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P48740

- MASP1_HUMAN

UniProt

P48740 - MASP1_HUMAN

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Protein

Mannan-binding lectin serine protease 1

Gene

MASP1

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

Functioni

Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5.1 Publication

Enzyme regulationi

Inhibited by SERPING1 and A2M.2 Publications

Kineticsi

  1. KM=0.10 mM for Ac-Gly-Lys-OMe (at 30 degrees Celsius)2 Publications
  2. KM=310 µM for Bz-Arg-OEt (at 30 degrees Celsius)2 Publications
  3. KM=4.8 µM for C2 (at 37 degrees Celsius)2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi68 – 681Calcium 1
Metal bindingi76 – 761Calcium 1
Metal bindingi121 – 1211Calcium 1
Metal bindingi123 – 1231Calcium 1; via carbonyl oxygen
Metal bindingi139 – 1391Calcium 2
Metal bindingi140 – 1401Calcium 2; via carbonyl oxygen
Metal bindingi142 – 1421Calcium 2
Metal bindingi159 – 1591Calcium 2
Metal bindingi160 – 1601Calcium 2; via carbonyl oxygen
Metal bindingi163 – 1631Calcium 2; via carbonyl oxygen
Metal bindingi235 – 2351Calcium 3
Metal bindingi245 – 2451Calcium 3
Metal bindingi282 – 2821Calcium 3
Metal bindingi284 – 2841Calcium 3; via carbonyl oxygen
Sitei448 – 4492Cleavage; by autolysis
Active sitei490 – 4901Charge relay systemBy similarity
Active sitei552 – 5521Charge relay systemBy similarity
Active sitei646 – 6461Charge relay systemBy similarity

GO - Molecular functioni

  1. calcium-dependent protein binding Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. peptidase activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. complement activation Source: Reactome
  2. complement activation, lectin pathway Source: UniProtKB
  3. innate immune response Source: Reactome
  4. negative regulation of complement activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement activation lectin pathway, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_163699. Scavenging by Class A Receptors.
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.
SABIO-RKP48740.

Protein family/group databases

MEROPSiS01.132.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan-binding lectin serine protease 1 (EC:3.4.21.-)
Alternative name(s):
Complement factor MASP-3
Complement-activating component of Ra-reactive factor
Mannose-binding lectin-associated serine protease 1
Short name:
MASP-1
Mannose-binding protein-associated serine protease
Ra-reactive factor serine protease p100
Short name:
RaRF
Serine protease 5
Cleaved into the following 2 chains:
Gene namesi
Name:MASP1
Synonyms:CRARF, CRARF1, PRSS5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:6901. MASP1.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

3MC syndrome 1 (3MC1) [MIM:257920]: A disorder characterized by facial dysmorphism that includes hypertelorism, blepharophimosis, blepharoptosis and highly arched eyebrows, cleft lip and/or palate, craniosynostosis, learning disability and genital, limb and vesicorenal anomalies. The term 3MC syndrome includes Carnevale, Mingarelli, Malpuech, and Michels syndromes.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: P48740-2)
Natural varianti497 – 4971H → Y in 3MC1. 1 Publication
Natural varianti630 – 6301C → R in 3MC1. 1 Publication
Natural varianti666 – 6661G → E in 3MC1. 1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681E → A or Q: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi77 – 771Y → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi99 – 991E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi121 – 1211D → A or N: Loss of interaction with FNC2 and FCN3 and partial loss of interaction with MBL2. 1 Publication
Mutagenesisi122 – 1221F → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi123 – 1231S → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi125 – 1251E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi237 – 2371H → A: Loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi239 – 2391E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi244 – 2441Y → A: Loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi262 – 2621E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi274 – 2741S → A: Partial loss of interaction with FCN2 and FCN3. No effect on interaction with MBL2. 1 Publication
Mutagenesisi283 – 2831N → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi286 – 2861E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
Mutagenesisi646 – 6461S → A: No autoproteolytic processing. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi257920. phenotype.
Orphaneti293843. Craniofacial-ulnar-renal syndrome.
PharmGKBiPA30644.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 699680Mannan-binding lectin serine protease 1PRO_0000027592Add
BLAST
Chaini20 – 448429Mannan-binding lectin serine protease 1 heavy chainPRO_0000027593Add
BLAST
Chaini449 – 699251Mannan-binding lectin serine protease 1 light chainPRO_0000027594Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi49 – 491N-linked (GlcNAc...)1 Publication
Disulfide bondi73 ↔ 911 Publication
Disulfide bondi143 ↔ 1571 Publication
Disulfide bondi153 ↔ 1661 Publication
Modified residuei159 – 1591(3R)-3-hydroxyasparagineSequence Analysis
Disulfide bondi168 ↔ 1811 Publication
Glycosylationi178 – 1781N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi185 ↔ 2121 Publication
Disulfide bondi242 ↔ 2601 Publication
Disulfide bondi301 ↔ 349By similarity
Disulfide bondi329 ↔ 362By similarity
Disulfide bondi367 ↔ 414By similarity
Glycosylationi385 – 3851N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi397 ↔ 432By similarity
Glycosylationi407 – 4071N-linked (GlcNAc...)1 Publication
Disulfide bondi436 ↔ 572Interchain (between heavy and light chains)PROSITE-ProRule annotation
Disulfide bondi475 ↔ 491By similarity
Disulfide bondi614 ↔ 631By similarity
Disulfide bondi642 ↔ 672By similarity

Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity
N-glycosylated. Some N-linked glycan are of the complex-type By similarity.By similarity
Autoproteolytic processing of the proenzyme produces the active enzyme composed on the heavy and the light chain held together by a disulfide bond. Isoform 1 but not isoform 2 is activated through autoproteolytic processing.1 Publication

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP48740.
PRIDEiP48740.

PTM databases

PhosphoSiteiP48740.

Miscellaneous databases

PMAP-CutDBQ96RS4.

Expressioni

Tissue specificityi

Protein of the plasma which is primarily expressed by liver.4 Publications

Gene expression databases

BgeeiP48740.
CleanExiHS_MASP1.
ExpressionAtlasiP48740. baseline and differential.
GenevestigatoriP48740.

Organism-specific databases

HPAiHPA001617.
HPA009641.

Interactioni

Subunit structurei

Homodimer. Interacts with the oligomeric lectins MBL2, FCN2 and FCN3; triggers the lectin pathway of complement through activation of C3. Interacts with SERPING1.8 Publications

Protein-protein interaction databases

BioGridi111629. 17 interactions.
IntActiP48740. 15 interactions.
MINTiMINT-4657209.

Structurei

Secondary structure

1
699
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 325Combined sources
Turni34 – 374Combined sources
Beta strandi42 – 5110Combined sources
Beta strandi56 – 6611Combined sources
Helixi71 – 733Combined sources
Beta strandi75 – 817Combined sources
Beta strandi86 – 905Combined sources
Beta strandi92 – 998Combined sources
Beta strandi110 – 12011Combined sources
Beta strandi130 – 13910Combined sources
Turni142 – 1443Combined sources
Beta strandi154 – 1607Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi192 – 1998Combined sources
Turni200 – 2034Combined sources
Beta strandi211 – 2177Combined sources
Beta strandi223 – 2286Combined sources
Beta strandi238 – 2447Combined sources
Beta strandi246 – 2516Combined sources
Beta strandi254 – 2596Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi273 – 2808Combined sources
Beta strandi291 – 2977Combined sources
Beta strandi310 – 3145Combined sources
Beta strandi317 – 3204Combined sources
Beta strandi324 – 3296Combined sources
Beta strandi333 – 3375Combined sources
Beta strandi340 – 34910Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi361 – 3644Combined sources
Beta strandi376 – 3827Combined sources
Beta strandi392 – 3976Combined sources
Turni399 – 4013Combined sources
Beta strandi402 – 4043Combined sources
Helixi405 – 4073Combined sources
Beta strandi411 – 4144Combined sources
Turni416 – 4183Combined sources
Beta strandi420 – 4223Combined sources
Turni423 – 4253Combined sources
Beta strandi426 – 4283Combined sources
Beta strandi432 – 4343Combined sources
Beta strandi463 – 4686Combined sources
Beta strandi473 – 4808Combined sources
Turni481 – 4833Combined sources
Beta strandi484 – 4874Combined sources
Helixi489 – 4913Combined sources
Beta strandi499 – 5013Combined sources
Turni505 – 5073Combined sources
Turni511 – 5133Combined sources
Beta strandi514 – 5196Combined sources
Beta strandi522 – 5254Combined sources
Beta strandi531 – 54010Combined sources
Turni546 – 5494Combined sources
Beta strandi554 – 5607Combined sources
Beta strandi565 – 5673Combined sources
Beta strandi583 – 5919Combined sources
Beta strandi594 – 5963Combined sources
Beta strandi602 – 6098Combined sources
Helixi611 – 6188Combined sources
Helixi619 – 6213Combined sources
Beta strandi629 – 6324Combined sources
Beta strandi649 – 6546Combined sources
Turni655 – 6584Combined sources
Beta strandi659 – 6668Combined sources
Helixi672 – 6754Combined sources
Beta strandi677 – 6837Combined sources
Helixi684 – 6874Combined sources
Helixi688 – 6958Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DEMX-ray2.30A/B20-297[»]
3GOVX-ray2.55A298-448[»]
B449-699[»]
4AQBX-ray4.20A20-363[»]
4DJZX-ray3.20A/C298-448[»]
B/D449-699[»]
4IGDX-ray2.50A298-699[»]
4IW4X-ray3.20E/F625-696[»]
4KKDX-ray2.60A/B298-696[»]
ProteinModelPortaliP48740.
SMRiP48740. Positions 22-699.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48740.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 138119CUB 1PROSITE-ProRule annotationAdd
BLAST
Domaini139 – 18244EGF-like; calcium-bindingAdd
BLAST
Domaini185 – 297113CUB 2PROSITE-ProRule annotationAdd
BLAST
Domaini299 – 36466Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini365 – 43470Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini449 – 696248Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 278259Interaction with FCN2Add
BLAST
Regioni20 – 184165HomodimerizationBy similarityAdd
BLAST
Regioni20 – 184165Interaction with MBL2Add
BLAST

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

eggNOGiCOG5640.
GeneTreeiENSGT00760000118890.
HOVERGENiHBG000559.
InParanoidiP48740.
KOiK03992.
OMAiPANICCL.
OrthoDBiEOG7W6WK4.
PhylomeDBiP48740.
TreeFamiTF330373.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
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.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P48740-1) [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
MRWLLLYYAL CFSLSKASAH TVELNNMFGQ IQSPGYPDSY PSDSEVTWNI
60 70 80 90 100
TVPDGFRIKL YFMHFNLESS YLCEYDYVKV ETEDQVLATF CGRETTDTEQ
110 120 130 140 150
TPGQEVVLSP GSFMSITFRS DFSNEERFTG FDAHYMAVDV DECKEREDEE
160 170 180 190 200
LSCDHYCHNY IGGYYCSCRF GYILHTDNRT CRVECSDNLF TQRTGVITSP
210 220 230 240 250
DFPNPYPKSS ECLYTIELEE GFMVNLQFED IFDIEDHPEV PCPYDYIKIK
260 270 280 290 300
VGPKVLGPFC GEKAPEPIST QSHSVLILFH SDNSGENRGW RLSYRAAGNE
310 320 330 340 350
CPELQPPVHG KIEPSQAKYF FKDQVLVSCD TGYKVLKDNV EMDTFQIECL
360 370 380 390 400
KDGTWSNKIP TCKIVDCRAP GELEHGLITF STRNNLTTYK SEIKYSCQEP
410 420 430 440 450
YYKMLNNNTG IYTCSAQGVW MNKVLGRSLP TCLPVCGLPK FSRKLMARIF
460 470 480 490 500
NGRPAQKGTT PWIAMLSHLN GQPFCGGSLL GSSWIVTAAH CLHQSLDPED
510 520 530 540 550
PTLRDSDLLS PSDFKIILGK HWRLRSDENE QHLGVKHTTL HPQYDPNTFE
560 570 580 590 600
NDVALVELLE SPVLNAFVMP ICLPEGPQQE GAMVIVSGWG KQFLQRFPET
610 620 630 640 650
LMEIEIPIVD HSTCQKAYAP LKKKVTRDMI CAGEKEGGKD ACAGDSGGPM
660 670 680 690
VTLNRERGQW YLVGTVSWGD DCGKKDRYGV YSYIHHNKDW IQRVTGVRN
Length:699
Mass (Da):79,247
Last modified:December 16, 2008 - v3
Checksum:i5B37C7FB9F51FD1D
GO
Isoform 2 (identifier: P48740-2) [UniParc]FASTAAdd to Basket

Also known as: MASP-3

The sequence of this isoform differs from the canonical sequence as follows:
     435-435: V → ECGQPSRSLP...QSVVEPQVER
     436-699: Missing.

Note: Glycosylated on Asn-533 and Asn-599.1 Publication

Show »
Length:728
Mass (Da):81,860
Checksum:i09B5297A6C14283A
GO
Isoform 3 (identifier: P48740-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     364-380: IVDCRAPGELEHGLITF → KNEIDLESELKSEQVTE
     381-699: Missing.

Show »
Length:380
Mass (Da):43,640
Checksum:iDDED114311A62714
GO
Isoform 4 (identifier: P48740-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-113: Missing.
     435-435: V → ECGQPSRSLP...QSVVEPQVER
     436-699: Missing.

Show »
Length:615
Mass (Da):68,918
Checksum:iEEE63886709340FA
GO

Sequence cautioni

The sequence AAH39724.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21R → K in BAF84375. (PubMed:14702039)Curated
Sequence conflicti89 – 891T → A in CAH18409. (PubMed:17974005)Curated
Sequence conflicti232 – 2321F → L in BAF84375. (PubMed:14702039)Curated
Sequence conflicti235 – 2351E → Q in BAA05928. (PubMed:8018603)Curated
Sequence conflicti235 – 2351E → Q in BAA34864. (PubMed:8921412)Curated
Sequence conflicti285 – 2851G → A in BAA05928. (PubMed:8018603)Curated
Sequence conflicti285 – 2851G → A in BAA34864. (PubMed:8921412)Curated
Sequence conflicti285 – 2851G → A in BAA89206. (PubMed:10475605)Curated
Sequence conflicti392 – 3921E → G in BAF83846. (PubMed:14702039)Curated
Sequence conflicti499 – 4991E → G in BAA05928. (PubMed:8018603)Curated
Sequence conflicti499 – 4991E → K in BAA04477. (PubMed:8240317)Curated
Sequence conflicti499 – 4991E → K in BAA89206. (PubMed:10475605)Curated
Sequence conflicti527 – 5271D → A in BAA34864. (PubMed:8921412)Curated
Sequence conflicti543 – 5431Q → K in BAA04477. (PubMed:8240317)Curated
Sequence conflicti552 – 5521D → V in BAA34864. (PubMed:8921412)Curated
Sequence conflicti643 – 6431A → S in BAA04477. (PubMed:8240317)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211T → I.
Corresponds to variant rs1062049 [ dbSNP | Ensembl ].
VAR_051831
Natural varianti568 – 5681V → A.
Corresponds to variant rs13322090 [ dbSNP | Ensembl ].
VAR_051832
Natural varianti679 – 6791G → R.
Corresponds to variant rs3774266 [ dbSNP | Ensembl ].
VAR_051833
Isoform 2 (identifier: P48740-2)
Natural varianti497 – 4971H → Y in 3MC1. 1 Publication
Natural varianti630 – 6301C → R in 3MC1. 1 Publication
Natural varianti666 – 6661G → E in 3MC1. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 113113Missing in isoform 4. 1 PublicationVSP_036809Add
BLAST
Alternative sequencei364 – 38017IVDCR…GLITF → KNEIDLESELKSEQVTE in isoform 3. 2 PublicationsVSP_036810Add
BLAST
Alternative sequencei381 – 699319Missing in isoform 3. 2 PublicationsVSP_036811Add
BLAST
Alternative sequencei435 – 4351V → ECGQPSRSLPSLVKRIIGGR NAEPGLFPWQALIVVEDTSR VPNDKWFGSGALLSASWILT AAHVLRSQRRDTTVIPVSKE HVTVYLGLHDVRDKSGAVNS SAARVVLHPDFNIQNYNHDI ALVQLQEPVPLGPHVMPVCL PRLEPEGPAPHMLGLVAGWG ISNPNVTVDEIISSGTRTLS DVLQYVKLPVVPHAECKTSY ESRSGNYSVTENMFCAGYYE GGKDTCLGDSGGAFVIFDDL SQRWVVQGLVSWGGPEECGS KQVYGVYTKVSNYVDWVWEQ MGLPQSVVEPQVER in isoform 2 and isoform 4. 3 PublicationsVSP_036812
Alternative sequencei436 – 699264Missing in isoform 2 and isoform 4. 3 PublicationsVSP_036813Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D17525 mRNA. Translation: BAA04477.1.
D28593 mRNA. Translation: BAA05928.1.
D61695 Genomic DNA. Translation: BAA34864.1.
AB007617 Genomic DNA. Translation: BAA89206.1.
AF284421 mRNA. Translation: AAK84071.1.
AK291157 mRNA. Translation: BAF83846.1.
AK291686 mRNA. Translation: BAF84375.1.
AK304334 mRNA. Translation: BAG65179.1.
CR749615 mRNA. Translation: CAH18409.1.
AC007920 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78153.1.
BC039724 mRNA. Translation: AAH39724.1. Different initiation.
BC106945 mRNA. Translation: AAI06946.1.
BC106946 mRNA. Translation: AAI06947.1.
CCDSiCCDS33907.1. [P48740-1]
CCDS33908.1. [P48740-2]
CCDS33909.1. [P48740-3]
PIRiI54763.
RefSeqiNP_001027019.1. NM_001031849.2. [P48740-3]
NP_001870.3. NM_001879.5. [P48740-1]
NP_624302.1. NM_139125.3. [P48740-2]
UniGeneiHs.89983.

Genome annotation databases

EnsembliENST00000169293; ENSP00000169293; ENSG00000127241. [P48740-3]
ENST00000296280; ENSP00000296280; ENSG00000127241. [P48740-2]
ENST00000337774; ENSP00000336792; ENSG00000127241. [P48740-1]
ENST00000392472; ENSP00000376264; ENSG00000127241. [P48740-4]
GeneIDi5648.
KEGGihsa:5648.
UCSCiuc003frh.2. human. [P48740-1]
uc003fri.3. human. [P48740-2]
uc003frk.2. human. [P48740-3]

Polymorphism databases

DMDMi218512135.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D17525 mRNA. Translation: BAA04477.1 .
D28593 mRNA. Translation: BAA05928.1 .
D61695 Genomic DNA. Translation: BAA34864.1 .
AB007617 Genomic DNA. Translation: BAA89206.1 .
AF284421 mRNA. Translation: AAK84071.1 .
AK291157 mRNA. Translation: BAF83846.1 .
AK291686 mRNA. Translation: BAF84375.1 .
AK304334 mRNA. Translation: BAG65179.1 .
CR749615 mRNA. Translation: CAH18409.1 .
AC007920 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78153.1 .
BC039724 mRNA. Translation: AAH39724.1 . Different initiation.
BC106945 mRNA. Translation: AAI06946.1 .
BC106946 mRNA. Translation: AAI06947.1 .
CCDSi CCDS33907.1. [P48740-1 ]
CCDS33908.1. [P48740-2 ]
CCDS33909.1. [P48740-3 ]
PIRi I54763.
RefSeqi NP_001027019.1. NM_001031849.2. [P48740-3 ]
NP_001870.3. NM_001879.5. [P48740-1 ]
NP_624302.1. NM_139125.3. [P48740-2 ]
UniGenei Hs.89983.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DEM X-ray 2.30 A/B 20-297 [» ]
3GOV X-ray 2.55 A 298-448 [» ]
B 449-699 [» ]
4AQB X-ray 4.20 A 20-363 [» ]
4DJZ X-ray 3.20 A/C 298-448 [» ]
B/D 449-699 [» ]
4IGD X-ray 2.50 A 298-699 [» ]
4IW4 X-ray 3.20 E/F 625-696 [» ]
4KKD X-ray 2.60 A/B 298-696 [» ]
ProteinModelPortali P48740.
SMRi P48740. Positions 22-699.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111629. 17 interactions.
IntActi P48740. 15 interactions.
MINTi MINT-4657209.

Protein family/group databases

MEROPSi S01.132.

PTM databases

PhosphoSitei P48740.

Polymorphism databases

DMDMi 218512135.

Proteomic databases

PaxDbi P48740.
PRIDEi P48740.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000169293 ; ENSP00000169293 ; ENSG00000127241 . [P48740-3 ]
ENST00000296280 ; ENSP00000296280 ; ENSG00000127241 . [P48740-2 ]
ENST00000337774 ; ENSP00000336792 ; ENSG00000127241 . [P48740-1 ]
ENST00000392472 ; ENSP00000376264 ; ENSG00000127241 . [P48740-4 ]
GeneIDi 5648.
KEGGi hsa:5648.
UCSCi uc003frh.2. human. [P48740-1 ]
uc003fri.3. human. [P48740-2 ]
uc003frk.2. human. [P48740-3 ]

Organism-specific databases

CTDi 5648.
GeneCardsi GC03M186935.
HGNCi HGNC:6901. MASP1.
HPAi HPA001617.
HPA009641.
MIMi 257920. phenotype.
600521. gene.
neXtProti NX_P48740.
Orphaneti 293843. Craniofacial-ulnar-renal syndrome.
PharmGKBi PA30644.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000118890.
HOVERGENi HBG000559.
InParanoidi P48740.
KOi K03992.
OMAi PANICCL.
OrthoDBi EOG7W6WK4.
PhylomeDBi P48740.
TreeFami TF330373.

Enzyme and pathway databases

Reactomei REACT_163699. Scavenging by Class A Receptors.
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.
SABIO-RK P48740.

Miscellaneous databases

ChiTaRSi MASP1. human.
EvolutionaryTracei P48740.
GeneWikii MASP1_(protein).
GenomeRNAii 5648.
NextBioi 21938.
PMAP-CutDB Q96RS4.
PROi P48740.
SOURCEi Search...

Gene expression databases

Bgeei P48740.
CleanExi HS_MASP1.
ExpressionAtlasi P48740. baseline and differential.
Genevestigatori P48740.

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.
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.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A new member of the C1s family of complement proteins found in a bactericidal factor, Ra-reactive factor, in human serum."
    Takada F., Takayama Y., Hatsuse H., Kawakami M.
    Biochem. Biophys. Res. Commun. 196:1003-1009(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein."
    Sato T., Endo Y., Matsushita M., Fujita T.
    Int. Immunol. 6:665-669(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Fetal liver.
  3. "Exon structure of the gene encoding the human mannose-binding protein-associated serine protease light chain: comparison with complement C1r and C1s genes."
    Endo Y., Sato T., Matsushita M., Fujita T.
    Int. Immunol. 8:1355-1358(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  4. "Gene structure of the P100 serine-protease component of the human Ra-reactive factor."
    Takayama Y., Takada F., Nowatari M., Kawakami M., Matsu-ura N.
    Mol. Immunol. 36:505-514(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway."
    Dahl M.R., Thiel S., Matsushita M., Fujita T., Willis A.C., Christensen T., Vorup-Jensen T., Jensenius J.C.
    Immunity 15:127-135(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 450-474; 506-526; 539-555; 577-590; 613-621 AND 679-695 (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Liver.
  6. "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] (ISOFORMS 2 AND 4).
    Tissue: Placenta, Teratocarcinoma and Trachea.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Fetal brain.
  8. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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 2 AND 3).
    Tissue: Fetal brain.
  11. "Interaction properties of human mannan-binding lectin (MBL)-associated serine proteases-1 and -2, MBL-associated protein 19, and MBL."
    Thielens N.M., Cseh S., Thiel S., Vorup-Jensen T., Rossi V., Jensenius J.C., Arlaud G.J.
    J. Immunol. 166:5068-5077(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-29 AND 449-458, SIGNAL SEQUENCE CLEAVAGE SITE, CLEAVAGE AT ARG-448, GLYCOSYLATION, HOMODIMERIZATION, INTERACTION WITH MBL2.
  12. "Human serum mannose-binding lectin (MBL)-associated serine protease-1 (MASP-1): determination of levels in body fluids and identification of two forms in serum."
    Terai I., Kobayashi K., Matsushita M., Fujita T.
    Clin. Exp. Immunol. 110:317-323(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. Cited for: INTERACTION WITH MBL2.
    Tissue: Liver.
  14. "Complement-activating complex of ficolin and mannose-binding lectin-associated serine protease."
    Matsushita M., Endo Y., Fujita T.
    J. Immunol. 164:2281-2284(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCN2.
  15. "Interaction of C1q and mannan-binding lectin (MBL) with C1r, C1s, MBL-associated serine proteases 1 and 2, and the MBL-associated protein MAp19."
    Thiel S., Petersen S.V., Vorup-Jensen T., Matsushita M., Fujita T., Stover C.M., Schwaeble W.J., Jensenius J.C.
    J. Immunol. 165:878-887(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MBL2.
  16. "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: CATALYTIC ACTIVITY, INTERACTION WITH SERPING1.
  17. "Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2."
    Rossi V., Cseh S., Bally I., Thielens N.M., Jensenius J.C., Arlaud G.J.
    J. Biol. Chem. 276:40880-40887(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  18. "Activation of the lectin complement pathway by H-ficolin (Hakata antigen)."
    Matsushita M., Kuraya M., Hamasaki N., Tsujimura M., Shiraki H., Fujita T.
    J. Immunol. 168:3502-3506(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCN3.
  19. "Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2."
    Cseh S., Vera L., Matsushita M., Fujita T., Arlaud G.J., Thielens N.M.
    J. Immunol. 169:5735-5743(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCN2.
  20. "Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments."
    Ambrus G., Gal P., Kojima M., Szilagyi K., Balczer J., Antal J., Graf L., Laich A., Moffatt B.E., Schwaeble W., Sim R.B., Zavodszky P.
    J. Immunol. 170:1374-1382(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  21. "Characterization of recombinant mannan-binding lectin-associated serine protease (MASP)-3 suggests an activation mechanism different from that of MASP-1 and MASP-2."
    Zundel S., Cseh S., Lacroix M., Dahl M.R., Matsushita M., Andrieu J.-P., Schwaeble W.J., Jensenius J.C., Fujita T., Arlaud G.J., Thielens N.M.
    J. Immunol. 172:4342-4350(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION (ISOFORM 2), MUTAGENESIS OF SER-646, AUTOCATALYTIC CLEAVAGE.
  22. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49; ASN-178; ASN-385; ASN-407 (ISOFORM 1), GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-533 AND ASN-599 (ISOFORM 2).
    Tissue: Plasma.
  23. "Mannan-binding lectin-associated serine protease 3 cleaves synthetic peptides and insulin-like growth factor-binding protein 5."
    Cortesio C.L., Jiang W.
    Arch. Biochem. Biophys. 449:164-170(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY (ISOFORM 2).
  24. "Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway."
    Moeller-Kristensen M., Thiel S., Sjoeholm A., Matsushita M., Jensenius J.C.
    Int. Immunol. 19:141-149(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORMS 1 AND 2).
  25. Cited for: GLYCOSYLATION AT ASN-178 AND ASN-385.
  26. "Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins."
    Teillet F., Gaboriaud C., Lacroix M., Martin L., Arlaud G.J., Thielens N.M.
    J. Biol. Chem. 283:25715-25724(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 20-295 IN COMPLEX WITH CALCIUM IONS, HOMODIMERIZATION, GLYCOSYLATION AT ASN-178, DISULFIDE BONDS, CALCIUM-BINDING SITES, INTERACTION WITH FCN2; FCN3 AND MBL2, MUTAGENESIS OF GLU-68; TYR-77; GLU-99; ASP-121; PHE-122; SER-123; GLU-125; HIS-237; GLU-239; TYR-244; GLU-262; SER-274; ASN-283 AND GLU-286.
  27. Cited for: VARIANTS 3MC1 TYR-497; ARG-630 AND GLU-666 (ISOFORM 2).

Entry informationi

Entry nameiMASP1_HUMAN
AccessioniPrimary (citable) accession number: P48740
Secondary accession number(s): A8K542
, A8K6M1, B4E2L7, O95570, Q68D21, Q8IUV8, Q96RS4, Q9UF09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 16, 2008
Last modified: October 29, 2014
This is version 151 of the entry and version 3 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 3
    Human chromosome 3: 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