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Q9CR35

- CTRB1_MOUSE

UniProt

Q9CR35 - CTRB1_MOUSE

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Protein

Chymotrypsinogen B

Gene

Ctrb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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. peptidase activity Source: MGI
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. digestion Source: UniProtKB-KW
  2. proteolysis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Enzyme and pathway databases

ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiS01.152.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymotrypsinogen B (EC:3.4.21.1)
Cleaved into the following 3 chains:
Gene namesi
Name:Ctrb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:88559. Ctrb1.

Subcellular locationi

Secretedextracellular space By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 263245Chymotrypsinogen BPRO_0000285874Add
BLAST
Chaini19 – 3113Chymotrypsin B chain ABy similarityPRO_0000285875Add
BLAST
Chaini34 – 164131Chymotrypsin B chain BBy similarityPRO_0000285876Add
BLAST
Chaini167 – 26397Chymotrypsin B chain CBy similarityPRO_0000285877Add
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

MaxQBiQ9CR35.
PaxDbiQ9CR35.
PRIDEiQ9CR35.

PTM databases

PhosphoSiteiQ9CR35.

Expressioni

Gene expression databases

BgeeiQ9CR35.
CleanExiMM_CTRB1.
GenevestigatoriQ9CR35.

Structurei

3D structure databases

ProteinModelPortaliQ9CR35.
SMRiQ9CR35. 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.
InParanoidiQ9CR35.
KOiK01310.
OMAiLATEARF.
OrthoDBiEOG7MKW6Q.
PhylomeDBiQ9CR35.
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.

Q9CR35-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFLWLVSCF ALVGATFGCG VPAIQPVLTG LSRIVNGEDA IPGSWPWQVS
60 70 80 90 100
LQDRTGFHFC GGSLISENWV VTAAHCGVKT TDVVVAGEFD QGSDEENVQV
110 120 130 140 150
LKIAQVFKNP KFNSFTVRND ITLLKLATPA QFSETVSAVC LPTVDDDFPA
160 170 180 190 200
GTLCATTGWG KTKYNALKTP DKLQQAALPI VSEAKCKESW GSKITDVMIC
210 220 230 240 250
AGASGVSSCM GDSGGPLVCQ KDGVWTLAGI VSWGSGFCST STPAVYARVT
260
ALMPWVQEIL EAN
Length:263
Mass (Da):27,822
Last modified:June 1, 2001 - v1
Checksum:i28C4487AF1A26B27
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631S → Y in BAB25112. (PubMed:16141072)Curated
Sequence conflicti82 – 821D → N in BAB22539. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003060 mRNA. Translation: BAB22539.1.
AK003079 mRNA. Translation: BAB22553.1.
AK007566 mRNA. Translation: BAB25112.1.
AK007765 mRNA. Translation: BAB25241.1.
AK007815 mRNA. Translation: BAB25280.1.
AK008644 mRNA. Translation: BAC25226.1.
AK008729 mRNA. Translation: BAB25861.1.
AK008888 mRNA. Translation: BAB25954.1.
AK008927 mRNA. Translation: BAB25971.1.
BC061083 mRNA. Translation: AAH61083.1.
CCDSiCCDS22679.1.
RefSeqiNP_079859.2. NM_025583.2.
UniGeneiMm.34374.

Genome annotation databases

EnsembliENSMUST00000034435; ENSMUSP00000034435; ENSMUSG00000031957.
GeneIDi66473.
KEGGimmu:66473.
UCSCiuc009nms.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003060 mRNA. Translation: BAB22539.1 .
AK003079 mRNA. Translation: BAB22553.1 .
AK007566 mRNA. Translation: BAB25112.1 .
AK007765 mRNA. Translation: BAB25241.1 .
AK007815 mRNA. Translation: BAB25280.1 .
AK008644 mRNA. Translation: BAC25226.1 .
AK008729 mRNA. Translation: BAB25861.1 .
AK008888 mRNA. Translation: BAB25954.1 .
AK008927 mRNA. Translation: BAB25971.1 .
BC061083 mRNA. Translation: AAH61083.1 .
CCDSi CCDS22679.1.
RefSeqi NP_079859.2. NM_025583.2.
UniGenei Mm.34374.

3D structure databases

ProteinModelPortali Q9CR35.
SMRi Q9CR35. Positions 19-263.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S01.152.

PTM databases

PhosphoSitei Q9CR35.

Proteomic databases

MaxQBi Q9CR35.
PaxDbi Q9CR35.
PRIDEi Q9CR35.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034435 ; ENSMUSP00000034435 ; ENSMUSG00000031957 .
GeneIDi 66473.
KEGGi mmu:66473.
UCSCi uc009nms.2. mouse.

Organism-specific databases

CTDi 1504.
MGIi MGI:88559. Ctrb1.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000119027.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi Q9CR35.
KOi K01310.
OMAi LATEARF.
OrthoDBi EOG7MKW6Q.
PhylomeDBi Q9CR35.
TreeFami TF330455.

Enzyme and pathway databases

Reactomei REACT_199000. Activation of Matrix Metalloproteinases.

Miscellaneous databases

ChiTaRSi Ctrb1. mouse.
NextBioi 321790.
PROi Q9CR35.
SOURCEi Search...

Gene expression databases

Bgeei Q9CR35.
CleanExi MM_CTRB1.
Genevestigatori Q9CR35.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas, Spleen and Stomach.
  2. "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].
    Tissue: Liver.

Entry informationi

Entry nameiCTRB1_MOUSE
AccessioniPrimary (citable) accession number: Q9CR35
Secondary accession number(s): Q9D8X8, Q9DC86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3