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Protein

Chymotrypsinogen B2

Gene

CTRB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei75 – 751Charge relay systemBy similarity
Active sitei120 – 1201Charge relay systemBy similarity
Active sitei213 – 2131Charge relay systemBy similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. cobalamin metabolic process Source: Reactome
  2. digestion Source: UniProtKB-KW
  3. extracellular matrix disassembly Source: Reactome
  4. extracellular matrix organization Source: Reactome
  5. small molecule metabolic process Source: Reactome
  6. vitamin metabolic process Source: Reactome
  7. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Enzyme and pathway databases

ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.
REACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.

Protein family/group databases

MEROPSiS01.152.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymotrypsinogen B2 (EC:3.4.21.1)
Cleaved into the following 3 chains:
Gene namesi
Name:CTRB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:2522. CTRB2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27023.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 263245Chymotrypsinogen B2PRO_0000285870Add
BLAST
Chaini19 – 3113Chymotrypsin B2 chain APRO_0000285871Add
BLAST
Chaini34 – 164131Chymotrypsin B2 chain BPRO_0000285872Add
BLAST
Chaini167 – 26397Chymotrypsin B2 chain CPRO_0000285873Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi19 ↔ 140PROSITE-ProRule annotation
Disulfide bondi60 ↔ 76PROSITE-ProRule annotation
Disulfide bondi154 ↔ 219PROSITE-ProRule annotation
Disulfide bondi186 ↔ 200PROSITE-ProRule annotation
Disulfide bondi209 ↔ 238PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiQ6GPI1.
PRIDEiQ6GPI1.

PTM databases

PhosphoSiteiQ6GPI1.

Expressioni

Gene expression databases

BgeeiQ6GPI1.
CleanExiHS_CTRB2.
ExpressionAtlasiQ6GPI1. baseline and differential.
GenevestigatoriQ6GPI1.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000303963.

Structurei

3D structure databases

ProteinModelPortaliQ6GPI1.
SMRiQ6GPI1. Positions 19-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 261228Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119027.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiQ6GPI1.
KOiK01310.
OMAiMFTVRND.
OrthoDBiEOG7MKW6Q.
PhylomeDBiQ6GPI1.
TreeFamiTF330455.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6GPI1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFLWLLSCW ALLGTTFGCG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS
60 70 80 90 100
LQDKTGFHFC GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV
110 120 130 140 150
LKIAKVFKNP KFSILTVNND ITLLKLATPA RFSQTVSAVC LPSADDDFPA
160 170 180 190 200
GTLCATTGWG KTKYNANKTP DKLQQAALPL LSNAECKKSW GRRITDVMIC
210 220 230 240 250
AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSRTCST TTPAVYARVA
260
KLIPWVQKIL AAN
Length:263
Mass (Da):27,923
Last modified:March 2, 2010 - v2
Checksum:i3B1C0549F3488351
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31F → S in AAH73145 (PubMed:15489334).Curated
Sequence conflicti10 – 167WALLGTT → FSLVGAA in AAH73145 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti250 – 2501A → T.1 Publication
Corresponds to variant rs4737 [ dbSNP | Ensembl ].
VAR_062766

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK291822 mRNA. Translation: BAF84511.1.
AC009078 Genomic DNA. No translation available.
BC073145 mRNA. Translation: AAH73145.1.
CCDSiCCDS32489.1.
RefSeqiNP_001020371.3. NM_001025200.3.
UniGeneiHs.632211.

Genome annotation databases

EnsembliENST00000303037; ENSP00000303963; ENSG00000168928.
GeneIDi440387.
KEGGihsa:440387.
UCSCiuc002fdr.3. human.

Polymorphism databases

DMDMi290457638.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Chymotrypsin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK291822 mRNA. Translation: BAF84511.1.
AC009078 Genomic DNA. No translation available.
BC073145 mRNA. Translation: AAH73145.1.
CCDSiCCDS32489.1.
RefSeqiNP_001020371.3. NM_001025200.3.
UniGeneiHs.632211.

3D structure databases

ProteinModelPortaliQ6GPI1.
SMRiQ6GPI1. Positions 19-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000303963.

Protein family/group databases

MEROPSiS01.152.

PTM databases

PhosphoSiteiQ6GPI1.

Polymorphism databases

DMDMi290457638.

Proteomic databases

PaxDbiQ6GPI1.
PRIDEiQ6GPI1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303037; ENSP00000303963; ENSG00000168928.
GeneIDi440387.
KEGGihsa:440387.
UCSCiuc002fdr.3. human.

Organism-specific databases

CTDi440387.
GeneCardsiGC16M075237.
HGNCiHGNC:2522. CTRB2.
neXtProtiNX_Q6GPI1.
PharmGKBiPA27023.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119027.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiQ6GPI1.
KOiK01310.
OMAiMFTVRND.
OrthoDBiEOG7MKW6Q.
PhylomeDBiQ6GPI1.
TreeFamiTF330455.

Enzyme and pathway databases

ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.
REACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.

Miscellaneous databases

GenomeRNAii440387.
NextBioi109214.
PROiQ6GPI1.

Gene expression databases

BgeeiQ6GPI1.
CleanExiHS_CTRB2.
ExpressionAtlasiQ6GPI1. baseline and differential.
GenevestigatoriQ6GPI1.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCTRB2_HUMAN
AccessioniPrimary (citable) accession number: Q6GPI1
Secondary accession number(s): A8K707
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 2, 2010
Last modified: January 7, 2015
This is version 95 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.