Q6GPI1 (CTRB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chymotrypsinogen B2
EC=3.4.21.1

Cleaved into the following 3 chains:

1. Chymotrypsin B2 chain A
2. Chymotrypsin B2 chain B
3. Chymotrypsin B2 chain C

Gene names

Name:

CTRB2

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

General annotation (Comments)

Catalytic activity	Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Subcellular location	Secreted › extracellular space.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Digestion
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	digestion Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix disassembly Traceable author statement. Source: Reactome proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	By similarity
	Chain	19 – 263	245	Chymotrypsinogen B2		PRO_0000285870
	Chain	19 – 31	13	Chymotrypsin B2 chain A		PRO_0000285871
	Chain	34 – 164	131	Chymotrypsin B2 chain B		PRO_0000285872
	Chain	167 – 263	97	Chymotrypsin B2 chain C		PRO_0000285873
Regions
	Domain	34 – 261	228	Peptidase S1
Sites
	Active site	75	1	Charge relay system By similarity
	Active site	120	1	Charge relay system By similarity
	Active site	213	1	Charge relay system By similarity
Amino acid modifications
	Disulfide bond	19 ↔ 140		By similarity
	Disulfide bond	60 ↔ 76		By similarity
	Disulfide bond	154 ↔ 219		By similarity
	Disulfide bond	186 ↔ 200		By similarity
	Disulfide bond	209 ↔ 238		By similarity
Natural variations
	Natural variant	250	1	A → T. Ref.3 Corresponds to variant rs4737 [ dbSNP | Ensembl ].		VAR_062766
Experimental info
	Sequence conflict	3	1	F → S in AAH73145. Ref.3
	Sequence conflict	10 – 16	7	WALLGTT → FSLVGAA in AAH73145. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q6GPI1 [UniParc]. Last modified March 2, 2010. Version 2. Checksum: 3B1C0549F3488351	FASTA	263	27,923
	10 20 30 40 50 60 MAFLWLLSCW ALLGTTFGCG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS LQDKTGFHFC 70 80 90 100 110 120 GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV LKIAKVFKNP KFSILTVNND 130 140 150 160 170 180 ITLLKLATPA RFSQTVSAVC LPSADDDFPA GTLCATTGWG KTKYNANKTP DKLQQAALPL 190 200 210 220 230 240 LSNAECKKSW GRRITDVMIC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSRTCST 250 260 TTPAVYARVA KLIPWVQKIL AAN

References

[1]	"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]. Tissue: Prostate.
[2]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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], VARIANT THR-250. Tissue: Pancreas.

Web resources

Wikipedia

Chymotrypsin entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK291822 mRNA. Translation: BAF84511.1. AC009078 Genomic DNA. No translation available. BC073145 mRNA. Translation: AAH73145.1.
IPI	IPI00742763.
RefSeq	NP_001020371.3. NM_001025200.3.
UniGene	Hs.632211.
3D structure databases
HSSP	HSSP built from PDB template 1CHG based on UniProtKB P00766.
ProteinModelPortal	Q6GPI1.
SMR	Q6GPI1. Positions 19-263.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000303963.
Protein family/group databases
MEROPS	S01.152.
PTM databases
PhosphoSite	Q6GPI1.
Polymorphism databases
DMDM	290457638.
Proteomic databases
PaxDb	Q6GPI1.
PRIDE	Q6GPI1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000303037; ENSP00000303963; ENSG00000168928.
GeneID	440387.
KEGG	hsa:440387.
UCSC	uc002fdr.3. human.
Organism-specific databases
CTD	440387.
GeneCards	GC16M075237.
HGNC	HGNC:2522. CTRB2.
neXtProt	NX_Q6GPI1.
PharmGKB	PA27023.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5640.
HOGENOM	HOG000251820.
HOVERGEN	HBG013304.
InParanoid	Q6GPI1.
KO	K01310.
OMA	ADCKKFW.
OrthoDB	EOG4VMFG1.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	Q6GPI1.
Bgee	Q6GPI1.
CleanEx	HS_CTRB2.
Genevestigator	Q6GPI1.
Family and domain databases
InterPro	IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	440387.
NextBio	109214.

Entry information

Entry name

CTRB2_HUMAN

Accession

Primary (citable) accession number: Q6GPI1
Secondary accession number(s): A8K707

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	March 2, 2010
Last modified:	April 3, 2013
This is version 82 of the entry and version 2 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.