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Q99933

- BAG1_HUMAN

UniProt

Q99933 - BAG1_HUMAN

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Protein

BAG family molecular chaperone regulator 1

Gene
BAG1, HAP
Organism
Homo sapiens (Human)
Status
Reviewed - 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. protein binding Source: UniProtKB
  2. 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: Chromosome 9

Organism-specific databases

HGNCiHGNC:937. BAG1.

Subcellular locationi

Isoform 1 : Nucleus. Cytoplasm
Note: Isoform 1 localizes predominantly to the nucleus.2 Publications
Isoform 2 : Cytoplasm. Nucleus
Note: Isoform 2 localizes to the cytoplasm and shuttles into the nucleus in response to heat shock.2 Publications
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.2 Publications

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 Inferred.

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

ArrayExpressiQ99933.
BgeeiQ99933.
CleanExiHS_BAG1.
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 BCL2.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPA8P1114210EBI-1030678,EBI-351896

Protein-protein interaction databases

BioGridi107049. 48 interactions.
DIPiDIP-3341N.
IntActiQ99933. 12 interactions.
MINTiMINT-189058.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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-likeAdd
BLAST
Domaini246 – 32681BAGAdd
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.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG72809.
HOVERGENiHBG000236.
InParanoidiQ99933.
KOiK09555.
PhylomeDBiQ99933.

Family and domain databases

Gene3Di1.20.58.120. 1 hit.
InterProiIPR003103. BAG_domain.
IPR017093. Molecular_chp_reg_BAG_1.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF02179. BAG. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PIRSFiPIRSF037029. BAG_1. 1 hit.
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. Align

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

MAQRGGARRP RGDRERLGSR LRALRPGREP RQSEPPAQRG PPPSGRPPAR    50
STASGHDRPT RGAAAGARRP RMKKKTRRRS TRSEELTRSE ELTLSEEATW 100
SEEATQSEEA TQGEEMNRSQ EVTRDEESTR SEEVTREEMA AAGLTVTVTH 150
SNEKHDLHVT SQQGSSEPVV QDLAQVVEEV IGVPQSFQKL IFKGKSLKEM 200
ETPLSALGIQ DGCRVMLIGK KNSPQEEVEL KKLKHLEKSV EKIADQLEEL 250
NKELTGIQQG FLPKDLQAEA LCKLDRRVKA TIEQFMKILE EIDTLILPEN 300
FKDSRLKRKG LVKKVQAFLA ECDTVEQNIC QETERLQSTN FALAE 345
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 BAD96469.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
The sequence AAD11467.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAD25045.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAA84624.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAH72516.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAH72518.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAH72741.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAH72742.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence EAW58515.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 115115Missing in isoform 4. VSP_038394Add
BLAST
Alternative sequencei1 – 7171Missing in isoform 3. VSP_038395Add
BLAST
Alternative sequencei302 – 34544KDSRL…FALAE → PTLTLVLNEK in isoform 2. VSP_000453Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451G → R in AAC34258. 1 Publication
Sequence conflicti45 – 451G → R in BAD96469. 1 Publication
Sequence conflicti45 – 451G → R in AAH01936. 1 Publication
Sequence conflicti45 – 451G → R in AAH14774. 1 Publication
Sequence conflicti79 – 791R → F in AAD11467. 1 Publication
Sequence conflicti84 – 841E → K in AAD11467. 1 Publication
Sequence conflicti90 – 901E → K in AAD11467. 1 Publication
Sequence conflicti245 – 2451D → N in AAD11467. 1 Publication
Sequence conflicti293 – 2931D → H in AAD11467. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS35004.1. [Q99933-1 ]
CCDS55301.1. [Q99933-4 ]
RefSeqi NP_001165886.1. NM_001172415.1. [Q99933-4 ]
NP_004314.5. NM_004323.5.
UniGenei Hs.377484.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HX1 X-ray 1.90 B 222-334 [» ]
1WXV NMR - A 144-222 [» ]
3FZF X-ray 2.20 B 222-334 [» ]
3FZH X-ray 2.00 B 222-334 [» ]
3FZK X-ray 2.10 B 222-334 [» ]
3FZL X-ray 2.20 B 222-334 [» ]
3FZM X-ray 2.30 B 222-334 [» ]
3LDQ X-ray 1.90 B 222-334 [» ]
3M3Z X-ray 2.10 B 222-334 [» ]
ProteinModelPortali Q99933.
SMRi Q99933. Positions 140-331.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107049. 48 interactions.
DIPi DIP-3341N.
IntActi Q99933. 12 interactions.
MINTi MINT-189058.

PTM databases

PhosphoSitei Q99933.

Polymorphism databases

DMDMi 296439462.

Proteomic databases

MaxQBi Q99933.
PaxDbi Q99933.
PRIDEi Q99933.

Protocols and materials databases

DNASUi 573.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379704 ; ENSP00000369026 ; ENSG00000107262 . [Q99933-4 ]
GeneIDi 573.
KEGGi hsa:573.
UCSCi uc003zsi.3. human. [Q99933-1 ]

Organism-specific databases

CTDi 573.
GeneCardsi GC09M033245.
HGNCi HGNC:937. BAG1.
HPAi CAB002486.
HPA018121.
MIMi 601497. gene.
neXtProti NX_Q99933.
PharmGKBi PA25237.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG72809.
HOVERGENi HBG000236.
InParanoidi Q99933.
KOi K09555.
PhylomeDBi Q99933.

Miscellaneous databases

ChiTaRSi BAG1. human.
EvolutionaryTracei Q99933.
GeneWikii BAG1.
GenomeRNAii 573.
NextBioi 2337.
PROi Q99933.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99933.
Bgeei Q99933.
CleanExi HS_BAG1.
Genevestigatori Q99933.

Family and domain databases

Gene3Di 1.20.58.120. 1 hit.
InterProi IPR003103. BAG_domain.
IPR017093. Molecular_chp_reg_BAG_1.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF02179. BAG. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view ]
PIRSFi PIRSF037029. BAG_1. 1 hit.
SMARTi SM00264. BAG. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS51035. BAG. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1995) [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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary gland.
  3. Takayama S.
    Submitted (SEP-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(2005) [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 (APR-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(2004) [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(2004) [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(1997) [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(1998) [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(1998) [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(1999) [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(1999) [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(2003) [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(2010) [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(2001) [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 (AUG-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: July 9, 2014
This is version 150 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

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