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Q99933 (BAG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence 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 does not interact with BCL2. Ref.4 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15

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 intumor 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 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 BAD96469.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSPA8P1114210EBI-1030678,EBI-351896

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345BAG family molecular chaperone regulator 1
PRO_0000088865

Regions

Repeat96 – 10161
Repeat102 – 10762
Repeat108 – 11363
Repeat114 – 11964
Repeat120 – 12565
Repeat126 – 13166
Repeat132 – 13767
Domain144 – 22481Ubiquitin-like
Domain246 – 32681BAG
Region96 – 137427 X 6 AA tandem repeat of E-E-X(4)
Region172 – 21948Interaction with HSPA8
Region216 – 345130Interaction with PPP1R15A
Compositional bias4 – 8279Arg-rich

Amino acid modifications

Modified residue2231Phosphoserine Ref.16

Natural variations

Alternative sequence1 – 115115Missing in isoform 4.
VSP_038394
Alternative sequence1 – 7171Missing in isoform 3.
VSP_038395
Alternative sequence302 – 34544KDSRL…FALAE → PTLTLVLNEK in isoform 2.
VSP_000453

Experimental info

Sequence conflict451G → R in AAC34258. Ref.2
Sequence conflict451G → R in BAD96469. Ref.5
Sequence conflict451G → R in AAH01936. Ref.8
Sequence conflict451G → R in AAH14774. Ref.8
Sequence conflict791R → F in AAD11467. Ref.2
Sequence conflict841E → K in AAD11467. Ref.2
Sequence conflict901E → K in AAD11467. Ref.2
Sequence conflict2451D → N in AAD11467. Ref.2
Sequence conflict2931D → H in AAD11467. Ref.2

Secondary structure

............................ 345
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (BAG-1L) (p50) [UniParc].

Last modified May 18, 2010. Version 4.
Checksum: 8B40EF078C66335F

FASTA34538,779
        10         20         30         40         50         60 
MAQRGGARRP RGDRERLGSR LRALRPGREP RQSEPPAQRG PPPSGRPPAR 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 

« Hide

Isoform 2 (BAG1V) (HAPV) [UniParc].

Checksum: 1F94BA55E21694D3
Show »

FASTA31134,866
Isoform 3 (BAG-1M) (RAP46) [UniParc].

Checksum: C13E200ED63A2CF0
Show »

FASTA27431,117
Isoform 4 (BAG-1) (p32) [UniParc].

Checksum: D4B34A8F54DE684D
Show »

FASTA23025,989

References

« Hide '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] [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. expand/collapse author list , 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]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. expand/collapse author list , 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] [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]"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] [Europe PMC] [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] [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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

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.
CCDSCCDS35004.1. [Q99933-1]
CCDS55301.1. [Q99933-4]
RefSeqNP_001165886.1. NM_001172415.1. [Q99933-4]
NP_004314.5. NM_004323.5.
UniGeneHs.377484.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ99933.
SMRQ99933. Positions 140-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107049. 48 interactions.
DIPDIP-3341N.
IntActQ99933. 12 interactions.
MINTMINT-189058.

PTM databases

PhosphoSiteQ99933.

Polymorphism databases

DMDM296439462.

Proteomic databases

MaxQBQ99933.
PaxDbQ99933.
PRIDEQ99933.

Protocols and materials databases

DNASU573.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379704; ENSP00000369026; ENSG00000107262. [Q99933-4]
GeneID573.
KEGGhsa:573.
UCSCuc003zsi.3. human. [Q99933-1]

Organism-specific databases

CTD573.
GeneCardsGC09M033245.
HGNCHGNC:937. BAG1.
HPACAB002486.
HPA018121.
MIM601497. gene.
neXtProtNX_Q99933.
PharmGKBPA25237.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72809.
HOVERGENHBG000236.
InParanoidQ99933.
KOK09555.
PhylomeDBQ99933.

Gene expression databases

ArrayExpressQ99933.
BgeeQ99933.
CleanExHS_BAG1.
GenevestigatorQ99933.

Family and domain databases

Gene3D1.20.58.120. 1 hit.
InterProIPR003103. BAG_domain.
IPR017093. Molecular_chp_reg_BAG_1.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF02179. BAG. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PIRSFPIRSF037029. BAG_1. 1 hit.
SMARTSM00264. BAG. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
PROSITEPS51035. BAG. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBAG1. human.
EvolutionaryTraceQ99933.
GeneWikiBAG1.
GenomeRNAi573.
NextBio2337.
PROQ99933.
SOURCESearch...

Entry information

Entry nameBAG1_HUMAN
AccessionPrimary (citable) accession number: Q99933
Secondary accession number(s): O75315 expand/collapse secondary AC list , Q14414, Q53H32, Q5VZE8, Q5VZE9, Q5VZF0, Q96TG2, Q9Y2V4
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM