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O95429

- BAG4_HUMAN

UniProt

O95429 - BAG4_HUMAN

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Protein

BAG family molecular chaperone regulator 4

Gene

BAG4

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

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. receptor signaling protein activity Source: ProtInc

GO - Biological processi

  1. cellular response to epidermal growth factor stimulus Source: Ensembl
  2. cellular response to tumor necrosis factor Source: UniProtKB
  3. intracellular signal transduction Source: GOC
  4. negative regulation of apoptotic process Source: ProtInc
  5. negative regulation of mRNA modification Source: Ensembl
  6. negative regulation of phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity Source: Ensembl
  7. positive regulation of actin filament polymerization Source: Ensembl
  8. positive regulation of cell adhesion Source: Ensembl
  9. positive regulation of fibroblast migration Source: Ensembl
  10. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  11. positive regulation of protein kinase B signaling Source: Ensembl
  12. positive regulation of stress fiber assembly Source: Ensembl
  13. protein folding Source: ProtInc
  14. protein heterooligomerization Source: Ensembl
  15. protein localization to plasma membrane Source: Ensembl
  16. ruffle assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

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: Chromosome 8

Organism-specific databases

HGNCiHGNC:940. BAG4.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. 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.

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.
GenevestigatoriO95429.

Organism-specific databases

HPAiCAB013716.
HPA018951.

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. 26 interactions.
MINTiMINT-209028.
STRINGi9606.ENSP00000287322.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiYTPGYTQ.
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. Align

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:
EMBL
GenBank
DDBJ
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. [O95429-1]
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS56533.1. [O95429-2 ]
CCDS6104.1. [O95429-1 ]
RefSeqi NP_001191807.1. NM_001204878.1. [O95429-2 ]
NP_004865.1. NM_004874.3. [O95429-1 ]
UniGenei Hs.194726.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M62 NMR - A 376-457 [» ]
1M7K NMR - A 358-456 [» ]
ProteinModelPortali O95429.
SMRi O95429. Positions 376-456.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114906. 34 interactions.
IntActi O95429. 26 interactions.
MINTi MINT-209028.
STRINGi 9606.ENSP00000287322.

PTM databases

PhosphoSitei O95429.

Proteomic databases

MaxQBi O95429.
PaxDbi O95429.
PRIDEi O95429.

Protocols and materials databases

DNASUi 9530.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000287322 ; ENSP00000287322 ; ENSG00000156735 . [O95429-1 ]
ENST00000432471 ; ENSP00000393298 ; ENSG00000156735 . [O95429-2 ]
GeneIDi 9530.
KEGGi hsa:9530.
UCSCi uc003xky.2. human. [O95429-1 ]
uc003xkz.2. human. [O95429-2 ]

Organism-specific databases

CTDi 9530.
GeneCardsi GC08P038051.
HGNCi HGNC:940. BAG4.
HPAi CAB013716.
HPA018951.
MIMi 603884. gene.
neXtProti NX_O95429.
PharmGKBi PA25240.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG275247.
GeneTreei ENSGT00530000063256.
HOGENOMi HOG000290673.
HOVERGENi HBG004809.
InParanoidi O95429.
KOi K09558.
OMAi YTPGYTQ.
OrthoDBi EOG75B85S.
PhylomeDBi O95429.
TreeFami TF102013.

Miscellaneous databases

EvolutionaryTracei O95429.
GeneWikii BAG4.
GenomeRNAii 9530.
NextBioi 35728.
PROi O95429.
SOURCEi Search...

Gene expression databases

Bgeei O95429.
CleanExi HS_BAG4.
ExpressionAtlasi O95429. baseline and differential.
Genevestigatori O95429.

Family and domain databases

Gene3Di 1.20.58.120. 1 hit.
InterProi IPR003103. BAG_domain.
[Graphical view ]
Pfami PF02179. BAG. 1 hit.
[Graphical view ]
SMARTi SM00264. BAG. 1 hit.
[Graphical view ]
PROSITEi PS51035. BAG. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. 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: October 29, 2014
This is version 129 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