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Protein

BAG family molecular chaperone regulator 4

Gene

BAG4

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 (By similarity). Prevents constitutive TNFRSF1A signaling. Negative regulator of PARK2 translocation to damaged mitochondria.By similarity1 Publication

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • receptor signaling protein activity Source: ProtInc
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiREACT_1432. TNF signaling.
REACT_264487. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
BAG family molecular chaperone regulator 4
Short name:
BAG-4
Alternative name(s):
Bcl-2-associated athanogene 4
Silencer of death domains
Gene namesi
Name:BAG4
Synonyms:SODD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:940. BAG4.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi414 – 4141E → A: Reduces interaction with HSP70. 1 Publication
Mutagenesisi424 – 4241D → A: Abolishes interaction with HSP70. 1 Publication
Mutagenesisi438 – 4392RK → AA: Reduces interaction with HSP70. 1 Publication
Mutagenesisi446 – 4461Q → A: Abolishes interaction with HSP70. 1 Publication

Organism-specific databases

PharmGKBiPA25240.

Polymorphism and mutation databases

BioMutaiBAG4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457BAG family molecular chaperone regulator 4PRO_0000088870Add
BLAST

Proteomic databases

MaxQBiO95429.
PaxDbiO95429.
PRIDEiO95429.

PTM databases

PhosphoSiteiO95429.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO95429.
CleanExiHS_BAG4.
ExpressionAtlasiO95429. baseline and differential.
GenevisibleiO95429. HS.

Organism-specific databases

HPAiCAB013716.
HPA018951.
HPA048818.

Interactioni

Subunit structurei

Binds to the ATPase domain of HSP/HSC70 chaperones. Binds to the death domain of TNFRSF1A in the absence of TNF and thereby prevents binding of adapter molecules such as TRADD or TRAF2. Binds to the death domain of TNFRSF12. Interacts with PARK2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q53FC72EBI-2949658,EBI-9356749
DCP1AQ9NPI63EBI-2949658,EBI-374238
DNAJC7Q996152EBI-2949658,EBI-357552
HSPA2P546522EBI-2949658,EBI-356991

Protein-protein interaction databases

BioGridi114906. 34 interactions.
IntActiO95429. 54 interactions.
MINTiMINT-209028.
STRINGi9606.ENSP00000287322.

Structurei

Secondary structure

1
457
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi380 – 39920Combined sources
Helixi407 – 42317Combined sources
Helixi432 – 45625Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M62NMR-A376-457[»]
1M7KNMR-A358-456[»]
ProteinModelPortaliO95429.
SMRiO95429. Positions 376-456.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95429.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini379 – 45678BAGPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 BAG domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG275247.
GeneTreeiENSGT00530000063256.
HOGENOMiHOG000290673.
HOVERGENiHBG004809.
InParanoidiO95429.
KOiK09558.
OMAiPAETTWP.
OrthoDBiEOG75B85S.
PhylomeDBiO95429.
TreeFamiTF102013.

Family and domain databases

Gene3Di1.20.58.120. 1 hit.
InterProiIPR003103. BAG_domain.
[Graphical view]
PfamiPF02179. BAG. 1 hit.
[Graphical view]
SMARTiSM00264. BAG. 1 hit.
[Graphical view]
PROSITEiPS51035. BAG. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95429-1) [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
MSALRRSGYG PSDGPSYGRY YGPGGGDVPV HPPPPLYPLR PEPPQPPISW
60 70 80 90 100
RVRGGGPAET TWLGEGGGGD GYYPSGGAWP EPGRAGGSHQ EQPPYPSYNS
110 120 130 140 150
NYWNSTARSR APYPSTYPVR PELQGQSLNS YTNGAYGPTY PPGPGANTAS
160 170 180 190 200
YSGAYYAPGY TQTSYSTEVP STYRSSGNSP TPVSRWIYPQ QDCQTEAPPL
210 220 230 240 250
RGQVPGYPPS QNPGMTLPHY PYGDGNRSVP QSGPTVRPQE DAWASPGAYG
260 270 280 290 300
MGGRYPWPSS APSAPPGNLY MTESTSPWPS SGSPQSPPSP PVQQPKDSSY
310 320 330 340 350
PYSQSDQSMN RHNFPCSVHQ YESSGTVNND DSDLLDSQVQ YSAEPQLYGN
360 370 380 390 400
ATSDHPNNQD QSSSLPEECV PSDESTPPSI KKIIHVLEKV QYLEQEVEEF
410 420 430 440 450
VGKKTDKAYW LLEEMLTKEL LELDSVETGG QDSVRQARKE AVCKIQAILE

KLEKKGL
Length:457
Mass (Da):49,594
Last modified:May 1, 1999 - v1
Checksum:iB89D59E8118684A3
GO
Isoform 2 (identifier: O95429-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     90-125: Missing.

Note: No experimental confirmation available.
Show »
Length:421
Mass (Da):45,410
Checksum:i3E39EF28E280E94A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei90 – 12536Missing in isoform 2. 1 PublicationVSP_042741Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095194 mRNA. Translation: AAD16123.2.
AF111116 mRNA. Translation: AAD05226.1.
AK304072 mRNA. Translation: BAG64979.1.
AC084024 Genomic DNA. No translation available.
BC038505 mRNA. Translation: AAH38505.2.
CCDSiCCDS56533.1. [O95429-2]
CCDS6104.1. [O95429-1]
RefSeqiNP_001191807.1. NM_001204878.1. [O95429-2]
NP_004865.1. NM_004874.3. [O95429-1]
UniGeneiHs.194726.

Genome annotation databases

EnsembliENST00000287322; ENSP00000287322; ENSG00000156735.
ENST00000432471; ENSP00000393298; ENSG00000156735. [O95429-2]
GeneIDi9530.
KEGGihsa:9530.
UCSCiuc003xky.2. human. [O95429-1]
uc003xkz.2. human. [O95429-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095194 mRNA. Translation: AAD16123.2.
AF111116 mRNA. Translation: AAD05226.1.
AK304072 mRNA. Translation: BAG64979.1.
AC084024 Genomic DNA. No translation available.
BC038505 mRNA. Translation: AAH38505.2.
CCDSiCCDS56533.1. [O95429-2]
CCDS6104.1. [O95429-1]
RefSeqiNP_001191807.1. NM_001204878.1. [O95429-2]
NP_004865.1. NM_004874.3. [O95429-1]
UniGeneiHs.194726.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M62NMR-A376-457[»]
1M7KNMR-A358-456[»]
ProteinModelPortaliO95429.
SMRiO95429. Positions 376-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114906. 34 interactions.
IntActiO95429. 54 interactions.
MINTiMINT-209028.
STRINGi9606.ENSP00000287322.

PTM databases

PhosphoSiteiO95429.

Polymorphism and mutation databases

BioMutaiBAG4.

Proteomic databases

MaxQBiO95429.
PaxDbiO95429.
PRIDEiO95429.

Protocols and materials databases

DNASUi9530.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000287322; ENSP00000287322; ENSG00000156735.
ENST00000432471; ENSP00000393298; ENSG00000156735. [O95429-2]
GeneIDi9530.
KEGGihsa:9530.
UCSCiuc003xky.2. human. [O95429-1]
uc003xkz.2. human. [O95429-2]

Organism-specific databases

CTDi9530.
GeneCardsiGC08P038051.
HGNCiHGNC:940. BAG4.
HPAiCAB013716.
HPA018951.
HPA048818.
MIMi603884. gene.
neXtProtiNX_O95429.
PharmGKBiPA25240.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG275247.
GeneTreeiENSGT00530000063256.
HOGENOMiHOG000290673.
HOVERGENiHBG004809.
InParanoidiO95429.
KOiK09558.
OMAiPAETTWP.
OrthoDBiEOG75B85S.
PhylomeDBiO95429.
TreeFamiTF102013.

Enzyme and pathway databases

ReactomeiREACT_1432. TNF signaling.
REACT_264487. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

EvolutionaryTraceiO95429.
GeneWikiiBAG4.
GenomeRNAii9530.
NextBioi35728.
PROiO95429.
SOURCEiSearch...

Gene expression databases

BgeeiO95429.
CleanExiHS_BAG4.
ExpressionAtlasiO95429. baseline and differential.
GenevisibleiO95429. HS.

Family and domain databases

Gene3Di1.20.58.120. 1 hit.
InterProiIPR003103. BAG_domain.
[Graphical view]
PfamiPF02179. BAG. 1 hit.
[Graphical view]
SMARTiSM00264. BAG. 1 hit.
[Graphical view]
PROSITEiPS51035. BAG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Leukemic T-cell.
  2. "Prevention of constitutive TNF receptor 1 signaling by silencer of death domains."
    Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.
    Science 283:543-546(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TNFRSF1A AND TNFRSF12.
    Tissue: Leukemic T-cell.
  3. Erratum
    Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.
    Science 283:1852-1852(1999)
  4. "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] (ISOFORM 2).
    Tissue: Trachea.
  5. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Brain.
  7. "High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy."
    Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.
    Nature 504:291-295(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PARK2.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: STRUCTURE BY NMR OF 376-457, INTERACTION WITH HSP70, MUTAGENESIS OF GLU-414; ASP-424; 438-ARG-LYS-439 AND GLN-446.

Entry informationi

Entry nameiBAG4_HUMAN
AccessioniPrimary (citable) accession number: O95429
Secondary accession number(s): B4E217, O95818
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1999
Last modified: July 22, 2015
This is version 137 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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.