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O00187

- MASP2_HUMAN

UniProt

O00187 - MASP2_HUMAN

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Protein

Mannan-binding lectin serine protease 2

Gene
MASP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase.1 Publication

Catalytic activityi

Selective cleavage after Arg-223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671Calcium 1
Metal bindingi75 – 751Calcium 1
Metal bindingi120 – 1201Calcium 1
Metal bindingi122 – 1221Calcium 1; via carbonyl oxygen
Metal bindingi123 – 1231Calcium 1
Metal bindingi138 – 1381Calcium 2
Metal bindingi139 – 1391Calcium 2; via carbonyl oxygen
Metal bindingi141 – 1411Calcium 2
Metal bindingi158 – 1581Calcium 2
Metal bindingi159 – 1591Calcium 2; via carbonyl oxygen
Metal bindingi162 – 1621Calcium 2; via carbonyl oxygen
Sitei444 – 4452Cleavage By similarity
Active sitei483 – 4831Charge relay system
Active sitei532 – 5321Charge relay system
Active sitei633 – 6331Charge relay system

GO - Molecular functioni

  1. calcium-dependent protein binding Source: UniProtKB
  2. calcium ion binding Source: InterPro
  3. complement component C4b binding Source: BHF-UCL
  4. peptidase activity Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. complement activation Source: Reactome
  2. complement activation, classical pathway Source: UniProtKB-KW
  3. complement activation, lectin pathway Source: UniProtKB
  4. innate immune response Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.104. 2681.
ReactomeiREACT_163810. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
REACT_7964. Lectin pathway of complement activation.
REACT_8024. Initial triggering of complement.

Protein family/group databases

MEROPSiS01.229.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan-binding lectin serine protease 2 (EC:3.4.21.104)
Alternative name(s):
MBL-associated serine protease 2
Mannose-binding protein-associated serine protease 2
Short name:
MASP-2
Cleaved into the following 2 chains:
Gene namesi
Name:MASP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6902. MASP2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

MASP2 deficiency (MASPD) [MIM:613791]: A disorder that results in autoimmune manifestations, recurrent severe infections, and chronic inflammatory disease.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201D → G in MASPD; found in a patient suffering from frequent infections and chronic inflammatory disease; strongly decreases affinity for MBL2 and FCN2. 4 Publications
Corresponds to variant rs72550870 [ dbSNP | Ensembl ].
VAR_025346
Natural varianti126 – 1261P → L in MASPD. 2 Publications
Corresponds to variant rs56392418 [ dbSNP | Ensembl ].
VAR_025347
Natural varianti156 – 1561C → CHNH in MASPD.
VAR_065814

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 741Y → A: Strongly decreases affinity for MBL2. Decreases affinity for FCN2. 1 Publication
Mutagenesisi121 – 1211Y → A: Strongly decreases affinity for MBL2, but not for FCN2. 1 Publication
Mutagenesisi124 – 1241E → A: Decreases affinity for MBL2. Slight decrease in affinity for FCN2. 1 Publication
Mutagenesisi444 – 4441R → Q: Abolishes autocatalytic cleavage. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613791. phenotype.
Orphaneti331187. Immunodeficiency due to MASP-2 deficiency.
PharmGKBiPA30645.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515 Reviewed predictionAdd
BLAST
Chaini16 – 686671Mannan-binding lectin serine protease 2PRO_0000027598Add
BLAST
Chaini16 – 444429Mannan-binding lectin serine protease 2 A chainPRO_0000027599Add
BLAST
Chaini445 – 686242Mannan-binding lectin serine protease 2 B chainPRO_0000027600Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi72 ↔ 902 Publications
Disulfide bondi142 ↔ 1562 Publications
Disulfide bondi152 ↔ 1652 Publications
Modified residuei158 – 1581(3R)-3-hydroxyasparagine Reviewed prediction
Disulfide bondi167 ↔ 1802 Publications
Disulfide bondi184 ↔ 211 By similarity
Disulfide bondi241 ↔ 259 By similarity
Disulfide bondi300 ↔ 348 By similarity
Disulfide bondi328 ↔ 361 By similarity
Disulfide bondi366 ↔ 4122 Publications
Disulfide bondi396 ↔ 4302 Publications
Disulfide bondi434 ↔ 552Interchain (between A and B chains)2 Publications
Disulfide bondi598 ↔ 6182 Publications
Disulfide bondi629 ↔ 6602 Publications

Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains By similarity.
Activated by cleavage after Arg-444. The uncleaved zymogen is inactive towards synthetic substrates, but has sufficient activity to effect autocatalytic cleavage.2 Publications

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Hydroxylation

Proteomic databases

PaxDbiO00187.
PRIDEiO00187.

PTM databases

PhosphoSiteiO00187.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiO00187.
GenevestigatoriO00187.

Organism-specific databases

HPAiHPA029313.
HPA029314.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Binds MBL2. Isoform 2 binds to MASP1. Binds SERPING1. Dimerization and MBL2 binding requires calcium ions.2 Publications

Protein-protein interaction databases

BioGridi115970. 5 interactions.
IntActiO00187. 1 interaction.
MINTiMINT-7970114.

Structurei

Secondary structure

1
686
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 315
Turni33 – 364
Beta strandi44 – 507
Beta strandi55 – 6511
Beta strandi74 – 8916
Turni93 – 964
Beta strandi98 – 1003
Beta strandi109 – 11810
Beta strandi129 – 13810
Beta strandi151 – 1599
Beta strandi162 – 1665
Beta strandi171 – 1733
Beta strandi309 – 3135
Beta strandi323 – 3286
Beta strandi332 – 3365
Beta strandi345 – 3484
Beta strandi350 – 3567
Beta strandi360 – 3634
Beta strandi375 – 3828
Beta strandi391 – 3966
Turni398 – 4003
Beta strandi401 – 4033
Beta strandi409 – 4124
Beta strandi416 – 4205
Beta strandi430 – 4323
Beta strandi459 – 47315
Turni474 – 4763
Beta strandi477 – 4804
Helixi482 – 4854
Turni487 – 4904
Beta strandi496 – 5005
Beta strandi510 – 51910
Beta strandi534 – 5407
Helixi558 – 5614
Beta strandi567 – 5737
Beta strandi577 – 5793
Beta strandi586 – 5927
Helixi595 – 6039
Beta strandi604 – 6063
Beta strandi616 – 6205
Beta strandi636 – 6416
Turni642 – 6454
Beta strandi646 – 65914
Beta strandi667 – 6715
Helixi672 – 6754
Helixi676 – 68510

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q3XX-ray2.23A/B363-686[»]
1SZBX-ray2.50A/B16-181[»]
1ZJKX-ray2.18A287-686[»]
3TVJX-ray1.28A363-444[»]
B445-686[»]
4FXGX-ray3.75G/I291-444[»]
H/J445-686[»]
ProteinModelPortaliO00187.
SMRiO00187. Positions 17-686.

Miscellaneous databases

EvolutionaryTraceiO00187.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 137122CUB 1Add
BLAST
Domaini138 – 18144EGF-like; calcium-bindingAdd
BLAST
Domaini184 – 296113CUB 2Add
BLAST
Domaini298 – 36366Sushi 1Add
BLAST
Domaini364 – 43269Sushi 2Add
BLAST
Domaini445 – 684240Peptidase S1Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.
Contains 2 CUB domains.
Contains 1 EGF-like domain.

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiCOG5640.
HOVERGENiHBG000559.
InParanoidiO00187.
KOiK03993.
OMAiWTLTAPP.
OrthoDBiEOG7W6WK4.
PhylomeDBiO00187.
TreeFamiTF330373.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS01186. EGF_2. 1 hit.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 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: O00187-1) [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

MRLLTLLGLL CGSVATPLGP KWPEPVFGRL ASPGFPGEYA NDQERRWTLT    50
APPGYRLRLY FTHFDLELSH LCEYDFVKLS SGAKVLATLC GQESTDTERA 100
PGKDTFYSLG SSLDITFRSD YSNEKPFTGF EAFYAAEDID ECQVAPGEAP 150
TCDHHCHNHL GGFYCSCRAG YVLHRNKRTC SALCSGQVFT QRSGELSSPE 200
YPRPYPKLSS CTYSISLEEG FSVILDFVES FDVETHPETL CPYDFLKIQT 250
DREEHGPFCG KTLPHRIETK SNTVTITFVT DESGDHTGWK IHYTSTAQPC 300
PYPMAPPNGH VSPVQAKYIL KDSFSIFCET GYELLQGHLP LKSFTAVCQK 350
DGSWDRPMPA CSIVDCGPPD DLPSGRVEYI TGPGVTTYKA VIQYSCEETF 400
YTMKVNDGKY VCEADGFWTS SKGEKSLPVC EPVCGLSART TGGRIYGGQK 450
AKPGDFPWQV LILGGTTAAG ALLYDNWVLT AAHAVYEQKH DASALDIRMG 500
TLKRLSPHYT QAWSEAVFIH EGYTHDAGFD NDIALIKLNN KVVINSNITP 550
ICLPRKEAES FMRTDDIGTA SGWGLTQRGF LARNLMYVDI PIVDHQKCTA 600
AYEKPPYPRG SVTANMLCAG LESGGKDSCR GDSGGALVFL DSETERWFVG 650
GIVSWGSMNC GEAGQYGVYT KVINYIPWIE NIISDF 686
Length:686
Mass (Da):75,702
Last modified:January 11, 2011 - v4
Checksum:iED952085FA115E21
GO
Isoform 2 (identifier: O00187-2) [UniParc]FASTAAdd to Basket

Also known as: MAp19, Small MBL-associated protein, sMAP

The sequence of this isoform differs from the canonical sequence as follows:
     182-185: ALCS → EQSL
     186-686: Missing.

Show »
Length:185
Mass (Da):20,629
Checksum:i73B133D56FB229C2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti99 – 991R → Q.2 Publications
Corresponds to variant rs61735600 [ dbSNP | Ensembl ].
VAR_025344
Natural varianti118 – 1181R → C.2 Publications
Corresponds to variant rs147270785 [ dbSNP | Ensembl ].
VAR_025345
Natural varianti120 – 1201D → G in MASPD; found in a patient suffering from frequent infections and chronic inflammatory disease; strongly decreases affinity for MBL2 and FCN2. 4 Publications
Corresponds to variant rs72550870 [ dbSNP | Ensembl ].
VAR_025346
Natural varianti126 – 1261P → L in MASPD. 2 Publications
Corresponds to variant rs56392418 [ dbSNP | Ensembl ].
VAR_025347
Natural varianti155 – 1551H → R.
Corresponds to variant rs2273343 [ dbSNP | Ensembl ].
VAR_028784
Natural varianti156 – 1561C → CHNH in MASPD.
VAR_065814
Natural varianti371 – 3711D → Y.1 Publication
Corresponds to variant rs12711521 [ dbSNP | Ensembl ].
VAR_028785
Natural varianti377 – 3771V → A Associated with reduced MASP2 levels in plasma. 2 Publications
Corresponds to variant rs2273346 [ dbSNP | Ensembl ].
VAR_028786
Natural varianti439 – 4391R → H.
Corresponds to variant rs12085877 [ dbSNP | Ensembl ].
VAR_028787

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei182 – 1854ALCS → EQSL in isoform 2. VSP_005383
Alternative sequencei186 – 686501Missing in isoform 2. VSP_005384Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411N → S in BAF83512. 1 Publication
Sequence conflicti225 – 2251L → P in BAF83512. 1 Publication
Sequence conflicti298 – 2992QP → HA in CAA71059. 1 Publication
Sequence conflicti298 – 2992QP → HA in CAB50733. 1 Publication
Sequence conflicti298 – 2992QP → HA in CAB50735. 1 Publication
Sequence conflicti298 – 2992QP → HA in CAA67050. 1 Publication
Sequence conflicti298 – 2992QP → HA in AAG50274. 1 Publication
Sequence conflicti361 – 3622Missing in CAB50733. 1 Publication
Sequence conflicti361 – 3622Missing in CAB50735. 1 Publication
Sequence conflicti372 – 3721L → LCS in CAB50733. 1 Publication
Sequence conflicti372 – 3721L → LCS in CAB50735. 1 Publication
Sequence conflicti399 – 3991T → A in BAF83512. 1 Publication
Sequence conflicti442 – 4421G → E in AAG50274. 1 Publication
Sequence conflicti447 – 4471G → E in AAG50274. 1 Publication
Sequence conflicti461 – 4622Missing in CAB50733. 1 Publication
Sequence conflicti461 – 4622Missing in CAB50735. 1 Publication
Sequence conflicti473 – 4731L → LIL in CAB50733. 1 Publication
Sequence conflicti473 – 4731L → LIL in CAB50735. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y09926 mRNA. Translation: CAA71059.1.
AB008047 mRNA. Translation: BAA78616.1.
Y18281 mRNA. Translation: CAB50728.1.
Y18282 mRNA. Translation: CAB50729.1.
Y18283 mRNA. Translation: CAB50730.1.
Y18284 mRNA. Translation: CAB50731.1.
Y18286 Genomic DNA. Translation: CAB50732.1.
Y18286 Genomic DNA. Translation: CAB50733.1.
Y18287 Genomic DNA. Translation: CAB50734.1.
Y18287 Genomic DNA. Translation: CAB50735.1.
X98400 mRNA. Translation: CAA67050.1.
AB033742 Genomic DNA. Translation: BAA85658.1.
AB033742 Genomic DNA. Translation: BAA85659.1.
AF321558 Genomic DNA. Translation: AAG50275.1.
AF321562
, AF321558, AF321559, AF321560, AF321561 Genomic DNA. Translation: AAG50274.1.
AK290823 mRNA. Translation: BAF83512.1.
AL109811 Genomic DNA. Translation: CAI22102.1.
AL109811 Genomic DNA. Translation: CAI22103.1.
AJ297949 Genomic DNA. Translation: CAC17138.1.
AJ297949 Genomic DNA. Translation: CAC17139.1.
AJ300188 Genomic DNA. Translation: CAC15568.1.
CCDSiCCDS123.1. [O00187-1]
CCDS124.1. [O00187-2]
PIRiA59271.
RefSeqiNP_006601.2. NM_006610.3. [O00187-1]
NP_631947.1. NM_139208.2. [O00187-2]
UniGeneiHs.655645.

Genome annotation databases

EnsembliENST00000400897; ENSP00000383690; ENSG00000009724. [O00187-1]
ENST00000400898; ENSP00000383691; ENSG00000009724. [O00187-2]
GeneIDi10747.
KEGGihsa:10747.
UCSCiuc001aru.3. human. [O00187-1]
uc001arv.3. human. [O00187-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

MASP2base

MASP2 mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y09926 mRNA. Translation: CAA71059.1 .
AB008047 mRNA. Translation: BAA78616.1 .
Y18281 mRNA. Translation: CAB50728.1 .
Y18282 mRNA. Translation: CAB50729.1 .
Y18283 mRNA. Translation: CAB50730.1 .
Y18284 mRNA. Translation: CAB50731.1 .
Y18286 Genomic DNA. Translation: CAB50732.1 .
Y18286 Genomic DNA. Translation: CAB50733.1 .
Y18287 Genomic DNA. Translation: CAB50734.1 .
Y18287 Genomic DNA. Translation: CAB50735.1 .
X98400 mRNA. Translation: CAA67050.1 .
AB033742 Genomic DNA. Translation: BAA85658.1 .
AB033742 Genomic DNA. Translation: BAA85659.1 .
AF321558 Genomic DNA. Translation: AAG50275.1 .
AF321562
, AF321558 , AF321559 , AF321560 , AF321561 Genomic DNA. Translation: AAG50274.1 .
AK290823 mRNA. Translation: BAF83512.1 .
AL109811 Genomic DNA. Translation: CAI22102.1 .
AL109811 Genomic DNA. Translation: CAI22103.1 .
AJ297949 Genomic DNA. Translation: CAC17138.1 .
AJ297949 Genomic DNA. Translation: CAC17139.1 .
AJ300188 Genomic DNA. Translation: CAC15568.1 .
CCDSi CCDS123.1. [O00187-1 ]
CCDS124.1. [O00187-2 ]
PIRi A59271.
RefSeqi NP_006601.2. NM_006610.3. [O00187-1 ]
NP_631947.1. NM_139208.2. [O00187-2 ]
UniGenei Hs.655645.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q3X X-ray 2.23 A/B 363-686 [» ]
1SZB X-ray 2.50 A/B 16-181 [» ]
1ZJK X-ray 2.18 A 287-686 [» ]
3TVJ X-ray 1.28 A 363-444 [» ]
B 445-686 [» ]
4FXG X-ray 3.75 G/I 291-444 [» ]
H/J 445-686 [» ]
ProteinModelPortali O00187.
SMRi O00187. Positions 17-686.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115970. 5 interactions.
IntActi O00187. 1 interaction.
MINTi MINT-7970114.

Protein family/group databases

MEROPSi S01.229.

PTM databases

PhosphoSitei O00187.

Proteomic databases

PaxDbi O00187.
PRIDEi O00187.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000400897 ; ENSP00000383690 ; ENSG00000009724 . [O00187-1 ]
ENST00000400898 ; ENSP00000383691 ; ENSG00000009724 . [O00187-2 ]
GeneIDi 10747.
KEGGi hsa:10747.
UCSCi uc001aru.3. human. [O00187-1 ]
uc001arv.3. human. [O00187-2 ]

Organism-specific databases

CTDi 10747.
GeneCardsi GC01M011086.
HGNCi HGNC:6902. MASP2.
HPAi HPA029313.
HPA029314.
MIMi 605102. gene.
613791. phenotype.
neXtProti NX_O00187.
Orphaneti 331187. Immunodeficiency due to MASP-2 deficiency.
PharmGKBi PA30645.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOVERGENi HBG000559.
InParanoidi O00187.
KOi K03993.
OMAi WTLTAPP.
OrthoDBi EOG7W6WK4.
PhylomeDBi O00187.
TreeFami TF330373.

Enzyme and pathway databases

BRENDAi 3.4.21.104. 2681.
Reactomei REACT_163810. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
REACT_7964. Lectin pathway of complement activation.
REACT_8024. Initial triggering of complement.

Miscellaneous databases

EvolutionaryTracei O00187.
GenomeRNAii 10747.
NextBioi 40811.
PROi O00187.
SOURCEi Search...

Gene expression databases

Bgeei O00187.
Genevestigatori O00187.

Family and domain databases

Gene3Di 2.60.120.290. 2 hits.
InterProi IPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00431. CUB. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEi PS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS01186. EGF_2. 1 hit.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "A truncated form of mannose-binding lectin-associated serine protease (MASP)-2 expressed by alternative polyadenylation is a component of the lectin complement pathway."
    Takahashi M., Endo Y., Fujita T., Matsushita M.
    Int. Immunol. 11:859-863(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
  3. "Two constituents of the initiation complex of the mannan-binding lectin activation pathway of complement are encoded by a single structural gene."
    Stover C.M., Thiel S., Thelen M., Lynch N.J., Vorup-Jensen T., Jensenius J.C., Schwaeble W.J.
    J. Immunol. 162:3481-3490(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), ACTIVATION BY PROTEOLYTIC CLEAVAGE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Liver.
  4. "Identification and characterization of a novel protein of the human complement system, mannan-binding lectin-associated serine protease-2 (MASP-2)."
    Thiel S., Vorup-Jensen T., Stover C.M., Schwaeble W., Laursen S.B., Poulsen K., Willis A.C., Eggleton P., Hansen S., Holmskov U., Reid K.B.M., Jensenius J.C.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Partial genomic structure of human MBL-associated serine protease (MASP)-2 (from exon 1 to exon 5)."
    Takahashi M., Fujita T.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-371.
  6. "Structure of human MASP-2 gene."
    Park D., Kim B., Baek K., Yoon J.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "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: Liver.
  8. "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].
  9. "Towards a comprehensive database of proteins from the urine of patients with bladder cancer."
    Rasmussen H.H., Orntoft T.F., Wolf H., Celis J.E.
    J. Urol. 155:2113-2119(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-45.
    Tissue: Urine.
  10. "The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, is part of a tightly linked gene cluster on chromosome 1p36.2-3."
    Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C., Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S., Fujita T., Schwaeble W.
    Genes Immun. 2:119-127(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-284 AND 364-686, VARIANT ALA-377.
  11. "Proteolytic activities of two types of mannose-binding lectin-associated serine protease."
    Matsushita M., Thiel S., Jensenius J.C., Terai I., Fujita T.
    J. Immunol. 165:2637-2642(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SERPING1.
  12. "The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin."
    Gregory L.A., Thielens N.M., Matsushita M., Sorensen R., Arlaud G.J., Fontecilla-Camps J.-C., Gaboriaud C.
    J. Biol. Chem. 279:29391-29397(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 16-181 (ISOFORM 2), CHARACTERIZATION OF VARIANT GLY-120, CALCIUM-BINDING SITES, DIMERIZATION, MUTAGENESIS OF TYR-74; TYR-121 AND GLU-124, INTERACTION WITH MBL2 AND FCN2, DISULFIDE BONDS.
  13. "The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions."
    Harmat V., Gal P., Kardos J., Szilagyi K., Ambrus G., Vegh B., Naray-Szabo G., Zavodszky P.
    J. Mol. Biol. 342:1533-1546(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 363-686, DISULFIDE BONDS.
  14. "A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations."
    Gal P., Harmat V., Kocsis A., Bian T., Barna L., Ambrus G., Vegh B., Balczer J., Sim R.B., Naray-Szabo G., Zavodszky P.
    J. Biol. Chem. 280:33435-33444(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 287-686, AUTOCATALYTIC CLEAVAGE AT ARG-444, MUTAGENESIS OF ARG-444.
  15. Cited for: VARIANT MASPD GLY-120, CHARACTERIZATION OF VARIANT MASPD GLY-120.
  16. "Novel MASP2 variants detected among North African and Sub-Saharan individuals."
    Lozano F., Suarez B., Munoz A., Jensenius J.C., Mensa J., Vives J., Horcajada J.P.
    Tissue Antigens 66:131-135(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLN-99; CYS-118; GLY-120 AND LEU-126.
  17. "Deficiency of mannan-binding lectin associated serine protease-2 due to missense polymorphisms."
    Thiel S., Steffensen R., Christensen I.J., Ip W.K., Lau Y.L., Reason I.J., Eiberg H., Gadjeva M., Ruseva M., Jensenius J.C.
    Genes Immun. 8:154-163(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MASPD GLY-120; LEU-126 AND HIS-ASN-HIS-156 INS, VARIANTS GLN-99; CYS-118 AND ALA-377.

Entry informationi

Entry nameiMASP2_HUMAN
AccessioniPrimary (citable) accession number: O00187
Secondary accession number(s): A8K458
, A8MWJ2, O75754, Q5TEQ5, Q5TER0, Q96QG4, Q9BZH0, Q9H498, Q9H499, Q9UBP3, Q9UC48, Q9ULC7, Q9UMV3, Q9Y270
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 164 of the entry and version 4 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 1
    Human chromosome 1: 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

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