Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

BAG family molecular chaperone regulator 1

Gene

BAG1

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

Functioni

Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli.3 Publications

GO - Molecular functioni

  1. receptor signaling protein activity Source: ProtInc

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell surface receptor signaling pathway Source: ProtInc
  3. chaperone cofactor-dependent protein refolding Source: UniProtKB
  4. intracellular signal transduction Source: GOC
  5. negative regulation of apoptotic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
BAG family molecular chaperone regulator 1
Short name:
BAG-1
Alternative name(s):
Bcl-2-associated athanogene 1
Gene namesi
Name:BAG1
Synonyms:HAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:937. BAG1.

Subcellular locationi

Isoform 1 : Nucleus. Cytoplasm
Note: Isoform 1 localizes predominantly to the nucleus.
Isoform 2 : Cytoplasm. Nucleus
Note: Isoform 2 localizes to the cytoplasm and shuttles into the nucleus in response to heat shock.
Isoform 4 : Cytoplasm. Nucleus
Note: Isoform 4 localizes predominantly to the cytoplasm. The cellular background in which it is expressed can influence whether it resides primarily in the cytoplasm or is also found in the nucleus. In the presence of BCL2, localizes to intracellular membranes (what appears to be the nuclear envelope and perinuclear membranes) as well as punctate cytosolic structures suggestive of mitochondria.

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25237.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345BAG family molecular chaperone regulator 1PRO_0000088865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei223 – 2231Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation.Curated

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ99933.
PaxDbiQ99933.
PRIDEiQ99933.

PTM databases

PhosphoSiteiQ99933.

Expressioni

Tissue specificityi

Isoform 4 is the most abundantly expressed isoform. It is ubiquitously expressed throughout most tissues, except the liver, colon, breast and uterine myometrium. Isoform 1 is expressed in the ovary and testis. Isoform 4 is expressed in several types of tumor cell lines, and at consistently high levels in leukemia and lymphoma cell lines. Isoform 1 is expressed in the prostate, breast and leukemia cell lines. Isoform 3 is the least abundant isoform in tumor cell lines (at protein level).1 Publication

Inductioni

Up-regulated during differentiation of bladder epithelial cells and down-regulated during differentiation of prostate epithelium.1 Publication

Gene expression databases

BgeeiQ99933.
CleanExiHS_BAG1.
ExpressionAtlasiQ99933. baseline and differential.
GenevestigatoriQ99933.

Organism-specific databases

HPAiCAB002486.
HPA018121.

Interactioni

Subunit structurei

Homodimer. Forms a heteromeric complex with HSP70/HSC70. Binds to the ATPase domain of HSP/HSC70 chaperones. Isoform 1, isoform 3 and isoform 4 but not isoform 2 interact with HSPA8/HSC70. Interacts with NR3C1. Interacts with the N-terminal region of STK19. Interacts with PPP1R15A. Interacts with BCL2 in an ATP-dependent manner. Isoform 2 does not interact with BCL2.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q53FC72EBI-1030678,EBI-9356749
Q96BE02EBI-1030678,EBI-9356686
HSPA8P1114210EBI-1030678,EBI-351896
PSMD2Q132002EBI-1030678,EBI-357648
STUB1Q9UNE72EBI-1030678,EBI-357085

Protein-protein interaction databases

BioGridi107049. 61 interactions.
DIPiDIP-3341N.
IntActiQ99933. 32 interactions.
MINTiMINT-189058.

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi144 – 1496Combined sources
Beta strandi151 – 1599Combined sources
Beta strandi163 – 1675Combined sources
Helixi170 – 18011Combined sources
Turni185 – 1873Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi200 – 2034Combined sources
Helixi204 – 2074Combined sources
Beta strandi211 – 2199Combined sources
Helixi224 – 25936Combined sources
Helixi264 – 2729Combined sources
Helixi275 – 29218Combined sources
Helixi302 – 32625Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HX1X-ray1.90B222-334[»]
1WXVNMR-A144-222[»]
3FZFX-ray2.20B222-334[»]
3FZHX-ray2.00B222-334[»]
3FZKX-ray2.10B222-334[»]
3FZLX-ray2.20B222-334[»]
3FZMX-ray2.30B222-334[»]
3LDQX-ray1.90B222-334[»]
3M3ZX-ray2.10B222-334[»]
ProteinModelPortaliQ99933.
SMRiQ99933. Positions 140-331.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99933.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati96 – 10161
Repeati102 – 10762
Repeati108 – 11363
Repeati114 – 11964
Repeati120 – 12565
Repeati126 – 13166
Repeati132 – 13767
Domaini144 – 22481Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini246 – 32681BAGPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 137427 X 6 AA tandem repeat of E-E-X(4)Add
BLAST
Regioni172 – 21948Interaction with HSPA8Add
BLAST
Regioni216 – 345130Interaction with PPP1R15AAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 8279Arg-richAdd
BLAST

Sequence similaritiesi

Contains 1 BAG domain.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG72809.
GeneTreeiENSGT00450000040296.
HOVERGENiHBG000236.
InParanoidiQ99933.
KOiK09555.
PhylomeDBiQ99933.

Family and domain databases

Gene3Di1.20.58.120. 1 hit.
InterProiIPR003103. BAG_domain.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF02179. BAG. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00264. BAG. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS51035. BAG. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: Q99933-1) [UniParc]FASTAAdd to basket

Also known as: BAG-1L, p50

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
MAQRGGARRP RGDRERLGSR LRALRPGREP RQSEPPAQRG PPPSGRPPAR
60 70 80 90 100
STASGHDRPT RGAAAGARRP RMKKKTRRRS TRSEELTRSE ELTLSEEATW
110 120 130 140 150
SEEATQSEEA TQGEEMNRSQ EVTRDEESTR SEEVTREEMA AAGLTVTVTH
160 170 180 190 200
SNEKHDLHVT SQQGSSEPVV QDLAQVVEEV IGVPQSFQKL IFKGKSLKEM
210 220 230 240 250
ETPLSALGIQ DGCRVMLIGK KNSPQEEVEL KKLKHLEKSV EKIADQLEEL
260 270 280 290 300
NKELTGIQQG FLPKDLQAEA LCKLDRRVKA TIEQFMKILE EIDTLILPEN
310 320 330 340
FKDSRLKRKG LVKKVQAFLA ECDTVEQNIC QETERLQSTN FALAE
Length:345
Mass (Da):38,779
Last modified:May 18, 2010 - v4
Checksum:i8B40EF078C66335F
GO
Isoform 2 (identifier: Q99933-2) [UniParc]FASTAAdd to basket

Also known as: BAG1V, HAPV

The sequence of this isoform differs from the canonical sequence as follows:
     302-345: KDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTNFALAE → PTLTLVLNEK

Note: Produced by alternative splicing.

Show »
Length:311
Mass (Da):34,866
Checksum:i1F94BA55E21694D3
GO
Isoform 3 (identifier: Q99933-3) [UniParc]FASTAAdd to basket

Also known as: BAG-1M, RAP46

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.

Note: Produced by alternative initiation at Met-72 of isoform 1.

Show »
Length:274
Mass (Da):31,117
Checksum:iC13E200ED63A2CF0
GO
Isoform 4 (identifier: Q99933-4) [UniParc]FASTAAdd to basket

Also known as: BAG-1, p32

The sequence of this isoform differs from the canonical sequence as follows:
     1-115: Missing.

Note: Produced by alternative initiation at Met-116 of isoform 1.

Show »
Length:230
Mass (Da):25,989
Checksum:iD4B34A8F54DE684D
GO

Sequence cautioni

The sequence AAD11467.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAD25045.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD96469.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAA84624.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAH72516.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAH72518.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAH72741.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAH72742.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW58515.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451G → R in AAC34258 (PubMed:8812483).Curated
Sequence conflicti45 – 451G → R in BAD96469 (Ref. 5) Curated
Sequence conflicti45 – 451G → R in AAH01936 (PubMed:15489334).Curated
Sequence conflicti45 – 451G → R in AAH14774 (PubMed:15489334).Curated
Sequence conflicti79 – 791R → F in AAD11467 (PubMed:8812483).Curated
Sequence conflicti84 – 841E → K in AAD11467 (PubMed:8812483).Curated
Sequence conflicti90 – 901E → K in AAD11467 (PubMed:8812483).Curated
Sequence conflicti245 – 2451D → N in AAD11467 (PubMed:8812483).Curated
Sequence conflicti293 – 2931D → H in AAD11467 (PubMed:8812483).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 115115Missing in isoform 4. CuratedVSP_038394Add
BLAST
Alternative sequencei1 – 7171Missing in isoform 3. CuratedVSP_038395Add
BLAST
Alternative sequencei302 – 34544KDSRL…FALAE → PTLTLVLNEK in isoform 2. 1 PublicationVSP_000453Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35491 mRNA. Translation: CAA84624.1. Different initiation.
U46917 mRNA. Translation: AAD11467.1. Different initiation.
AF022224 mRNA. Translation: AAC34258.1.
AF116273 mRNA. Translation: AAD25045.1. Different initiation.
AK222749 mRNA. Translation: BAD96469.1. Different initiation.
AL161445, AL356472 Genomic DNA. Translation: CAH72516.1. Sequence problems.
AL161445, AL356472 Genomic DNA. Translation: CAH72517.1.
AL161445, AL356472 Genomic DNA. Translation: CAH72518.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72741.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72742.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72743.1.
CH471071 Genomic DNA. Translation: EAW58514.1.
CH471071 Genomic DNA. Translation: EAW58515.1. Sequence problems.
BC001936 mRNA. Translation: AAH01936.2.
BC014774 mRNA. Translation: AAH14774.2.
CCDSiCCDS35004.1. [Q99933-1]
CCDS55301.1. [Q99933-4]
RefSeqiNP_001165886.1. NM_001172415.1. [Q99933-4]
NP_004314.5. NM_004323.5.
UniGeneiHs.377484.

Genome annotation databases

EnsembliENST00000379704; ENSP00000369026; ENSG00000107262. [Q99933-4]
GeneIDi573.
KEGGihsa:573.
UCSCiuc003zsi.3. human. [Q99933-1]

Polymorphism databases

DMDMi296439462.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35491 mRNA. Translation: CAA84624.1. Different initiation.
U46917 mRNA. Translation: AAD11467.1. Different initiation.
AF022224 mRNA. Translation: AAC34258.1.
AF116273 mRNA. Translation: AAD25045.1. Different initiation.
AK222749 mRNA. Translation: BAD96469.1. Different initiation.
AL161445, AL356472 Genomic DNA. Translation: CAH72516.1. Sequence problems.
AL161445, AL356472 Genomic DNA. Translation: CAH72517.1.
AL161445, AL356472 Genomic DNA. Translation: CAH72518.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72741.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72742.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72743.1.
CH471071 Genomic DNA. Translation: EAW58514.1.
CH471071 Genomic DNA. Translation: EAW58515.1. Sequence problems.
BC001936 mRNA. Translation: AAH01936.2.
BC014774 mRNA. Translation: AAH14774.2.
CCDSiCCDS35004.1. [Q99933-1]
CCDS55301.1. [Q99933-4]
RefSeqiNP_001165886.1. NM_001172415.1. [Q99933-4]
NP_004314.5. NM_004323.5.
UniGeneiHs.377484.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HX1X-ray1.90B222-334[»]
1WXVNMR-A144-222[»]
3FZFX-ray2.20B222-334[»]
3FZHX-ray2.00B222-334[»]
3FZKX-ray2.10B222-334[»]
3FZLX-ray2.20B222-334[»]
3FZMX-ray2.30B222-334[»]
3LDQX-ray1.90B222-334[»]
3M3ZX-ray2.10B222-334[»]
ProteinModelPortaliQ99933.
SMRiQ99933. Positions 140-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107049. 61 interactions.
DIPiDIP-3341N.
IntActiQ99933. 32 interactions.
MINTiMINT-189058.

PTM databases

PhosphoSiteiQ99933.

Polymorphism databases

DMDMi296439462.

Proteomic databases

MaxQBiQ99933.
PaxDbiQ99933.
PRIDEiQ99933.

Protocols and materials databases

DNASUi573.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379704; ENSP00000369026; ENSG00000107262. [Q99933-4]
GeneIDi573.
KEGGihsa:573.
UCSCiuc003zsi.3. human. [Q99933-1]

Organism-specific databases

CTDi573.
GeneCardsiGC09M033245.
HGNCiHGNC:937. BAG1.
HPAiCAB002486.
HPA018121.
MIMi601497. gene.
neXtProtiNX_Q99933.
PharmGKBiPA25237.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG72809.
GeneTreeiENSGT00450000040296.
HOVERGENiHBG000236.
InParanoidiQ99933.
KOiK09555.
PhylomeDBiQ99933.

Miscellaneous databases

ChiTaRSiBAG1. human.
EvolutionaryTraceiQ99933.
GeneWikiiBAG1.
GenomeRNAii573.
NextBioi2337.
PROiQ99933.
SOURCEiSearch...

Gene expression databases

BgeeiQ99933.
CleanExiHS_BAG1.
ExpressionAtlasiQ99933. baseline and differential.
GenevestigatoriQ99933.

Family and domain databases

Gene3Di1.20.58.120. 1 hit.
InterProiIPR003103. BAG_domain.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF02179. BAG. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00264. BAG. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS51035. BAG. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A protein that interacts with members of the nuclear hormone receptor family: identification and cDNA cloning."
    Zeiner M., Gehring U.
    Proc. Natl. Acad. Sci. U.S.A. 92:11465-11469(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Cloning of cDNAs encoding the human BAG1 protein and localization of the human BAG1 gene to chromosome 9p12."
    Takayama S., Kochel K., Irie S., Inazawa J., Abe T., Sato T., Druck T., Huebner K., Reed J.C.
    Genomics 35:494-498(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary gland.
  3. Takayama S.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO N-TERMINUS; 79; 84; 90; 245 AND 293.
  4. "Characterization of Hap/BAG-1 variants as RP1 binding proteins with antiapoptotic activity."
    Wadle A., Mischo A., Henrich P.P., Stenner-Lieven F., Scherer C., Imig J., Petersen G., Pfreundschuh M., Renner C.
    Int. J. Cancer 117:896-904(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ANTI-APOPTOTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH STK19.
    Tissue: T-cell.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Dermoid cancer.
  6. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Cervix and Lung.
  9. "Mammalian cells express two differently localized Bag-1 isoforms generated by alternative translation initiation."
    Packham G., Brimmell M., Cleveland J.L.
    Biochem. J. 328:807-813(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF ISOFORMS 1 AND 4, ALTERNATIVE INITIATION.
  10. Cited for: FUNCTION, SUBUNIT, INTERACTION WITH BCL2; HSP70 AND HSPA8.
  11. "Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines."
    Takayama S., Krajewski S., Krajewska M., Kitada S., Zapata J.M., Kochel K., Knee D., Scudiero D., Tudor G., Miller G.J., Miyashita T., Yamada M., Reed J.C.
    Cancer Res. 58:3116-3131(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF ISOFORMS 1; 3 AND 4, ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA8, INDUCTION, TISSUE SPECIFICITY.
  12. "p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1."
    Matsuzawa S., Takayama S., Froesch B.A., Zapata J.M., Reed J.C.
    EMBO J. 17:2736-2747(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIAH1.
  13. "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators."
    Takayama S., Xie Z., Reed J.C.
    J. Biol. Chem. 274:781-786(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity."
    Schneikert J., Huebner S., Martin E., Cato A.B.C.
    J. Cell Biol. 146:929-940(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR3C1.
  15. "Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions."
    Hung W.J., Roberson R.S., Taft J., Wu D.Y.
    Mol. Cell. Biol. 23:3477-3486(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R15A, FUNCTION.
  16. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors."
    Sondermann H., Scheufler C., Schneider C., Hohfeld J., Hartl F.U., Moarefi I.
    Science 291:1553-1557(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 222-334 IN COMPLEX WITH HSC70.
  19. "Solution structure of the ubiquitin domain of Bcl-2 binding athanogene-1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 143-223.

Entry informationi

Entry nameiBAG1_HUMAN
AccessioniPrimary (citable) accession number: Q99933
Secondary accession number(s): O75315
, Q14414, Q53H32, Q5VZE8, Q5VZE9, Q5VZF0, Q96TG2, Q9Y2V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: April 1, 2015
This is version 157 of the entry and version 4 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 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.