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P00736

- C1R_HUMAN

UniProt

P00736 - C1R_HUMAN

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Protein
Complement C1r subcomponent
Gene
C1R
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.

Catalytic activityi

Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form the active form of C1s (EC 3.4.21.42).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei502 – 5021Charge relay system
Active sitei557 – 5571Charge relay system
Active sitei654 – 6541Charge relay system

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. protein binding Source: IntAct
  3. serine-type endopeptidase activity Source: Reactome
  4. serine-type peptidase activity Source: ProtInc

GO - Biological processi

  1. complement activation Source: Reactome
  2. complement activation, classical pathway Source: Reactome
  3. immune response Source: ProtInc
  4. innate immune response Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_7956. Classical antibody-mediated complement activation.
REACT_8024. Initial triggering of complement.

Protein family/group databases

MEROPSiS01.192.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C1r subcomponent (EC:3.4.21.41)
Alternative name(s):
Complement component 1 subcomponent r
Cleaved into the following 2 chains:
Gene namesi
Name:C1R
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:1246. C1R.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

MIMi216950. phenotype.
Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
PharmGKBiPA25635.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 Publication
Add
BLAST
Chaini18 – 705688Complement C1r subcomponent
PRO_0000027577Add
BLAST
Chaini18 – 463446Complement C1r subcomponent heavy chain
PRO_0000027578Add
BLAST
Chaini464 – 705242Complement C1r subcomponent light chain
PRO_0000027579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi71 ↔ 89 Inferred
Glycosylationi125 – 1251N-linked (GlcNAc...)1 Publication
Disulfide bondi146 ↔ 165
Disulfide bondi161 ↔ 174
Modified residuei167 – 1671(3R)-3-hydroxyasparagine
Disulfide bondi176 ↔ 189
Disulfide bondi193 ↔ 220 Inferred
Modified residuei206 – 2061Phosphoserine; by CK21 Publication
Glycosylationi221 – 2211N-linked (GlcNAc...)1 Publication
Disulfide bondi250 ↔ 268 Inferred
Disulfide bondi309 ↔ 358
Disulfide bondi338 ↔ 371
Disulfide bondi376 ↔ 429
Disulfide bondi406 ↔ 447
Disulfide bondi451 ↔ 577Interchain (between heavy and light chains)
Glycosylationi514 – 5141N-linked (GlcNAc...)2 Publications
Glycosylationi581 – 5811N-linked (GlcNAc...)
Disulfide bondi620 ↔ 639
Disulfide bondi650 ↔ 680

Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

PaxDbiP00736.
PeptideAtlasiP00736.
PRIDEiP00736.

PTM databases

PhosphoSiteiP00736.

Expressioni

Gene expression databases

BgeeiP00736.
CleanExiHS_C1R.
GenevestigatoriP00736.

Organism-specific databases

HPAiHPA001551.

Interactioni

Subunit structurei

C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. C1r is a dimer of identical chains, each of which is activated by cleavage into two chains, A and B, connected by disulfide bonds.

Binary interactionsi

WithEntry#Exp.IntActNotes
C1SP098713EBI-3926504,EBI-2810045

Protein-protein interaction databases

BioGridi107176. 6 interactions.
IntActiP00736. 3 interactions.
MINTiMINT-8045732.
STRINGi9606.ENSP00000290575.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni145 – 1473
Turni150 – 1523
Beta strandi156 – 1583
Beta strandi162 – 1687
Beta strandi171 – 1755
Beta strandi319 – 3224
Beta strandi326 – 3283
Beta strandi333 – 3386
Beta strandi342 – 3465
Beta strandi349 – 3524
Beta strandi355 – 3584
Beta strandi364 – 3663
Beta strandi370 – 3734
Beta strandi385 – 3928
Beta strandi401 – 4066
Turni408 – 4103
Beta strandi411 – 4133
Beta strandi426 – 4294
Beta strandi433 – 4375
Turni438 – 4403
Beta strandi447 – 4493
Beta strandi478 – 49215
Turni493 – 4953
Beta strandi496 – 4994
Helixi501 – 5044
Beta strandi518 – 5225
Helixi526 – 5327
Beta strandi537 – 5426
Beta strandi548 – 5525
Beta strandi559 – 5657
Beta strandi571 – 5733
Helixi582 – 5854
Beta strandi590 – 5956
Beta strandi600 – 6023
Beta strandi608 – 6147
Helixi617 – 62610
Beta strandi637 – 6415
Helixi643 – 6508
Turni651 – 6555
Beta strandi657 – 6615
Turni663 – 6653
Beta strandi668 – 6769
Beta strandi678 – 6836
Beta strandi685 – 6895
Helixi690 – 6934
Helixi694 – 7007

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1APQNMR-A140-192[»]
1GPZX-ray2.90A/B307-705[»]
1MD7X-ray3.20A375-702[»]
1MD8X-ray2.80A375-703[»]
2QY0X-ray2.60A/C309-463[»]
B/D464-705[»]
DisProtiDP00621.
ProteinModelPortaliP00736.
SMRiP00736. Positions 25-703.

Miscellaneous databases

EvolutionaryTraceiP00736.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 141124CUB 1
Add
BLAST
Domaini142 – 19049EGF-like; calcium-binding Reviewed prediction
Add
BLAST
Domaini193 – 305113CUB 2
Add
BLAST
Domaini307 – 37367Sushi 1
Add
BLAST
Domaini374 – 44976Sushi 2
Add
BLAST
Domaini464 – 702239Peptidase S1
Add
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.
KOiK01330.
OrthoDBiEOG7W6WK4.
PhylomeDBiP00736.
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.
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]

Sequencei

Sequence statusi: Complete.

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

P00736-1 [UniParc]FASTAAdd to Basket

« Hide

MWLLYLLVPA LFCRAGGSIP IPQKLFGEVT SPLFPKPYPN NFETTTVITV    50
PTGYRVKLVF QQFDLEPSEG CFYDYVKISA DKKSLGRFCG QLGSPLGNPP 100
GKKEFMSQGN KMLLTFHTDF SNEENGTIMF YKGFLAYYQA VDLDECASRS 150
KSGEEDPQPQ CQHLCHNYVG GYFCSCRPGY ELQEDTHSCQ AECSSELYTE 200
ASGYISSLEY PRSYPPDLRC NYSIRVERGL TLHLKFLEPF DIDDHQQVHC 250
PYDQLQIYAN GKNIGEFCGK QRPPDLDTSS NAVDLLFFTD ESGDSRGWKL 300
RYTTEIIKCP QPKTLDEFTI IQNLQPQYQF RDYFIATCKQ GYQLIEGNQV 350
LHSFTAVCQD DGTWHRAMPR CKIKDCGQPR NLPNGDFRYT TTMGVNTYKA 400
RIQYYCHEPY YKMQTRAGSR ESEQGVYTCT AQGIWKNEQK GEKIPRCLPV 450
CGKPVNPVEQ RQRIIGGQKA KMGNFPWQVF TNIHGRGGGA LLGDRWILTA 500
AHTLYPKEHE AQSNASLDVF LGHTNVEELM KLGNHPIRRV SVHPDYRQDE 550
SYNFEGDIAL LELENSVTLG PNLLPICLPD NDTFYDLGLM GYVSGFGVME 600
EKIAHDLRFV RLPVANPQAC ENWLRGKNRM DVFSQNMFCA GHPSLKQDAC 650
QGDSGGVFAV RDPNTDRWVA TGIVSWGIGC SRGYGFYTKV LNYVDWIKKE 700
MEEED 705
Length:705
Mass (Da):80,119
Last modified:December 16, 2008 - v2
Checksum:iB45D120201061462
GO

Polymorphismi

Complement component C1r deficiency [MIMi:216950] leads to the failure of the classical complement system activation pathway (C1 deficiency). Individuals with C1 deficiency are highly susceptible to infections by microorganisms and have greater risk in developing autoimmune diseases such as systemic lupus erythematosus (SLE).

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti131 – 1311Y → H.1 Publication
VAR_018667
Natural varianti152 – 1521S → L Common polymorphism. 4 Publications
Corresponds to variant rs1801046 [ dbSNP | Ensembl ].
VAR_016103
Natural varianti163 – 1631H → Y.1 Publication
VAR_018668
Natural varianti184 – 1841E → K Polymorphism confirmed at protein level. 2 Publications
Corresponds to variant rs1126605 [ dbSNP | Ensembl ].
VAR_018669
Natural varianti186 – 1861T → R.4 Publications
Corresponds to variant rs4519167 [ dbSNP | Ensembl ].
VAR_047933
Natural varianti261 – 2611G → R Polymorphism confirmed at protein level. 2 Publications
Corresponds to variant rs3813728 [ dbSNP | Ensembl ].
VAR_018670

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14058 mRNA. Translation: AAA51851.1.
X04701 mRNA. Translation: CAA28407.1.
AB083037 Genomic DNA. Translation: BAC19850.2.
AC094008 Genomic DNA. No translation available.
AC140077 Genomic DNA. No translation available.
CR749540 mRNA. Translation: CAH18343.1.
BC035220 mRNA. Translation: AAH35220.1.
PIRiA24170. C1HURB.
RefSeqiNP_001724.3. NM_001733.4.
UniGeneiHs.524224.

Genome annotation databases

EnsembliENST00000290575; ENSP00000290575; ENSG00000159403.
GeneIDi715.
KEGGihsa:715.

Polymorphism databases

DMDMi218511956.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14058 mRNA. Translation: AAA51851.1 .
X04701 mRNA. Translation: CAA28407.1 .
AB083037 Genomic DNA. Translation: BAC19850.2 .
AC094008 Genomic DNA. No translation available.
AC140077 Genomic DNA. No translation available.
CR749540 mRNA. Translation: CAH18343.1 .
BC035220 mRNA. Translation: AAH35220.1 .
PIRi A24170. C1HURB.
RefSeqi NP_001724.3. NM_001733.4.
UniGenei Hs.524224.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1APQ NMR - A 140-192 [» ]
1GPZ X-ray 2.90 A/B 307-705 [» ]
1MD7 X-ray 3.20 A 375-702 [» ]
1MD8 X-ray 2.80 A 375-703 [» ]
2QY0 X-ray 2.60 A/C 309-463 [» ]
B/D 464-705 [» ]
DisProti DP00621.
ProteinModelPortali P00736.
SMRi P00736. Positions 25-703.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107176. 6 interactions.
IntActi P00736. 3 interactions.
MINTi MINT-8045732.
STRINGi 9606.ENSP00000290575.

Chemistry

BindingDBi P00736.
ChEMBLi CHEMBL4611.
DrugBanki DB00054. Abciximab.
DB00051. Adalimumab.
DB00092. Alefacept.
DB00087. Alemtuzumab.
DB00074. Basiliximab.
DB00112. Bevacizumab.
DB00002. Cetuximab.
DB00111. Daclizumab.
DB00095. Efalizumab.
DB00005. Etanercept.
DB00056. Gemtuzumab ozogamicin.
DB00078. Ibritumomab.
DB00028. Immune globulin.
DB00075. Muromonab.
DB00108. Natalizumab.
DB00110. Palivizumab.
DB00073. Rituximab.
DB00081. Tositumomab.
DB00072. Trastuzumab.
GuidetoPHARMACOLOGYi 2334.

Protein family/group databases

MEROPSi S01.192.

PTM databases

PhosphoSitei P00736.

Polymorphism databases

DMDMi 218511956.

Proteomic databases

PaxDbi P00736.
PeptideAtlasi P00736.
PRIDEi P00736.

Protocols and materials databases

DNASUi 715.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290575 ; ENSP00000290575 ; ENSG00000159403 .
GeneIDi 715.
KEGGi hsa:715.

Organism-specific databases

CTDi 715.
GeneCardsi GC12M007187.
HGNCi HGNC:1246. C1R.
HPAi HPA001551.
MIMi 216950. phenotype.
613785. gene.
neXtProti NX_P00736.
Orphaneti 169147. Immunodeficiency due to an early component of complement deficiency.
PharmGKBi PA25635.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOVERGENi HBG000559.
KOi K01330.
OrthoDBi EOG7W6WK4.
PhylomeDBi P00736.
TreeFami TF330373.

Enzyme and pathway databases

Reactomei REACT_7956. Classical antibody-mediated complement activation.
REACT_8024. Initial triggering of complement.

Miscellaneous databases

ChiTaRSi C1R. human.
EvolutionaryTracei P00736.
GeneWikii C1R_(gene).
GenomeRNAii 715.
NextBioi 2906.
PROi P00736.
SOURCEi Search...

Gene expression databases

Bgeei P00736.
CleanExi HS_C1R.
Genevestigatori P00736.

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.
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. "Nucleotide sequence of the cDNA coding for human complement C1r."
    Leytus S.P., Kurachi K., Sakariassen K.S., Davie E.W.
    Biochemistry 25:4855-4863(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-186.
  2. "Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r."
    Journet A., Tosi M.
    Biochem. J. 240:783-787(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-152 AND ARG-186.
  3. "The human complement component C1R gene: the exon-intron structure and the molecular basis of allelic diversity."
    Nakagawa M., Yuasa I., Irizawa Y., Umetsu K.
    Ann. Hum. Genet. 67:207-215(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-131; LEU-152; TYR-163; LYS-184; ARG-186 AND ARG-261.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon endothelium.
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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], VARIANTS LEU-152 AND ARG-186.
    Tissue: Skin.
  7. "Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme C1r."
    Arlaud G.J., Willis A.C., Gagnon J.
    Biochem. J. 241:711-720(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-463.
  8. "Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r."
    Arlaud G.J., Gagnon J.
    Biochemistry 22:1758-1764(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 464-705.
  9. "Identification of erythro-beta-hydroxyasparagine in the EGF-like domain of human C1r."
    Arlaud G.J., van Dorsselaer A., Bell A., Mancini M., Aude C., Gagnon J.
    FEBS Lett. 222:129-134(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 152-186, HYDROXYLATION AT ASN-167.
  10. "Identification of a cryptic protein kinase CK2 phosphorylation site in human complement protease Clr, and its use to probe intramolecular interaction."
    Pelloux S., Thielens N.M., Hudry-Clergeon G., Petillot Y., Filhol O., Arlaud G.J.
    FEBS Lett. 386:15-20(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 133-137; 187-211 AND 609-613, PHOSPHORYLATION AT SER-206 BY CK2.
  11. "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-125; ASN-221 AND ASN-514.
    Tissue: Plasma.
  12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-514.
    Tissue: Liver.
  13. "Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family."
    Bersch B., Hernandez J.-F., Marion D., Arlaud G.J.
    Biochemistry 37:1204-1214(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 140-192.
  14. "The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex."
    Budayova-Spano M., Lacroix M., Thielens N.M., Arlaud G.J., Fontecilla-Camps J.-C., Gaboriaud C.
    EMBO J. 21:231-239(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 307-702.
  15. "Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism."
    Budayova-Spano M., Grabarse W., Thielens N.M., Hillen H., Lacroix M., Schmidt M., Fontecilla-Camps J.-C., Arlaud G.J., Gaboriaud C.
    Structure 10:1509-1519(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 375-702.
  16. "A common amino acid polymorphism in complement component C1R."
    Nothen M.M., Dewald G.
    Hum. Mol. Genet. 3:217-217(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-152.
  17. "Quantitative detection of single amino acid polymorphisms by targeted proteomics."
    Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.
    J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LYS-184 AND ARG-261, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiC1R_HUMAN
AccessioniPrimary (citable) accession number: P00736
Secondary accession number(s): A6NJQ8, Q68D77, Q8J012
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 16, 2008
Last modified: September 3, 2014
This is version 180 of the entry and version 2 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 12
    Human chromosome 12: 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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