-5]
ENST00000375964; ENSP00000365131; ENSG00000204463. [P46379-1]
ENST00000375976; ENSP00000365143; ENSG00000204463. [P46379-2]
ENST00000383446; ENSP00000372938; ENSG00000096155. [P46379-2]
ENST00000383448; ENSP00000372940; ENSG00000096155. [P46379-2]
ENST00000417144; ENSP00000412110; ENSG00000229524. [P46379-2]
ENST00000419847; ENSP00000389121; ENSG00000233348. [P46379-2]
ENST00000439687; ENSP00000402856; ENSG00000204463. [P46379-4]
ENST00000442479; ENSP00000413698; ENSG00000229524. [P46379-2]
ENST00000443182; ENSP00000410156; ENSG00000233348. [P46379-2]
ENST00000449450; ENSP00000397894; ENSG00000229524. [P46379-1]
ENST00000451932; ENSP00000390966; ENSG00000233348. [P46379-1]
ENST00000551350; ENSP00000447546; ENSG00000229524. [P46379-5]
ENST00000552116; ENSP00000447946; ENSG00000233348. [P46379-5]
ENST00000552605; ENSP00000446525; ENSG00000096155. [P46379-5]
ENST00000613474; ENSP00000478966; ENSG00000227761. [P46379-4]
ENST00000615143; ENSP00000482413; ENSG00000229524. [P46379-4]
ENST00000615224; ENSP00000477951; ENSG00000228760. [P46379-4]
ENST00000615725; ENSP00000479238; ENSG00000233348. [P46379-4]
ENST00000617635; ENSP00000484238; ENSG00000096155. [P46379-4]
ENST00000621056; ENSP00000477867; ENSG00000234651. [P46379-4]
GeneIDi7917.
KEGGihsa:7917.
UCSCiuc003nvf.4. human. [P46379-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33519 mRNA. Translation: AAA35587.1.
M33521, M33520 Genomic DNA. Translation: AAA35588.1.
BX647244 mRNA. Translation: CAI46045.1.
AK302695 mRNA. Translation: BAG63924.1.
AK304879 mRNA. Translation: BAG65616.1.
AF129756 Genomic DNA. Translation: AAD18085.1. Different initiation.
BA000025 Genomic DNA. Translation: BAB63390.1. Different initiation.
AL662801 Genomic DNA. Translation: CAI18314.1.
AL662801 Genomic DNA. Translation: CAI18315.1.
AL662801 Genomic DNA. Translation: CAI18316.2.
AL662801 Genomic DNA. Translation: CAI18318.2. Sequence problems.
AL662847, AL670886 Genomic DNA. Translation: CAI17658.1.
AL662847, AL670886 Genomic DNA. Translation: CAI17659.1.
AL670886, AL662847 Genomic DNA. Translation: CAI17784.1.
AL670886, AL662847 Genomic DNA. Translation: CAI17785.1.
AL670886, AL662847 Genomic DNA. Translation: CAI17786.1.
AL805934 Genomic DNA. Translation: CAI18501.1.
AL805934 Genomic DNA. Translation: CAI18504.1.
AL805934 Genomic DNA. Translation: CAI18508.2.
AL805934 Genomic DNA. Translation: CAI18509.1.
AL670886, AL662847 Genomic DNA. Translation: CAM25014.1.
BX511262 Genomic DNA. Translation: CAM45799.1.
BX511262 Genomic DNA. Translation: CAM45800.1.
BX511262 Genomic DNA. Translation: CAM45801.1.
AL662847, AL670886 Genomic DNA. Translation: CAO72072.1.
CR753842, CR753892 Genomic DNA. Translation: CAQ06558.1.
CR753892, CR753842 Genomic DNA. Translation: CAQ06931.1.
CR354443 Genomic DNA. Translation: CAQ06977.1.
CR759761 Genomic DNA. Translation: CAQ10854.1.
CH471081 Genomic DNA. Translation: EAX03455.1.
BC003133 mRNA. Translation: AAH03133.1.
CCDSiCCDS4709.1. [P46379-2]
CCDS47403.1. [P46379-1]
CCDS56414.1. [P46379-4]
CCDS56415.1. [P46379-5]
PIRiA35098.
RefSeqiNP_001092004.1. NM_001098534.1. [P46379-2]
NP_001186626.1. NM_001199697.1. [P46379-4]
NP_001186627.1. NM_001199698.1. [P46379-5]
NP_004630.3. NM_004639.3. [P46379-1]
NP_542433.1. NM_080702.2. [P46379-2]
NP_542434.1. NM_080703.2. [P46379-2]
XP_006715255.1. XM_006715192.1. [P46379-3]
XP_006725572.1. XM_006725509.1. [P46379-3]
XP_006726088.1. XM_006726025.1. [P46379-3]
XP_006726176.1. XM_006726113.1. [P46379-3]
XP_011513208.1. XM_011514906.1. [P46379-5]
XP_011545610.1. XM_011547308.1. [P46379-5]
XP_011546596.1. XM_011548294.1. [P46379-5]
XP_011546784.1. XM_011548482.1. [P46379-5]
UniGeneiHs.440900.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WX9NMR-A17-89[»]
4DWFX-ray1.80A/B13-101[»]
4EEWX-ray1.30A/B1-87[»]
4WWRX-ray2.00A/C/E/G1060-1111[»]
4X86X-ray1.85B1048-1123[»]
ProteinModelPortaliP46379.
SMRiP46379. Positions 13-87, 1057-1112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113647. 261 interactions.
DIPiDIP-31191N.
IntActiP46379. 240 interactions.
MINTiMINT-1032268.
STRINGi9606.ENSP00000365131.

PTM databases

iPTMnetiP46379.
PhosphoSiteiP46379.

Polymorphism and mutation databases

BioMutaiBAG6.
DMDMi76800648.

Proteomic databases

EPDiP46379.
MaxQBiP46379.
PaxDbiP46379.
PRIDEiP46379.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000211379; ENSP00000211379; ENSG00000204463. [P46379-2]
ENST00000361076; ENSP00000354368; ENSG00000096155. [P46379-1]
ENST00000362049; ENSP00000354875; ENSG00000204463. [P46379-5]
ENST00000375964; ENSP00000365131; ENSG00000204463. [P46379-1]
ENST00000375976; ENSP00000365143; ENSG00000204463. [P46379-2]
ENST00000383446; ENSP00000372938; ENSG00000096155. [P46379-2]
ENST00000383448; ENSP00000372940; ENSG00000096155. [P46379-2]
ENST00000417144; ENSP00000412110; ENSG00000229524. [P46379-2]
ENST00000419847; ENSP00000389121; ENSG00000233348. [P46379-2]
ENST00000439687; ENSP00000402856; ENSG00000204463. [P46379-4]
ENST00000442479; ENSP00000413698; ENSG00000229524. [P46379-2]
ENST00000443182; ENSP00000410156; ENSG00000233348. [P46379-2]
ENST00000449450; ENSP00000397894; ENSG00000229524. [P46379-1]
ENST00000451932; ENSP00000390966; ENSG00000233348. [P46379-1]
ENST00000551350; ENSP00000447546; ENSG00000229524. [P46379-5]
ENST00000552116; ENSP00000447946; ENSG00000233348. [P46379-5]
ENST00000552605; ENSP00000446525; ENSG00000096155. [P46379-5]
ENST00000613474; ENSP00000478966; ENSG00000227761. [P46379-4]
ENST00000615143; ENSP00000482413; ENSG00000229524. [P46379-4]
ENST00000615224; ENSP00000477951; ENSG00000228760. [P46379-4]
ENST00000615725; ENSP00000479238; ENSG00000233348. [P46379-4]
ENST00000617635; ENSP00000484238; ENSG00000096155. [P46379-4]
ENST00000621056; ENSP00000477867; ENSG00000234651. [P46379-4]
GeneIDi7917.
KEGGihsa:7917.
UCSCiuc003nvf.4. human. [P46379-1]

Organism-specific databases

CTDi7917.
GeneCardsiBAG6.
H-InvDBHIX0165051.
HIX0166179.
HIX0166289.
HIX0166578.
HIX0166832.
HIX0167081.
HIX0167222.
HIX0167321.
HIX0167461.
HIX0167568.
HGNCiHGNC:13919. BAG6.
HPAiCAB020704.
HPA045116.
HPA053291.
MIMi142590. gene.
neXtProtiNX_P46379.
PharmGKBiPA25264.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4248. Eukaryota.
ENOG410XS9P. LUCA.
GeneTreeiENSGT00390000016199.
HOVERGENiHBG002193.
InParanoidiP46379.
OMAiPFIERTH.
PhylomeDBiP46379.
TreeFamiTF328437.

Miscellaneous databases

ChiTaRSiBAG6. human.
EvolutionaryTraceiP46379.
GeneWikiiHLA-B_associated_transcript_3.
GenomeRNAii7917.
NextBioi30391.
PMAP-CutDBB0UX84.
PROiP46379.
SOURCEiSearch...

Gene expression databases

BgeeiP46379.
ExpressionAtlasiP46379. baseline and differential.
GenevisibleiP46379. HS.

Family and domain databases

InterProiIPR021925. DUF3538.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF12057. DUF3538. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A gene pair from the human major histocompatibility complex encodes large proline-rich proteins with multiple repeated motifs and a single ubiquitin-like domain."
    Banerji J., Sands J., Strominger J.L., Spies T.
    Proc. Natl. Acad. Sci. U.S.A. 87:2374-2378(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT PRO-625.
    Tissue: T-cell.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Endometrium.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), VARIANT PRO-625.
    Tissue: Testis.
  4. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
    Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
    Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
    Hirakawa M., Yamaguchi H., Imai K., Shimada J., Shiina S., Tamiya G., Oka A., Inoko H.
    Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-625.
  6. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-625.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-625.
  8. "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 2).
    Tissue: Kidney.
  9. "Ricin triggers apoptotic morphological changes through caspase-3 cleavage of BAT3."
    Wu Y.-H., Shih S.-F., Lin J.-Y.
    J. Biol. Chem. 279:19264-19275(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RICIN A CHAIN, MUTAGENESIS OF ASP-1001, CLEAVAGE BY CASPASE-3.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53."
    Sasaki T., Gan E.C., Wakeham A., Kornbluth S., Mak T.W., Okada H.
    Genes Dev. 21:848-861(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EP300.
  13. "Human leukocyte antigen-B-associated transcript 3 is released from tumor cells and engages the NKp30 receptor on natural killer cells."
    Pogge von Strandmann E., Simhadri V.R., von Tresckow B., Sasse S., Reiners K.S., Hansen H.P., Rothe A., Boll B., Simhadri V.L., Borchmann P., McKinnon P.J., Hallek M., Engert A.
    Immunity 27:965-974(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NK CELL ACTIVATION, INTERACTION WITH NCR3.
  14. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  16. "BAT3 and SET1A form a complex with CTCFL/BORIS to modulate H3K4 histone dimethylation and gene expression."
    Nguyen P., Bar-Sela G., Sun L., Bisht K.S., Cui H., Kohn E., Feinberg A.P., Gius D.
    Mol. Cell. Biol. 28:6720-6729(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CTCFL.
  17. "Dendritic cells release HLA-B-associated transcript-3 positive exosomes to regulate natural killer function."
    Simhadri V.R., Reiners K.S., Hansen H.P., Topolar D., Simhadri V.L., Nohroudi K., Kufer T.A., Engert A., Pogge von Strandmann E.
    PLoS ONE 3:E3377-E3377(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NK CELL ACTIVATION, INTERACTION WITH NCR3.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-973; SER-1081 AND SER-1117, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964 AND SER-973, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "E3 ubiquitin ligase activity and targeting of BAT3 by multiple Legionella pneumophila translocated substrates."
    Ensminger A.W., Isberg R.R.
    Infect. Immun. 78:3905-3919(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION IN CASE OF INFECTION BY L.PNEUMOPHILA.
  22. "Bat3 promotes the membrane integration of tail-anchored proteins."
    Leznicki P., Clancy A., Schwappach B., High S.
    J. Cell Sci. 123:2170-2178(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "A ribosome-associating factor chaperones tail-anchored membrane proteins."
    Mariappan M., Li X., Stefanovic S., Sharma A., Mateja A., Keenan R.J., Hegde R.S.
    Nature 466:1120-1124(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, RIBOSOME-BINDING, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BAG6/BAT3 COMPLEX.
  24. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-350; SER-964; SER-973 AND SER-1117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964 AND SER-973, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND THR-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  28. "Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6."
    Rodrigo-Brenni M.C., Gutierrez E., Hegde R.S.
    Mol. Cell 55:227-237(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RNF126.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Solution structure of the N-terminal ubiquitin-like domain in the human BAT3 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 17-89.

Entry informationi

Entry nameiBAG6_HUMAN
AccessioniPrimary (citable) accession number: P46379
Secondary accession number(s): A2ADJ7
, A3KQ42, A3KQ44, A6NGY6, A6PWF7, B0UX84, B4DZ12, B4E3V4, E7EMZ4, F8VXY4, O95874, Q5HYL9, Q5SQ35, Q5SQ36, Q5SQ37, Q5SQ41, Q5SRP8, Q5SRP9, Q5STC1, Q5STX1, Q5STX3, Q96SA6, Q9BCN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 27, 2005
Last modified: May 11, 2016
This is version 153 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 6
    Human chromosome 6: 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.