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Protein

Mannan-binding lectin serine protease 2

Gene

MASP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi67Calcium 11
Metal bindingi75Calcium 11
Metal bindingi120Calcium 11
Metal bindingi122Calcium 1; via carbonyl oxygen1
Metal bindingi123Calcium 11
Metal bindingi138Calcium 21
Metal bindingi139Calcium 2; via carbonyl oxygen1
Metal bindingi141Calcium 21
Metal bindingi158Calcium 21
Metal bindingi159Calcium 2; via carbonyl oxygen1
Metal bindingi162Calcium 2; via carbonyl oxygen1
Active sitei483Charge relay system1
Active sitei532Charge relay system1
Active sitei633Charge relay system1

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • calcium ion binding Source: InterPro
  • complement component C4b binding Source: BHF-UCL
  • peptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

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

BioCyciZFISH:HS00265-MONOMER.
BRENDAi3.4.21.104. 2681.
ReactomeiR-HSA-166662. Lectin pathway of complement activation.
R-HSA-166663. Initial triggering of complement.
R-HSA-2855086. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
SABIO-RKO00187.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6902. MASP2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

MASP2 deficiency (MASPD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder that results in autoimmune manifestations, recurrent severe infections, and chronic inflammatory disease.
See also OMIM:613791
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025346120D → G in MASPD; found in a patient suffering from frequent infections and chronic inflammatory disease; strongly decreases affinity for MBL2 and FCN2. 4 PublicationsCorresponds to variant rs72550870dbSNPEnsembl.1
Natural variantiVAR_025347126P → L in MASPD. 2 PublicationsCorresponds to variant rs56392418dbSNPEnsembl.1
Natural variantiVAR_065814156C → CHNH in MASPD. 1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi74Y → A: Strongly decreases affinity for MBL2. Decreases affinity for FCN2. 1 Publication1
Mutagenesisi121Y → A: Strongly decreases affinity for MBL2, but not for FCN2. 1 Publication1
Mutagenesisi124E → A: Decreases affinity for MBL2. Slight decrease in affinity for FCN2. 1 Publication1
Mutagenesisi444R → Q: Abolishes autocatalytic cleavage. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi10747.
MalaCardsiMASP2.
MIMi613791. phenotype.
OpenTargetsiENSG00000009724.
Orphaneti331187. Immunodeficiency due to MASP-2 deficiency.
PharmGKBiPA30645.

Polymorphism and mutation databases

BioMutaiMASP2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 15Sequence analysisAdd BLAST15
ChainiPRO_000002759816 – 686Mannan-binding lectin serine protease 2Add BLAST671
ChainiPRO_000002759916 – 444Mannan-binding lectin serine protease 2 A chainAdd BLAST429
ChainiPRO_0000027600445 – 686Mannan-binding lectin serine protease 2 B chainAdd BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi72 ↔ 90
Disulfide bondi142 ↔ 156
Disulfide bondi152 ↔ 165
Modified residuei158(3R)-3-hydroxyasparagineSequence analysis1
Disulfide bondi167 ↔ 180
Disulfide bondi184 ↔ 211By similarity
Disulfide bondi241 ↔ 259By similarity
Disulfide bondi300 ↔ 348By similarity
Disulfide bondi328 ↔ 361By similarity
Disulfide bondi366 ↔ 412
Disulfide bondi396 ↔ 430
Disulfide bondi434 ↔ 552Interchain (between A and B chains)
Disulfide bondi598 ↔ 618
Disulfide bondi629 ↔ 660

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei444 – 445CleavageBy similarity2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Hydroxylation

Proteomic databases

PaxDbiO00187.
PeptideAtlasiO00187.
PRIDEiO00187.

PTM databases

iPTMnetiO00187.
PhosphoSitePlusiO00187.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSG00000009724.
GenevisibleiO00187. HS.

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.3 Publications

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • complement component C4b binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi115970. 5 interactors.
IntActiO00187. 1 interactor.
MINTiMINT-7970114.
STRINGi9606.ENSP00000383690.

Structurei

Secondary structure

1686
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 31Combined sources5
Turni33 – 36Combined sources4
Beta strandi44 – 50Combined sources7
Beta strandi55 – 65Combined sources11
Beta strandi74 – 89Combined sources16
Turni93 – 96Combined sources4
Beta strandi98 – 100Combined sources3
Beta strandi109 – 118Combined sources10
Beta strandi129 – 138Combined sources10
Beta strandi151 – 159Combined sources9
Beta strandi162 – 166Combined sources5
Beta strandi171 – 173Combined sources3
Beta strandi309 – 313Combined sources5
Beta strandi323 – 328Combined sources6
Beta strandi332 – 336Combined sources5
Beta strandi345 – 348Combined sources4
Beta strandi350 – 356Combined sources7
Beta strandi360 – 363Combined sources4
Beta strandi375 – 382Combined sources8
Beta strandi391 – 396Combined sources6
Turni398 – 400Combined sources3
Beta strandi401 – 403Combined sources3
Beta strandi409 – 412Combined sources4
Beta strandi416 – 420Combined sources5
Beta strandi430 – 432Combined sources3
Beta strandi459 – 473Combined sources15
Turni474 – 476Combined sources3
Beta strandi477 – 480Combined sources4
Helixi482 – 485Combined sources4
Turni487 – 490Combined sources4
Beta strandi496 – 500Combined sources5
Beta strandi510 – 519Combined sources10
Beta strandi534 – 540Combined sources7
Helixi558 – 561Combined sources4
Beta strandi567 – 573Combined sources7
Beta strandi577 – 579Combined sources3
Beta strandi586 – 592Combined sources7
Helixi595 – 603Combined sources9
Beta strandi604 – 606Combined sources3
Beta strandi616 – 620Combined sources5
Beta strandi636 – 641Combined sources6
Turni642 – 645Combined sources4
Beta strandi646 – 659Combined sources14
Beta strandi667 – 671Combined sources5
Helixi672 – 675Combined sources4
Helixi676 – 685Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5JPMX-ray3.75G/I291-444[»]
H/J445-686[»]
ProteinModelPortaliO00187.
SMRiO00187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00187.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 137CUB 1PROSITE-ProRule annotationAdd BLAST122
Domaini138 – 181EGF-like; calcium-bindingAdd BLAST44
Domaini184 – 296CUB 2PROSITE-ProRule annotationAdd BLAST113
Domaini298 – 363Sushi 1PROSITE-ProRule annotationAdd BLAST66
Domaini364 – 432Sushi 2PROSITE-ProRule annotationAdd BLAST69
Domaini445 – 684Peptidase S1PROSITE-ProRule annotationAdd BLAST240

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 CUB domains.PROSITE-ProRule annotation
Contains 1 EGF-like domain.Curated
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOVERGENiHBG000559.
InParanoidiO00187.
KOiK03993.
OMAiWTLTAPP.
OrthoDBiEOG091G02DS.
PhylomeDBiO00187.
TreeFamiTF330373.

Family and domain databases

CDDicd00033. CCP. 2 hits.
cd00041. CUB. 2 hits.
cd00190. Tryp_SPc. 1 hit.
Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR001254. Trypsin_dom.
IPR033116. TRYPSIN_SER.
[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.
SM00181. EGF. 1 hit.
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. AlignAdd to basket

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

        10         20         30         40         50
MRLLTLLGLL CGSVATPLGP KWPEPVFGRL ASPGFPGEYA NDQERRWTLT
60 70 80 90 100
APPGYRLRLY FTHFDLELSH LCEYDFVKLS SGAKVLATLC GQESTDTERA
110 120 130 140 150
PGKDTFYSLG SSLDITFRSD YSNEKPFTGF EAFYAAEDID ECQVAPGEAP
160 170 180 190 200
TCDHHCHNHL GGFYCSCRAG YVLHRNKRTC SALCSGQVFT QRSGELSSPE
210 220 230 240 250
YPRPYPKLSS CTYSISLEEG FSVILDFVES FDVETHPETL CPYDFLKIQT
260 270 280 290 300
DREEHGPFCG KTLPHRIETK SNTVTITFVT DESGDHTGWK IHYTSTAQPC
310 320 330 340 350
PYPMAPPNGH VSPVQAKYIL KDSFSIFCET GYELLQGHLP LKSFTAVCQK
360 370 380 390 400
DGSWDRPMPA CSIVDCGPPD DLPSGRVEYI TGPGVTTYKA VIQYSCEETF
410 420 430 440 450
YTMKVNDGKY VCEADGFWTS SKGEKSLPVC EPVCGLSART TGGRIYGGQK
460 470 480 490 500
AKPGDFPWQV LILGGTTAAG ALLYDNWVLT AAHAVYEQKH DASALDIRMG
510 520 530 540 550
TLKRLSPHYT QAWSEAVFIH EGYTHDAGFD NDIALIKLNN KVVINSNITP
560 570 580 590 600
ICLPRKEAES FMRTDDIGTA SGWGLTQRGF LARNLMYVDI PIVDHQKCTA
610 620 630 640 650
AYEKPPYPRG SVTANMLCAG LESGGKDSCR GDSGGALVFL DSETERWFVG
660 670 680
GIVSWGSMNC GEAGQYGVYT KVINYIPWIE NIISDF
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti41N → S in BAF83512 (PubMed:14702039).Curated1
Sequence conflicti225L → P in BAF83512 (PubMed:14702039).Curated1
Sequence conflicti298 – 299QP → HA in CAA71059 (PubMed:9087411).Curated2
Sequence conflicti298 – 299QP → HA in CAB50733 (PubMed:10092804).Curated2
Sequence conflicti298 – 299QP → HA in CAB50735 (PubMed:10092804).Curated2
Sequence conflicti298 – 299QP → HA in CAA67050 (Ref. 4) Curated2
Sequence conflicti298 – 299QP → HA in AAG50274 (Ref. 6) Curated2
Sequence conflicti361 – 362Missing in CAB50733 (PubMed:10092804).Curated2
Sequence conflicti361 – 362Missing in CAB50735 (PubMed:10092804).Curated2
Sequence conflicti372L → LCS in CAB50733 (PubMed:10092804).Curated1
Sequence conflicti372L → LCS in CAB50735 (PubMed:10092804).Curated1
Sequence conflicti399T → A in BAF83512 (PubMed:14702039).Curated1
Sequence conflicti442G → E in AAG50274 (Ref. 6) Curated1
Sequence conflicti447G → E in AAG50274 (Ref. 6) Curated1
Sequence conflicti461 – 462Missing in CAB50733 (PubMed:10092804).Curated2
Sequence conflicti461 – 462Missing in CAB50735 (PubMed:10092804).Curated2
Sequence conflicti473L → LIL in CAB50733 (PubMed:10092804).Curated1
Sequence conflicti473L → LIL in CAB50735 (PubMed:10092804).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02534499R → Q.2 PublicationsCorresponds to variant rs61735600dbSNPEnsembl.1
Natural variantiVAR_025345118R → C.2 PublicationsCorresponds to variant rs147270785dbSNPEnsembl.1
Natural variantiVAR_025346120D → G in MASPD; found in a patient suffering from frequent infections and chronic inflammatory disease; strongly decreases affinity for MBL2 and FCN2. 4 PublicationsCorresponds to variant rs72550870dbSNPEnsembl.1
Natural variantiVAR_025347126P → L in MASPD. 2 PublicationsCorresponds to variant rs56392418dbSNPEnsembl.1
Natural variantiVAR_075087128T → M.1 PublicationCorresponds to variant rs141145402dbSNPEnsembl.1
Natural variantiVAR_028784155H → R.Corresponds to variant rs2273343dbSNPEnsembl.1
Natural variantiVAR_065814156C → CHNH in MASPD. 1
Natural variantiVAR_028785371D → Y.1 PublicationCorresponds to variant rs12711521dbSNPEnsembl.1
Natural variantiVAR_028786377V → A Associated with reduced MASP2 levels in plasma; no effect on catalytic activity. 2 PublicationsCorresponds to variant rs2273346dbSNPEnsembl.1
Natural variantiVAR_075088405V → M.1 PublicationCorresponds to variant rs61735594dbSNPEnsembl.1
Natural variantiVAR_028787439R → H.Corresponds to variant rs12085877dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005383182 – 185ALCS → EQSL in isoform 2. 2 Publications4
Alternative sequenceiVSP_005384186 – 686Missing in isoform 2. 2 PublicationsAdd BLAST501

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [O00187-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

MASP2base

MASP2 mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5JPMX-ray3.75G/I291-444[»]
H/J445-686[»]
ProteinModelPortaliO00187.
SMRiO00187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115970. 5 interactors.
IntActiO00187. 1 interactor.
MINTiMINT-7970114.
STRINGi9606.ENSP00000383690.

Protein family/group databases

MEROPSiS01.229.

PTM databases

iPTMnetiO00187.
PhosphoSitePlusiO00187.

Polymorphism and mutation databases

BioMutaiMASP2.

Proteomic databases

PaxDbiO00187.
PeptideAtlasiO00187.
PRIDEiO00187.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000400897; ENSP00000383690; ENSG00000009724. [O00187-1]
ENST00000400898; ENSP00000383691; ENSG00000009724. [O00187-2]
GeneIDi10747.
KEGGihsa:10747.
UCSCiuc001aru.4. human. [O00187-1]

Organism-specific databases

CTDi10747.
DisGeNETi10747.
GeneCardsiMASP2.
HGNCiHGNC:6902. MASP2.
HPAiHPA029313.
HPA029314.
MalaCardsiMASP2.
MIMi605102. gene.
613791. phenotype.
neXtProtiNX_O00187.
OpenTargetsiENSG00000009724.
Orphaneti331187. Immunodeficiency due to MASP-2 deficiency.
PharmGKBiPA30645.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOVERGENiHBG000559.
InParanoidiO00187.
KOiK03993.
OMAiWTLTAPP.
OrthoDBiEOG091G02DS.
PhylomeDBiO00187.
TreeFamiTF330373.

Enzyme and pathway databases

BioCyciZFISH:HS00265-MONOMER.
BRENDAi3.4.21.104. 2681.
ReactomeiR-HSA-166662. Lectin pathway of complement activation.
R-HSA-166663. Initial triggering of complement.
R-HSA-2855086. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
SABIO-RKO00187.

Miscellaneous databases

EvolutionaryTraceiO00187.
GenomeRNAii10747.
PROiO00187.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000009724.
GenevisibleiO00187. HS.

Family and domain databases

CDDicd00033. CCP. 2 hits.
cd00041. CUB. 2 hits.
cd00190. Tryp_SPc. 1 hit.
Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR001254. Trypsin_dom.
IPR033116. TRYPSIN_SER.
[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.
SM00181. EGF. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 187 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

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 one 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.