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P23946

- CMA1_HUMAN

UniProt

P23946 - CMA1_HUMAN

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Protein

Chymase

Gene

CMA1

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

Functioni

Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.

Catalytic activityi

Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei66 – 661Charge relay system
Active sitei110 – 1101Charge relay system
Active sitei203 – 2031Charge relay system

GO - Molecular functioni

  1. peptide binding Source: Ensembl
  2. serine-type endopeptidase activity Source: UniProtKB
  3. serine-type peptidase activity Source: ProtInc

GO - Biological processi

  1. angiotensin maturation Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. cellular response to glucose stimulus Source: Ensembl
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. interleukin-1 beta biosynthetic process Source: BHF-UCL
  7. midbrain development Source: Ensembl
  8. peptide metabolic process Source: Ensembl
  9. positive regulation of angiogenesis Source: Ensembl
  10. regulation of inflammatory response Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
SABIO-RKP23946.

Protein family/group databases

MEROPSiS01.140.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymase (EC:3.4.21.39)
Alternative name(s):
Alpha-chymase
Mast cell protease I
Gene namesi
Name:CMA1
Synonyms:CYH, CYM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:2097. CMA1.

Subcellular locationi

Secreted. Cytoplasmic granule
Note: Mast cell granules.

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. intracellular Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26623.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Propeptidei20 – 212Activation peptide1 PublicationPRO_0000027433
Chaini22 – 247226ChymasePRO_0000027434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 67
Glycosylationi80 – 801N-linked (GlcNAc...)2 Publications
Glycosylationi103 – 1031N-linked (GlcNAc...)1 Publication
Disulfide bondi144 ↔ 209
Disulfide bondi175 ↔ 188

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP23946.
PRIDEiP23946.

PTM databases

PhosphoSiteiP23946.

Miscellaneous databases

PMAP-CutDBP23946.

Expressioni

Tissue specificityi

Mast cells in lung, heart, skin and placenta. Expressed in both normal skin and in urticaria pigmentosa lesions.1 Publication

Gene expression databases

BgeeiP23946.
CleanExiHS_CMA1.
ExpressionAtlasiP23946. baseline and differential.
GenevestigatoriP23946.

Organism-specific databases

HPAiCAB000363.
HPA052634.

Interactioni

Protein-protein interaction databases

BioGridi107624. 2 interactions.
STRINGi9606.ENSP00000250378.

Structurei

Secondary structure

1
247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 427Combined sources
Beta strandi44 – 474Combined sources
Beta strandi49 – 579Combined sources
Beta strandi60 – 634Combined sources
Helixi65 – 673Combined sources
Beta strandi70 – 778Combined sources
Beta strandi79 – 835Combined sources
Beta strandi89 – 9810Combined sources
Turni104 – 1063Combined sources
Beta strandi112 – 1187Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi143 – 15311Combined sources
Beta strandi163 – 1708Combined sources
Helixi172 – 1754Combined sources
Turni183 – 1853Combined sources
Beta strandi186 – 1905Combined sources
Turni192 – 1943Combined sources
Beta strandi206 – 2094Combined sources
Beta strandi212 – 2198Combined sources
Beta strandi228 – 2325Combined sources
Helixi233 – 24614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KLTX-ray1.90A22-247[»]
1NN6X-ray1.75A20-247[»]
1PJPX-ray2.20A22-247[»]
1T31X-ray1.90A22-247[»]
2HVXX-ray2.60A22-247[»]
3N7OX-ray1.80A22-247[»]
3S0NX-ray1.95A22-247[»]
4AFQX-ray1.51A/B22-247[»]
4AFSX-ray1.90A22-247[»]
4AFUX-ray1.82A/B22-247[»]
4AFZX-ray2.25A/B22-247[»]
4AG1X-ray1.40A22-247[»]
4AG2X-ray1.80A/B22-247[»]
4K2YX-ray2.30A22-247[»]
4K5ZX-ray1.80A22-247[»]
4K60X-ray1.50A22-247[»]
4K69X-ray1.50A22-247[»]
4KP0X-ray2.80A22-247[»]
ProteinModelPortaliP23946.
SMRiP23946. Positions 22-247.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23946.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 245224Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP23946.
KOiK01329.
OMAiTLHHDIM.
OrthoDBiEOG7RRF7Z.
PhylomeDBiP23946.
TreeFamiTF333630.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P23946-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MLLLPLPLLL FLLCSRAEAG EIIGGTECKP HSRPYMAYLE IVTSNGPSKF
60 70 80 90 100
CGGFLIRRNF VLTAAHCAGR SITVTLGAHN ITEEEDTWQK LEVIKQFRHP
110 120 130 140 150
KYNTSTLHHD IMLLKLKEKA SLTLAVGTLP FPSQFNFVPP GRMCRVAGWG
160 170 180 190 200
RTGVLKPGSD TLQEVKLRLM DPQACSHFRD FDHNLQLCVG NPRKTKSAFK
210 220 230 240
GDSGGPLLCA GVAQGIVSYG RSDAKPPAVF TRISHYRPWI NQILQAN
Length:247
Mass (Da):27,325
Last modified:March 1, 1992 - v1
Checksum:iDC1464A049ED6B00
GO
Isoform 2 (identifier: P23946-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-111: Missing.

Note: No experimental confirmation available

Show »
Length:136
Mass (Da):14,893
Checksum:iDA8A15F89D222FC4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281C → S in AAB26828. (PubMed:8495723)Curated
Sequence conflicti131 – 1322FP → AV AA sequence (PubMed:8144971)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461G → R.
Corresponds to variant rs5246 [ dbSNP | Ensembl ].
VAR_011770
Natural varianti66 – 661H → R.1 Publication
Corresponds to variant rs5247 [ dbSNP | Ensembl ].
VAR_011771
Natural varianti98 – 981R → H.
Corresponds to variant rs13306252 [ dbSNP | Ensembl ].
VAR_029190

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 111111Missing in isoform 2. 1 PublicationVSP_056947Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64269 Genomic DNA. Translation: AAA52020.1.
M69137 Genomic DNA. Translation: AAA52021.1.
M69136 mRNA. Translation: AAA52019.1.
AB451464 mRNA. Translation: BAG70278.1.
AL132800 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66007.1.
BC069110 mRNA. Translation: AAH69110.1.
BC069370 mRNA. Translation: AAH69370.1.
BC069490 mRNA. Translation: AAH69490.1.
BC103974 mRNA. Translation: AAI03975.1.
BC103975 mRNA. Translation: AAI03976.1.
S61334 mRNA. Translation: AAB26828.1.
X59072 Genomic DNA. Translation: CAA41796.1.
CCDSiCCDS9630.1.
PIRiA40967. KYHUCM.
RefSeqiNP_001827.1. NM_001836.3.
UniGeneiHs.135626.

Genome annotation databases

EnsembliENST00000206446; ENSP00000206446; ENSG00000092009. [P23946-2]
ENST00000250378; ENSP00000250378; ENSG00000092009. [P23946-1]
GeneIDi1215.
KEGGihsa:1215.
UCSCiuc001wpp.1. human. [P23946-1]

Polymorphism databases

DMDMi126825.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64269 Genomic DNA. Translation: AAA52020.1 .
M69137 Genomic DNA. Translation: AAA52021.1 .
M69136 mRNA. Translation: AAA52019.1 .
AB451464 mRNA. Translation: BAG70278.1 .
AL132800 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66007.1 .
BC069110 mRNA. Translation: AAH69110.1 .
BC069370 mRNA. Translation: AAH69370.1 .
BC069490 mRNA. Translation: AAH69490.1 .
BC103974 mRNA. Translation: AAI03975.1 .
BC103975 mRNA. Translation: AAI03976.1 .
S61334 mRNA. Translation: AAB26828.1 .
X59072 Genomic DNA. Translation: CAA41796.1 .
CCDSi CCDS9630.1.
PIRi A40967. KYHUCM.
RefSeqi NP_001827.1. NM_001836.3.
UniGenei Hs.135626.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KLT X-ray 1.90 A 22-247 [» ]
1NN6 X-ray 1.75 A 20-247 [» ]
1PJP X-ray 2.20 A 22-247 [» ]
1T31 X-ray 1.90 A 22-247 [» ]
2HVX X-ray 2.60 A 22-247 [» ]
3N7O X-ray 1.80 A 22-247 [» ]
3S0N X-ray 1.95 A 22-247 [» ]
4AFQ X-ray 1.51 A/B 22-247 [» ]
4AFS X-ray 1.90 A 22-247 [» ]
4AFU X-ray 1.82 A/B 22-247 [» ]
4AFZ X-ray 2.25 A/B 22-247 [» ]
4AG1 X-ray 1.40 A 22-247 [» ]
4AG2 X-ray 1.80 A/B 22-247 [» ]
4K2Y X-ray 2.30 A 22-247 [» ]
4K5Z X-ray 1.80 A 22-247 [» ]
4K60 X-ray 1.50 A 22-247 [» ]
4K69 X-ray 1.50 A 22-247 [» ]
4KP0 X-ray 2.80 A 22-247 [» ]
ProteinModelPortali P23946.
SMRi P23946. Positions 22-247.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107624. 2 interactions.
STRINGi 9606.ENSP00000250378.

Chemistry

BindingDBi P23946.
ChEMBLi CHEMBL4068.
GuidetoPHARMACOLOGYi 2340.

Protein family/group databases

MEROPSi S01.140.

PTM databases

PhosphoSitei P23946.

Polymorphism databases

DMDMi 126825.

Proteomic databases

PaxDbi P23946.
PRIDEi P23946.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000206446 ; ENSP00000206446 ; ENSG00000092009 . [P23946-2 ]
ENST00000250378 ; ENSP00000250378 ; ENSG00000092009 . [P23946-1 ]
GeneIDi 1215.
KEGGi hsa:1215.
UCSCi uc001wpp.1. human. [P23946-1 ]

Organism-specific databases

CTDi 1215.
GeneCardsi GC14M024974.
HGNCi HGNC:2097. CMA1.
HPAi CAB000363.
HPA052634.
MIMi 118938. gene.
neXtProti NX_P23946.
PharmGKBi PA26623.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000118895.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P23946.
KOi K01329.
OMAi TLHHDIM.
OrthoDBi EOG7RRF7Z.
PhylomeDBi P23946.
TreeFami TF333630.

Enzyme and pathway databases

Reactomei REACT_111040. Signaling by SCF-KIT.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
SABIO-RK P23946.

Miscellaneous databases

EvolutionaryTracei P23946.
GeneWikii CMA1.
GenomeRNAii 1215.
NextBioi 5003.
PMAP-CutDB P23946.
PROi P23946.
SOURCEi Search...

Gene expression databases

Bgeei P23946.
CleanExi HS_CMA1.
ExpressionAtlasi P23946. baseline and differential.
Genevestigatori P23946.

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

« Hide 'large scale' publications
  1. "Structure, chromosomal assignment, and deduced amino acid sequence of a human gene for mast cell chymase."
    Caughey G.H., Zerweck E.H., Vanderslice P.
    J. Biol. Chem. 266:12956-12963(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning of the gene and cDNA for human heart chymase."
    Urata H., Kinoshita A., Perez D.M., Misono K.S., Bumpus F.M., Graham R.M., Husain A.
    J. Biol. Chem. 266:17173-17179(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    Tissue: Heart.
  3. "Determination of the primary structures of human skin chymase and cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions."
    Schechter N.M., Wang Z.M., Blacher R.W., Lessin S.R., Lazarus G.S., Rubin H.
    J. Immunol. 152:4062-4069(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 22-56; 123-132; 136-148; 167-194 AND 197-247, TISSUE SPECIFICITY.
    Tissue: Skin.
  4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS 1 AND 2), VARIANT ARG-66.
  8. "Purification and molecular cloning of chymase from human tonsils."
    Sukenaga Y., Kido H., Neki A., Enomoto M., Ishida K., Takagi K., Katunuma N.
    FEBS Lett. 323:119-122(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-247 (ISOFORM 1).
  9. "Angiotensin II-forming heart chymase is a mast-cell-specific enzyme."
    Jenne D.E., Tschopp J.
    Biochem. J. 276:567-568(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-60.
    Tissue: Placenta.
  10. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80 AND ASN-103.
    Tissue: Liver.
  11. "Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9 A."
    McGrath M.E., Mirzadegan T., Schmidt B.F.
    Biochemistry 36:14318-14324(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  12. "The 2.2-A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity."
    Pereira P.J.P., Wang Z.-M., Rubin H., Huber R., Bode W., Schechter N.M., Strobl S.
    J. Mol. Biol. 286:163-173(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiCMA1_HUMAN
AccessioniPrimary (citable) accession number: P23946
Secondary accession number(s): B5BUM8
, Q16018, Q3SY36, Q3SY37, Q9UDH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: November 26, 2014
This is version 151 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3