Reviewed, UniProtKB/Swiss-Prot Q99933 (BAG1_HUMAN)

Names and origin

Protein names

Recommended name:
    BAG family molecular chaperone regulator 1
      Short name=BAG-1
Alternative name(s):
    Bcl-2-associated athanogene 1

Gene names

Name:	BAG1
Synonyms:	HAP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.10 Ref.13 Ref.15
Subunit structure	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 doesn't interact with BCL2. Ref.10 Ref.15 Ref.4 Ref.11 Ref.12 Ref.14
Subcellular location	Isoform 1: Nucleus. Cytoplasm. Note: Isoform 1 localizes predominantly to the nucleus. Ref.4 Ref.11 Isoform 2: Cytoplasm. Nucleus. Note: Isoform 2 localizes to the cytoplasm and shuttles into the nucleus in response to heat shock. Ref.4 Ref.11 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. Ref.4 Ref.11
Tissue specificity	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). Ref.11
Induction	Up-regulated during differentiation of bladder epithelial cells and down-regulated during differentiation of prostate epithelium. Ref.11
Post-translational modification	Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation Probable.
Sequence similarities	Contains 1 BAG domain. Contains 1 ubiquitin-like domain.
Sequence caution	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.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative initiation Alternative splicing
Domain	Repeat
Molecular function	Chaperone
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: ProtInc apoptosis Inferred from electronic annotation. Source: UniProtKB-KW cell surface receptor linked signal transduction Traceable author statement. Source: ProtInc
Cellular component	cytoskeleton Inferred from direct assay. Source: HPA nucleus Ref.11 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Ref.10 Ref.16 Inferred from physical interaction. Source: UniProtKB receptor signaling protein activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSPA8	P19120	1	EBI-1030678,EBI-907802	From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Isoform 1 (identifier: Q99933-1)

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.

Note: Isoform 1 localizes predominantly to the nucleus. Ref.4 Ref.11

Isoform 2 (identifier: Q99933-2)

Also known as: BAG1V; HAPV;

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

Note: Isoform 2 localizes to the cytoplasm and shuttles into the nucleus in response to heat shock. Ref.4 Ref.11 Produced by alternative splicing.

Isoform 3 (identifier: Q99933-3)

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.

Isoform 4 (identifier: Q99933-4)

Also known as: BAG-1; p32;

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

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. Ref.4 Ref.11 Produced by alternative initiation at Met-116 of isoform 1.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 345

345

BAG family molecular chaperone regulator 1

PRO_0000088865

Regions

Repeat

96 – 101

6

1

Repeat

102 – 107

6

2

Repeat

108 – 113

6

3

Repeat

114 – 119

6

4

Repeat

120 – 125

6

5

Repeat

126 – 131

6

6

Repeat

132 – 137

6

7

Domain

144 – 224

81

Ubiquitin-like

Domain

246 – 326

81

BAG

Region

96 – 137

42

7 X 6 AA tandem repeat of E-E-X(4)

Region

172 – 219

48

Interaction with HSPA8

Region

216 – 345

130

Interaction with PPP1R15A

Compositional bias

4 – 82

79

Arg-rich

Natural variations

Alternative sequence

1 – 115

115

Missing in isoform 4.

VSP_038394

Alternative sequence

1 – 71

71

Missing in isoform 3.

VSP_038395

Alternative sequence

302 – 345

44

KDSRL…FALAE → PTLTLVLNEK in isoform 2.

VSP_000453

Experimental info

Sequence conflict

79

1

R → F in AAD11467. Ref.2

Sequence conflict

84

1

E → K in AAD11467. Ref.2

Sequence conflict

90

1

E → K in AAD11467. Ref.2

Sequence conflict

245

1

D → N in AAD11467. Ref.2

Sequence conflict

293

1

D → H in AAD11467. Ref.2

Secondary structure

1

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345

Helix Strand Turn

Details...

Beta strand

72 – 78

7

Beta strand

80 – 88

9

Beta strand

92 – 96

5

Helix

99 – 109

11

Turn

114 – 116

3

Beta strand

118 – 121

4

Beta strand

124 – 126

3

Beta strand

129 – 132

4

Helix

133 – 136

4

Beta strand

140 – 148

9

Helix

224 – 259

36

Helix

264 – 272

9

Helix

275 – 292

18

Helix

302 – 326

25

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (BAG-1L) (p50) [UniParc]. Last modified November 28, 2006. Version 3. Checksum: 9895EF082D73335B	FASTA	345	38,878
	10 20 30 40 50 60 MAQRGGARRP RGDRERLGSR LRALRPGREP RQSEPPAQRG PPPSRRPPAR STASGHDRPT 70 80 90 100 110 120 RGAAAGARRP RMKKKTRRRS TRSEELTRSE ELTLSEEATW SEEATQSEEA TQGEEMNRSQ 130 140 150 160 170 180 EVTRDEESTR SEEVTREEMA AAGLTVTVTH SNEKHDLHVT SQQGSSEPVV QDLAQVVEEV 190 200 210 220 230 240 IGVPQSFQKL IFKGKSLKEM ETPLSALGIQ DGCRVMLIGK KNSPQEEVEL KKLKHLEKSV 250 260 270 280 290 300 EKIADQLEEL NKELTGIQQG FLPKDLQAEA LCKLDRRVKA TIEQFMKILE EIDTLILPEN 310 320 330 340 FKDSRLKRKG LVKKVQAFLA ECDTVEQNIC QETERLQSTN FALAE
	Isoform 2 (BAG1V) (HAPV). Checksum: EA94BE05A7169FD3	FASTA	311	34,965
	10 20 30 40 50 60 MAQRGGARRP RGDRERLGSR LRALRPGREP RQSEPPAQRG PPPSRRPPAR STASGHDRPT 70 80 90 100 110 120 RGAAAGARRP RMKKKTRRRS TRSEELTRSE ELTLSEEATW SEEATQSEEA TQGEEMNRSQ 130 140 150 160 170 180 EVTRDEESTR SEEVTREEMA AAGLTVTVTH SNEKHDLHVT SQQGSSEPVV QDLAQVVEEV 190 200 210 220 230 240 IGVPQSFQKL IFKGKSLKEM ETPLSALGIQ DGCRVMLIGK KNSPQEEVEL KKLKHLEKSV 250 260 270 280 290 300 EKIADQLEEL NKELTGIQQG FLPKDLQAEA LCKLDRRVKA TIEQFMKILE EIDTLILPEN 310 FPTLTLVLNE K
	Isoform 3 (BAG-1M) (RAP46). Checksum: C13E200ED63A2CF0	FASTA	274	31,117
	10 20 30 40 50 60 MKKKTRRRST RSEELTRSEE LTLSEEATWS EEATQSEEAT QGEEMNRSQE VTRDEESTRS 70 80 90 100 110 120 EEVTREEMAA AGLTVTVTHS NEKHDLHVTS QQGSSEPVVQ DLAQVVEEVI GVPQSFQKLI 130 140 150 160 170 180 FKGKSLKEME TPLSALGIQD GCRVMLIGKK NSPQEEVELK KLKHLEKSVE KIADQLEELN 190 200 210 220 230 240 KELTGIQQGF LPKDLQAEAL CKLDRRVKAT IEQFMKILEE IDTLILPENF KDSRLKRKGL 250 260 270 VKKVQAFLAE CDTVEQNICQ ETERLQSTNF ALAE
	Isoform 4 (BAG-1) (p32). Checksum: D4B34A8F54DE684D	FASTA	230	25,989
	10 20 30 40 50 60 MNRSQEVTRD EESTRSEEVT REEMAAAGLT VTVTHSNEKH DLHVTSQQGS SEPVVQDLAQ 70 80 90 100 110 120 VVEEVIGVPQ SFQKLIFKGK SLKEMETPLS ALGIQDGCRV MLIGKKNSPQ EEVELKKLKH 130 140 150 160 170 180 LEKSVEKIAD QLEELNKELT GIQQGFLPKD LQAEALCKLD RRVKATIEQF MKILEEIDTL 190 200 210 220 230 ILPENFKDSR LKRKGLVKKV QAFLAECDTV EQNICQETER LQSTNFALAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8524784] [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: 8812483] [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: 15986447] [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: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 9396724] [Abstract] Cited for: IDENTIFICATION OF ISOFORMS 1 AND 4, ALTERNATIVE INITIATION.
[10]	"BAG-1 modulates the chaperone activity of Hsp70/Hsc70." Takayama S., Bimston D.N., Matsuzawa S.-I., Freeman B.C., Aime-Sempe C., Xie Z., Morimoto R.I., Reed J.C. EMBO J. 16:4887-4896(1997) [PubMed: 9305631] [Abstract] 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: 9679980] [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: 9582267] [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: 9873016] [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: 10477749] [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: 12724406] [Abstract] Cited for: INTERACTION WITH PPP1R15A, FUNCTION.
[16]	"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: 11222862] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 222-334 IN COMPLEX WITH HSC70.
[17]	"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 72-152.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00218546.
IPI00300531.
IPI00641336.
IPI00954014.

UniGene

Hs.377484

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HX1	X-ray	1.90	B	222-334	[»]
1WXV	NMR	-	A	143-223	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3341N.

IntAct

Q99933. 2 interactions.

STRING

Q99933.

Proteomic databases

PRIDE

Q99933.

Genome annotation databases

Ensembl

ENST00000224112; ENSP00000224112; ENSG00000107262; Homo sapiens. [Genome view]

Organism-specific databases

GeneCards

GC09M033245.

H-InvDB

HIX0007978.
HIX0080318.

HGNC

HGNC:937. BAG1.

HPA

CAB002486.
HPA018121.

MIM

601497. gene.

PharmGKB

PA25237.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12631.

HOGENOM

HBG445922.

HOVERGEN

Q99933.

InParanoid

Q99933.

Enzyme and pathway databases

Pathway_Interaction_DB

met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).

Gene expression databases

ArrayExpress

Q99933.

Bgee

Q99933.

CleanEx

HS_BAG1.

Genevestigator

Q99933.

GermOnline

ENSG00000107262. Homo sapiens.

Family and domain databases

InterPro

IPR003103. Apoptosis_reg_Bcl-2_prot_BAG.
IPR017093. Molecular_chp_reg_BAG_1.
IPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
[Graphical view]

Pfam

PF02179. BAG. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]

PIRSF

PIRSF037029. BAG_1. 1 hit.

SMART

SM00264. BAG. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]

PROSITE

PS51035. BAG. 1 hit.
PS00299. UBIQUITIN_1. False negative.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

BAG1_HUMAN

Accession

Primary (citable) accession number: Q99933
Secondary accession number(s): O75315 , Q14414, Q53H32, Q5VZE8, Q5VZE9, Q5VZF0, Q96TG2, Q9Y2V4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 28, 2006
Last modified:	February 9, 2010
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.