Q9BZP6 (CHIA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acidic mammalian chitinase
Short name=AMCase
EC=3.2.1.14

Alternative name(s):
Lung-specific protein TSA1902

Gene names

Name:

CHIA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding. Ref.2 Ref.7 Ref.8 Ref.10
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Ref.7 Ref.9 Ref.10
Subunit structure	Interacts with EGFR. Ref.7
Subcellular location	Isoform 1: Secreted. Note: Secretion depends on EGFR activity. Ref.7 Isoform 2: Cytoplasm Ref.7. Isoform 3: Cytoplasm Ref.7.
Tissue specificity	Detected in lung epithelial cells from asthma patients (at protein level). Highly expressed in stomach. Detected at lower levels in lung. Ref.2 Ref.6
Induction	Up-regulated in lung epithelial cells from asthma patients. Ref.6
Sequence similarities	Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily. Contains 1 chitin-binding type-2 domain.

Ontologies

Keywords
Biological process	Apoptosis Carbohydrate metabolism Chitin degradation Immunity Inflammatory response Polysaccharide degradation
Cellular component	Cytoplasm Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell wall chitin metabolic process Traceable author statement Ref.2. Source: UniProtKB chitin catabolic process Inferred from direct assay Ref.10. Source: UniProtKB digestion Non-traceable author statement Ref.2. Source: UniProtKB immune response Non-traceable author statement Ref.2. Source: UniProtKB polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of chemokine secretion Inferred from direct assay Ref.7. Source: UniProtKB production of molecular mediator involved in inflammatory response Inferred from direct assay Ref.7. Source: UniProtKB response to acid Traceable author statement Ref.2. Source: UniProtKB response to fungus Traceable author statement Ref.2. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	carbohydrate binding Non-traceable author statement Ref.2. Source: UniProtKB chitin binding Traceable author statement Ref.2. Source: UniProtKB chitinase activity Inferred from direct assay Ref.2Ref.10. Source: UniProtKB lysozyme activity Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BZP6-1)

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: Q9BZP6-2)

Also known as: TSA1902-L;

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.

Isoform 3 (identifier: Q9BZP6-3)

Also known as: TSA1902-S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

By similarity

Chain

22 – 476

455

Acidic mammalian chitinase

PRO_0000011944

Regions

Domain

427 – 476

50

Chitin-binding type-2

Region

70 – 71

2

Chitooligosaccharide binding Probable

Region

97 – 100

4

Chitooligosaccharide binding Probable

Region

210 – 213

4

Chitooligosaccharide binding Probable

Compositional bias

415 – 420

6

Poly-Ser

Sites

Active site

140

1

Proton donor Probable

Binding site

141

1

Chitooligosaccharide By similarity

Binding site

360

1

Chitooligosaccharide By similarity

Amino acid modifications

Disulfide bond

26 ↔ 51

Ref.9

Disulfide bond

49 ↔ 394

Ref.9

Disulfide bond

307 ↔ 372

Ref.9

Natural variations

Alternative sequence

1 – 161

161

Missing in isoform 3.

VSP_008634

Alternative sequence

1 – 108

108

Missing in isoform 2.

VSP_008635

Natural variant

45

1

N → D Increased chitinase activity; when associated with N-47 and M-61. Ref.10
Corresponds to variant rs41282492 [ dbSNP | Ensembl ].

VAR_063030

Natural variant

47

1

D → N Increased chitinase activity; when associated with N-47 and M-61. Ref.10
Corresponds to variant rs41282494 [ dbSNP | Ensembl ].

VAR_063031

Natural variant

61

1

R → M Increased chitinase activity; when associated with N-47 and M-61. Ref.10
Corresponds to variant rs41282496 [ dbSNP | Ensembl ].

VAR_063032

Natural variant

102

1

G → R. Ref.10
Corresponds to variant rs3818822 [ dbSNP | Ensembl ].

VAR_049192

Natural variant

125

1

K → R. Ref.10

VAR_063033

Natural variant

324

1

V → G.
Corresponds to variant rs2256721 [ dbSNP | Ensembl ].

VAR_033730

Natural variant

339

1

I → V. Ref.1 Ref.10
Corresponds to variant rs2275253 [ dbSNP | Ensembl ].

VAR_049193

Natural variant

354

1

F → S. Ref.10
Corresponds to variant rs2275254 [ dbSNP | Ensembl ].

VAR_049194

Natural variant

377

1

F → L.
Corresponds to variant rs36011905 [ dbSNP | Ensembl ].

VAR_049195

Natural variant

432

1

V → G. Ref.1 Ref.10
Corresponds to variant rs2256721 [ dbSNP | Ensembl ].

VAR_049196

Experimental info

Mutagenesis

138

1

D → A: Loss of chitinase activity. No effect on protection against apoptosis or on AKT1 activation. Ref.8

Sequence conflict

203

1

Y → C in AAX81431. Ref.3

Secondary structure

1

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476

Helix Strand Turn

Details...

Beta strand

23 – 29

7

Helix

32 – 34

3

Helix

37 – 39

3

Helix

43 – 45

3

Turn

48 – 50

3

Beta strand

52 – 62

11

Beta strand

65 – 67

3

Helix

73 – 82

10

Helix

83 – 85

3

Beta strand

91 – 97

7

Helix

99 – 101

3

Helix

104 – 110

7

Helix

113 – 130

18

Beta strand

133 – 138

6

Helix

151 – 173

23

Beta strand

179 – 184

6

Helix

188 – 194

7

Helix

197 – 203

7

Beta strand

205 – 209

5

Helix

217 – 219

3

Helix

236 – 240

5

Helix

243 – 252

10

Helix

257 – 259

3

Beta strand

260 – 275

16

Beta strand

284 – 288

5

Turn

293 – 295

3

Beta strand

300 – 302

3

Helix

303 – 311

9

Beta strand

315 – 319

5

Turn

320 – 323

4

Beta strand

324 – 329

6

Beta strand

332 – 335

4

Helix

339 – 351

13

Beta strand

355 – 360

6

Helix

362 – 364

3

Beta strand

367 – 369

3

Turn

370 – 372

3

Helix

378 – 386

9

Helix

392 – 394

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 92B27BAD2F7EB4CC	FASTA	476	52,271
	10 20 30 40 50 60 MTKLILLTGL VLILNLQLGS AYQLTCYFTN WAQYRPGLGR FMPDNIDPCL CTHLIYAFAG 70 80 90 100 110 120 RQNNEITTIE WNDVTLYQAF NGLKNKNSQL KTLLAIGGWN FGTAPFTAMV STPENRQTFI 130 140 150 160 170 180 TSVIKFLRQY EFDGLDFDWE YPGSRGSPPQ DKHLFTVLVQ EMREAFEQEA KQINKPRLMV 190 200 210 220 230 240 TAAVAAGISN IQSGYEIPQL SQYLDYIHVM TYDLHGSWEG YTGENSPLYK YPTDTGSNAY 250 260 270 280 290 300 LNVDYVMNYW KDNGAPAEKL IVGFPTYGHN FILSNPSNTG IGAPTSGAGP AGPYAKESGI 310 320 330 340 350 360 WAYYEICTFL KNGATQGWDA PQEVPYAYQG NVWVGYDNIK SFDIKAQWLK HNKFGGAMVW 370 380 390 400 410 420 AIDLDDFTGT FCNQGKFPLI STLKKALGLQ SASCTAPAQP IEPITAAPSG SGNGSGSSSS 430 440 450 460 470 GGSSGGSGFC AVRANGLYPV ANNRNAFWHC VNGVTYQQNC QAGLVFDTSC DCCNWA
	Isoform 2 (TSA1902-L) [UniParc]. Checksum: FC2558C4CEA48609	FASTA	368	40,139
	10 20 30 40 50 60 MVSTPENRQT FITSVIKFLR QYEFDGLDFD WEYPGSRGSP PQDKHLFTVL VQEMREAFEQ 70 80 90 100 110 120 EAKQINKPRL MVTAAVAAGI SNIQSGYEIP QLSQYLDYIH VMTYDLHGSW EGYTGENSPL 130 140 150 160 170 180 YKYPTDTGSN AYLNVDYVMN YWKDNGAPAE KLIVGFPTYG HNFILSNPSN TGIGAPTSGA 190 200 210 220 230 240 GPAGPYAKES GIWAYYEICT FLKNGATQGW DAPQEVPYAY QGNVWVGYDN IKSFDIKAQW 250 260 270 280 290 300 LKHNKFGGAM VWAIDLDDFT GTFCNQGKFP LISTLKKALG LQSASCTAPA QPIEPITAAP 310 320 330 340 350 360 SGSGNGSGSS SSGGSSGGSG FCAVRANGLY PVANNRNAFW HCVNGVTYQQ NCQAGLVFDT SCDCCNWA
	Isoform 3 (TSA1902-S) [UniParc]. Checksum: 61D614709B577CAD	FASTA	315	33,906
	10 20 30 40 50 60 MREAFEQEAK QINKPRLMVT AAVAAGISNI QSGYEIPQLS QYLDYIHVMT YDLHGSWEGY 70 80 90 100 110 120 TGENSPLYKY PTDTGSNAYL NVDYVMNYWK DNGAPAEKLI VGFPTYGHNF ILSNPSNTGI 130 140 150 160 170 180 GAPTSGAGPA GPYAKESGIW AYYEICTFLK NGATQGWDAP QEVPYAYQGN VWVGYDNIKS 190 200 210 220 230 240 FDIKAQWLKH NKFGGAMVWA IDLDDFTGTF CNQGKFPLIS TLKKALGLQS ASCTAPAQPI 250 260 270 280 290 300 EPITAAPSGS GNGSGSSSSG GSSGGSGFCA VRANGLYPVA NNRNAFWHCV NGVTYQQNCQ 310 AGLVFDTSCD CCNWA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and mapping of a human lung-specific gene, TSA1902, encoding a novel chitinase family member." Saito A., Ozaki K., Fujiwara T., Nakamura Y., Tanigami A. Gene 239:325-331(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANTS VAL-339 AND GLY-432. Tissue: Lung.
[2]	"Identification of a novel acidic mammalian chitinase distinct from chitotriosidase." Boot R.G., Blommaart E.F.C., Swart E., Ghauharali-van der Vlugt K., Bijl N., Moe C., Place A., Aerts J.M.F.G. J. Biol. Chem. 276:6770-6778(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[3]	"A novel chitinase family member." Chen X.H., Cai G.P. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). Tissue: Kidney.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 2).
[6]	"Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation." Zhu Z., Zheng T., Homer R.J., Kim Y.K., Chen N.Y., Cohn L., Hamid Q., Elias J.A. Science 304:1678-1682(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, TISSUE SPECIFICITY.
[7]	"Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth factor receptor-dependent pathway and stimulates chemokine production by pulmonary epithelial cells." Hartl D., He C.H., Koller B., Da Silva C.A., Homer R., Lee C.G., Elias J.A. J. Biol. Chem. 283:33472-33482(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EGFR, SUBCELLULAR LOCATION.
[8]	"Acidic mammalian chitinase regulates epithelial cell apoptosis via a chitinolytic-independent mechanism." Hartl D., He C.H., Koller B., Da Silva C.A., Kobayashi Y., Lee C.G., Flavell R.A., Elias J.A. J. Immunol. 182:5098-5106(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-138.
[9]	"Triad of polar residues implicated in pH specificity of acidic mammalian chitinase." Olland A.M., Strand J., Presman E., Czerwinski R., Joseph-McCarthy D., Krykbaev R., Schlingmann G., Chopra R., Lin L., Fleming M., Kriz R., Stahl M., Somers W., Fitz L., Mosyak L. Protein Sci. 18:569-578(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-408 IN COMPLEX WITH METHYLALLOSAMIDIN, CATALYTIC ACTIVITY, DISULFIDE BONDS.
[10]	"Differential enzymatic activity of common haplotypic versions of the human acidic mammalian chitinase protein." Seibold M.A., Reese T.A., Choudhry S., Salam M.T., Beckman K., Eng C., Atakilit A., Meade K., Lenoir M., Watson H.G., Thyne S., Kumar R., Weiss K.B., Grammer L.C., Avila P., Schleimer R.P., Fahy J.V., Rodriguez-Santana J. , Rodriguez-Cintron W., Boot R.G., Sheppard D., Gilliland F.D., Locksley R.M., Burchard E.G. J. Biol. Chem. 284:19650-19658(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ASP-45; ASN-47; MET-61; ARG-102; ARG-125; VAL-339; SER-354 AND GLY-432, CATALYTIC ACTIVITY, FUNCTION, CHARACTERIZATION OF VARIANTS ASP-45; ASN-47 AND MET-61.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB025008 mRNA. Translation: BAA86980.1.
AB025009 mRNA. Translation: BAA86981.1.
AF290004 mRNA. Translation: AAG60019.1.
AY789444 mRNA. Translation: AAX81431.1.
AY789445 mRNA. Translation: AAX81432.1.
AL513202, AL356387 Genomic DNA. Translation: CAH70803.1.
AL356387, AL513202 Genomic DNA. Translation: CAI19265.1.
BC047336 mRNA. Translation: AAH47336.2.
BC036339 mRNA. Translation: AAH36339.2.
BC106910 mRNA. Translation: AAI06911.1.

IPI

IPI00033102.
IPI00374037.
IPI00374038.

RefSeq

NP_001035713.1. NM_001040623.2.
NP_001244930.1. NM_001258001.1.
NP_001244931.1. NM_001258002.1.
NP_001244932.1. NM_001258003.1.
NP_001244933.1. NM_001258004.1.
NP_001244934.1. NM_001258005.1.
NP_068569.2. NM_021797.3.
NP_970615.2. NM_201653.3.

UniGene

Hs.128814.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YBT	X-ray	2.22	A/B/C/D/E/F	21-398	[»]
2YBU	X-ray	2.25	A/B/C/D/E/F	21-398	[»]
3FXY	X-ray	2.00	A/B/C/D	22-408	[»]
3FY1	X-ray	1.70	A/B	22-408	[»]
3RM4	X-ray	1.90	A/B	22-408	[»]
3RM8	X-ray	1.80	A/B	22-408	[»]
3RM9	X-ray	2.10	A/B	22-408	[»]
3RME	X-ray	1.80	A/B	22-408	[»]

ProteinModelPortal

Q9BZP6.

ModBase

Search...

Protein family/group databases

CAZy

CBM14. Carbohydrate-Binding Module Family 14.
GH18. Glycoside Hydrolase Family 18.

PTM databases

PhosphoSite

Q9BZP6.

Polymorphism databases

DMDM

37999771.

Proteomic databases

PaxDb

Q9BZP6.

PRIDE

Q9BZP6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000343320; ENSP00000341828; ENSG00000134216.
ENST00000353665; ENSP00000338970; ENSG00000134216.
ENST00000369740; ENSP00000358755; ENSG00000134216.
ENST00000430615; ENSP00000391132; ENSG00000134216.
ENST00000451398; ENSP00000390476; ENSG00000134216.
ENST00000483391; ENSP00000436946; ENSG00000134216.

GeneID

27159.

KEGG

hsa:27159.

UCSC

uc001eaq.3. human.

Organism-specific databases

CTD

27159.

GeneCards

GC01P111833.

HGNC

HGNC:17432. CHIA.

MIM

606080. gene.

neXtProt

NX_Q9BZP6.

PharmGKB

PA142672117.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3325.

HOVERGEN

HBG011684.

InParanoid

Q9BZP6.

KO

K01183.

OMA

GLGRFMP.

PhylomeDB

Q9BZP6.

Enzyme and pathway databases

BRENDA

3.2.1.14. 2681.

Gene expression databases

ArrayExpress

Q9BZP6.

Bgee

Q9BZP6.

Genevestigator

Q9BZP6.

GermOnline

ENSG00000134216. Homo sapiens.

Family and domain databases

Gene3D

2.170.140.10. 1 hit.
3.20.20.80. 2 hits.

InterPro

IPR002557. Chitin-bd_dom.
IPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF01607. CBM_14. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]

SMART

SM00494. ChtBD2. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]

SUPFAM

SSF57625. Chitin_bind_PerA. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS50940. CHIT_BIND_II. 1 hit.
PS01095. CHITINASE_18. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9BZP6.

ChEMBL

CHEMBL1293197.

EvolutionaryTrace

Q9BZP6.

GenomeRNAi

27159.

NextBio

49937.

SOURCE

Search...

Entry information

Entry name

CHIA_HUMAN

Accession

Primary (citable) accession number: Q9BZP6
Secondary accession number(s): Q32W79 , Q32W80, Q3B866, Q5U5Z5, Q5VUV4, Q86UD8, Q9ULY3, Q9ULY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.