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P04070

- PROC_HUMAN

UniProt

P04070 - PROC_HUMAN

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Protein

Vitamin K-dependent protein C

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

Functioni

Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids.

Catalytic activityi

Degradation of blood coagulation factors Va and VIIIa.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei211 – 2122Cleavage; by thrombin
Active sitei253 – 2531Charge relay system
Active sitei299 – 2991Charge relay system
Active sitei402 – 4021Charge relay system

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. protein binding Source: IntAct
  3. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. leukocyte migration Source: Reactome
  4. negative regulation of apoptotic process Source: UniProtKB
  5. negative regulation of blood coagulation Source: UniProtKB
  6. peptidyl-glutamic acid carboxylation Source: Reactome
  7. post-translational protein modification Source: Reactome
  8. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_1050. Gamma-carboxylation of protein precursors.
REACT_12051. Cell surface interactions at the vascular wall.
REACT_1439. Common Pathway.
REACT_1906. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Protein family/group databases

MEROPSiS01.218.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K-dependent protein C (EC:3.4.21.69)
Alternative name(s):
Anticoagulant protein C
Autoprothrombin IIA
Blood coagulation factor XIV
Cleaved into the following 3 chains:
Gene namesi
Name:PROC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9451. PROC.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. extracellular region Source: UniProtKB
  3. Golgi lumen Source: Reactome
  4. plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Thrombophilia due to protein C deficiency, autosomal dominant (THPH3) [MIM:176860]: A hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. Individuals with decreased amounts of protein C are classically referred to as having type I protein C deficiency and those with normal amounts of a functionally defective protein as having type II deficiency.
Note: The disease is caused by mutations affecting the gene represented in this entry.14 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321R → C in THPH3. 1 Publication
VAR_006635
Natural varianti42 – 421R → S in THPH3; type II; Osaka-10; alters proteolytic processing so that S-42 is the N-terminus of the mature protein. 1 Publication
VAR_055074
Natural varianti57 – 571R → W in THPH3. 2 Publications
VAR_006642
Natural varianti62 – 621E → A in THPH3; Vermont-1. 1 Publication
VAR_006645
Natural varianti76 – 761V → M in THPH3; Vermont-1. 1 Publication
VAR_006646
Natural varianti114 – 1141G → R in THPH3. 1 Publication
VAR_006651
Natural varianti145 – 1451G → R in THPH3. 1 Publication
VAR_006656
Natural varianti210 – 2101P → L in THPH3. 1 Publication
VAR_006664
Natural varianti211 – 2111R → W in THPH3; London-1/Tochigi. 2 Publications
Corresponds to variant rs28933986 [ dbSNP | Ensembl ].
VAR_006665
Natural varianti220 – 2201R → Q in THPH3; Vermont-3. 3 Publications
VAR_006669
Natural varianti220 – 2201R → W in THPH3. 1 Publication
VAR_006668
Natural varianti243 – 2431I → T in THPH3. 1 Publication
VAR_006671
Natural varianti272 – 2721R → C in THPH3. 1 Publication
VAR_006677
Natural varianti321 – 3211P → L in THPH3. 2 Publications
VAR_006687
Natural varianti324 – 3241G → R in THPH3. 1 Publication
VAR_006688
Natural varianti328 – 3281R → C in THPH3. 2 Publications
VAR_006689
Natural varianti340 – 3401T → M in THPH3; Vermont-2. 2 Publications
VAR_006692
Natural varianti369 – 3691P → L in THPH3; Osaka-6. 2 Publications
VAR_006696
Natural varianti392 – 3921G → R in THPH3; Osaka-9. 1 Publication
VAR_006700
Natural varianti401 – 4011D → N in THPH3; La Jolla-2/Osaka-7 and -8. 1 Publication
VAR_006702
Natural varianti423 – 4231G → S in THPH3. 1 Publication
VAR_006704
Natural varianti426 – 4261C → Y in THPH3. 1 Publication
VAR_006705
Natural varianti436 – 4361T → N in THPH3. 1 Publication
VAR_006707
Natural varianti441 – 4411Y → H in THPH3; Osaka-4. 1 Publication
VAR_006708
Natural varianti444 – 4441W → C in THPH3. 1 Publication
VAR_006709
Thrombophilia due to protein C deficiency, autosomal recessive (THPH4) [MIM:612304]: A hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. It results in a thrombotic condition that can manifest as a severe neonatal disorder or as a milder disorder with late-onset thrombophilia. The severe form leads to neonatal death through massive neonatal venous thrombosis. Often associated with ecchymotic skin lesions which can turn necrotic called purpura fulminans, this disorder is very rare.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti144 – 1452NG → K in THPH4; neonatal purpura fulminans.
VAR_006655
Natural varianti178 – 1781A → P in THPH4; Clamart. 1 Publication
VAR_006660
Natural varianti289 – 2891P → L in THPH4. 1 Publication
VAR_006679
Natural varianti328 – 3281R → H in THPH4; Muenchen. 1 Publication
VAR_006690
Natural varianti334 – 3341G → S in THPH4. 1 Publication
VAR_006691
Natural varianti367 – 3671V → A in THPH4; neonatal purpura fulminans. 1 Publication
VAR_006695
Natural varianti418 – 4181G → D in THPH4; Hong Kong-2. 1 Publication
VAR_006703

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

MIMi176860. phenotype.
612304. phenotype.
Orphaneti745. Hereditary thrombophilia due to congenital protein C deficiency.
PharmGKBiPA33799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed predictionAdd
BLAST
Propeptidei19 – 4224PRO_0000028107Add
BLAST
Chaini43 – 461419Vitamin K-dependent protein CPRO_0000028108Add
BLAST
Chaini43 – 197155Vitamin K-dependent protein C light chainPRO_0000028109Add
BLAST
Chaini200 – 461262Vitamin K-dependent protein C heavy chainPRO_0000028110Add
BLAST
Peptidei200 – 21112Activation peptidePRO_0000028111Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi19 – 191O-linked (GalNAc...)1 Publication
Modified residuei48 – 4814-carboxyglutamate1 Publication
Modified residuei49 – 4914-carboxyglutamate1 Publication
Modified residuei56 – 5614-carboxyglutamate1 Publication
Modified residuei58 – 5814-carboxyglutamate1 Publication
Disulfide bondi59 ↔ 64
Modified residuei61 – 6114-carboxyglutamate1 Publication
Modified residuei62 – 6214-carboxyglutamate1 Publication
Modified residuei67 – 6714-carboxyglutamate1 Publication
Modified residuei68 – 6814-carboxyglutamate1 Publication
Modified residuei71 – 7114-carboxyglutamate1 Publication
Disulfide bondi92 ↔ 111
Disulfide bondi101 ↔ 106
Disulfide bondi105 ↔ 120
Modified residuei113 – 1131(3R)-3-hydroxyaspartate
Disulfide bondi122 ↔ 131
Glycosylationi139 – 1391N-linked (GlcNAc...)
Disulfide bondi140 ↔ 151
Disulfide bondi147 ↔ 160
Disulfide bondi162 ↔ 175
Disulfide bondi183 ↔ 319Interchain (between light and heavy chains)
Disulfide bondi238 ↔ 254
Glycosylationi290 – 2901N-linked (GlcNAc...)2 Publications
Glycosylationi355 – 3551N-linked (GlcNAc...)1 Publication
Glycosylationi371 – 3711N-linked (GlcNAc...); partial; atypical2 Publications
Disulfide bondi373 ↔ 387
Disulfide bondi398 ↔ 426

Post-translational modificationi

The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.
N- and O-glycosylated. Partial (70%) N-glycosylation of Asn-371 with an atypical N-X-C site produces a higher molecular weight form referred to as alpha. The lower molecular weight form, not N-glycosylated at Asn-371, is beta. O-glycosylated with core 1 or possibly core 8 glycans.3 Publications
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
May be phosphorylated on a Ser or Thr in a region (AA 25-30) of the propeptide.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Zymogen

Proteomic databases

MaxQBiP04070.
PaxDbiP04070.
PeptideAtlasiP04070.
PRIDEiP04070.

PTM databases

PhosphoSiteiP04070.
UniCarbKBiP04070.

Miscellaneous databases

PMAP-CutDBP04070.

Expressioni

Tissue specificityi

Plasma; synthesized in the liver.

Gene expression databases

ArrayExpressiP04070.
BgeeiP04070.
CleanExiHS_PROC.
GenevestigatoriP04070.

Organism-specific databases

HPAiCAB016721.
CAB016792.
HPA005550.

Interactioni

Subunit structurei

Synthesized as a single chain precursor, which is cleaved into a light chain and a heavy chain held together by a disulfide bond. The enzyme is then activated by thrombin, which cleaves a tetradecapeptide from the amino end of the heavy chain; this reaction, which occurs at the surface of endothelial cells, is strongly promoted by thrombomodulin.

Binary interactionsi

WithEntry#Exp.IntActNotes
MMP15P515112EBI-1383018,EBI-1383043

Protein-protein interaction databases

BioGridi111608. 5 interactions.
IntActiP04070. 3 interactions.
MINTiMINT-8247437.
STRINGi9606.ENSP00000234071.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 503
Helixi55 – 595
Helixi66 – 738
Beta strandi100 – 1034
Turni104 – 1074
Beta strandi108 – 1114
Beta strandi120 – 1223
Beta strandi126 – 1283
Beta strandi137 – 1426
Helixi143 – 1464
Beta strandi148 – 1536
Beta strandi155 – 1617
Beta strandi166 – 1683
Beta strandi175 – 1773
Beta strandi179 – 1813
Beta strandi226 – 2305
Beta strandi236 – 2449
Beta strandi247 – 2504
Helixi252 – 2543
Beta strandi255 – 2573
Beta strandi262 – 2665
Beta strandi269 – 2724
Beta strandi278 – 28710
Turni293 – 2964
Beta strandi301 – 3077
Helixi323 – 3286
Turni329 – 3313
Beta strandi336 – 3416
Beta strandi357 – 3593
Beta strandi361 – 3688
Helixi370 – 3767
Beta strandi385 – 3884
Beta strandi405 – 4106
Beta strandi413 – 42210
Beta strandi424 – 4274
Beta strandi433 – 4364
Helixi438 – 4403
Helixi442 – 4498

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AUTX-ray2.80C212-461[»]
L84-197[»]
1LQVX-ray1.60C/D43-75[»]
1PCUmodel-A175-450[»]
2PCTmodel-A175-450[»]
3F6UX-ray2.80H212-451[»]
L91-188[»]
3JTCX-ray1.60C/D43-75[»]
4DT7X-ray1.90E/F204-223[»]
ProteinModelPortaliP04070.
SMRiP04070. Positions 43-451.

Miscellaneous databases

EvolutionaryTraceiP04070.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 8846GlaAdd
BLAST
Domaini97 – 13236EGF-like 1Add
BLAST
Domaini136 – 17641EGF-like 2Add
BLAST
Domaini212 – 450239Peptidase S1Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
KOiK01344.
PhylomeDBiP04070.
TreeFamiTF327329.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P04070-1) [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

MWQLTSLLLF VATWGISGTP APLDSVFSSS ERAHQVLRIR KRANSFLEEL    50
RHSSLERECI EEICDFEEAK EIFQNVDDTL AFWSKHVDGD QCLVLPLEHP 100
CASLCCGHGT CIDGIGSFSC DCRSGWEGRF CQREVSFLNC SLDNGGCTHY 150
CLEEVGWRRC SCAPGYKLGD DLLQCHPAVK FPCGRPWKRM EKKRSHLKRD 200
TEDQEDQVDP RLIDGKMTRR GDSPWQVVLL DSKKKLACGA VLIHPSWVLT 250
AAHCMDESKK LLVRLGEYDL RRWEKWELDL DIKEVFVHPN YSKSTTDNDI 300
ALLHLAQPAT LSQTIVPICL PDSGLAEREL NQAGQETLVT GWGYHSSREK 350
EAKRNRTFVL NFIKIPVVPH NECSEVMSNM VSENMLCAGI LGDRQDACEG 400
DSGGPMVASF HGTWFLVGLV SWGEGCGLLH NYGVYTKVSR YLDWIHGHIR 450
DKEAPQKSWA P 461
Length:461
Mass (Da):52,071
Last modified:November 1, 1986 - v1
Checksum:i3531B0AE5345B39A
GO
Isoform 2 (identifier: P04070-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAAGRRTCSISTTRPCASASRM
     133-133: R → RGEGERWMLAGGGAGLGPGWGRGTSTSCPRPPLPA

Note: No experimental confirmation available.

Show »
Length:516
Mass (Da):57,556
Checksum:i6F21DD7C17317C88
GO

Sequence cautioni

The sequence S76088 differs from that shown. Reason: Erroneous termination at position 151. Translated as Cys.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141W → G in patients with PROC deficiency. 2 Publications
VAR_006634
Natural varianti32 – 321R → C in THPH3. 1 Publication
VAR_006635
Natural varianti38 – 381R → W in patients with PROC deficiency. 1 Publication
VAR_006636
Natural varianti42 – 421R → C in patients with PROC deficiency. 1 Publication
VAR_006638
Natural varianti42 – 421R → H in Malakoff; low anticoagulant activity. 1 Publication
VAR_006637
Natural varianti42 – 421R → S in THPH3; type II; Osaka-10; alters proteolytic processing so that S-42 is the N-terminus of the mature protein. 1 Publication
VAR_055074
Natural varianti43 – 431A → T.1 Publication
VAR_006639
Natural varianti49 – 491E → D in patients with PROC deficiency. 1 Publication
VAR_006640
Natural varianti51 – 511R → C in patients with PROC deficiency.
VAR_006641
Natural varianti57 – 571R → G in Yonago; defective anticoagulant activity. 1 Publication
VAR_006643
Natural varianti57 – 571R → Q in patients with PROC deficiency.
VAR_006644
Natural varianti57 – 571R → W in THPH3. 2 Publications
VAR_006642
Natural varianti62 – 621E → A in THPH3; Vermont-1. 1 Publication
VAR_006645
Natural varianti76 – 761V → M in THPH3; Vermont-1. 1 Publication
VAR_006646
Natural varianti89 – 891G → C in patients with PROC deficiency. 1 Publication
VAR_006647
Natural varianti108 – 1081H → N in patients with PROC deficiency; La Jolla-1.
VAR_006648
Natural varianti109 – 1091G → R in patients with PROC deficiency.
VAR_006649
Natural varianti114 – 1185Missing in patients with PROC deficiency.
VAR_006650
Natural varianti114 – 1141G → R in THPH3. 1 Publication
VAR_006651
Natural varianti118 – 1181F → L in patients with PROC deficiency.
VAR_006652
Natural varianti119 – 1246Missing in patients with PROC deficiency; St Louis-2.
VAR_006653
Natural varianti120 – 1256Missing in patients with PROC deficiency; St Louis-3.
VAR_006654
Natural varianti144 – 1452NG → K in THPH4; neonatal purpura fulminans.
VAR_006655
Natural varianti145 – 1451G → R in THPH3. 1 Publication
VAR_006656
Natural varianti147 – 1471C → Y in patients with PROC deficiency.
VAR_006657
Natural varianti149 – 1491H → P in patients with PROC deficiency.
VAR_006658
Natural varianti161 – 1611S → R in patients with PROC deficiency.
VAR_006659
Natural varianti178 – 1781A → P in THPH4; Clamart. 1 Publication
VAR_006660
Natural varianti183 – 1831C → R in patients with PROC deficiency.
VAR_006661
Natural varianti189 – 1891R → W in patients with PROC deficiency; La Jolla-3.
Corresponds to variant rs146922325 [ dbSNP | Ensembl ].
VAR_006662
Natural varianti194 – 1941R → C in patients with PROC deficiency.
VAR_006663
Natural varianti210 – 2101P → L in THPH3. 1 Publication
VAR_006664
Natural varianti211 – 2111R → Q in patients with PROC deficiency. 1 Publication
Corresponds to variant rs28933987 [ dbSNP | Ensembl ].
VAR_006666
Natural varianti211 – 2111R → W in THPH3; London-1/Tochigi. 2 Publications
Corresponds to variant rs28933986 [ dbSNP | Ensembl ].
VAR_006665
Natural varianti220 – 2201R → P in patients with PROC deficiency. 1 Publication
VAR_006667
Natural varianti220 – 2201R → Q in THPH3; Vermont-3. 3 Publications
VAR_006669
Natural varianti220 – 2201R → W in THPH3. 1 Publication
VAR_006668
Natural varianti226 – 2261Q → H in patients with PROC deficiency.
VAR_006670
Natural varianti243 – 2431I → T in THPH3. 1 Publication
VAR_006671
Natural varianti244 – 2441H → Y in patients with PROC deficiency. 1 Publication
VAR_006672
Natural varianti253 – 2531H → Q in patients with PROC deficiency. 1 Publication
VAR_006673
Natural varianti265 – 2651L → F in patients with PROC deficiency.
VAR_006674
Natural varianti271 – 2711R → Q in Marseille; low anticoagulant activity. 1 Publication
VAR_006675
Natural varianti271 – 2711R → W in patients with PROC deficiency.
VAR_006676
Natural varianti272 – 2721R → C in THPH3. 1 Publication
VAR_006677
Natural varianti281 – 2811D → DLD in patients with PROC deficiency.
VAR_006678
Natural varianti289 – 2891P → L in THPH4. 1 Publication
VAR_006679
Natural varianti294 – 2941S → N in Paris; low anticoagulant activity. 1 Publication
VAR_006680
Natural varianti298 – 2981N → D in patients with PROC deficiency.
VAR_006681
Natural varianti301 – 3011A → T in patients with PROC deficiency. 1 Publication
VAR_006682
Natural varianti301 – 3011A → V in patients with PROC deficiency.
VAR_006683
Natural varianti309 – 3091A → T in patients with PROC deficiency.
VAR_006684
Natural varianti312 – 3121S → L in patients with PROC deficiency.
VAR_006685
Natural varianti312 – 3121S → P in a patient with PROC deficiency; sporadic case. 1 Publication
VAR_006686
Natural varianti321 – 3211P → L in THPH3. 2 Publications
VAR_006687
Natural varianti324 – 3241G → R in THPH3. 1 Publication
VAR_006688
Natural varianti328 – 3281R → C in THPH3. 2 Publications
VAR_006689
Natural varianti328 – 3281R → H in THPH4; Muenchen. 1 Publication
VAR_006690
Natural varianti334 – 3341G → S in THPH4. 1 Publication
VAR_006691
Natural varianti340 – 3401T → M in THPH3; Vermont-2. 2 Publications
VAR_006692
Natural varianti343 – 3431G → D in patients with PROC deficiency.
VAR_006693
Natural varianti363 – 3631Missing in patients with PROC deficiency.
VAR_006694
Natural varianti367 – 3671V → A in THPH4; neonatal purpura fulminans. 1 Publication
VAR_006695
Natural varianti369 – 3691P → L in THPH3; Osaka-6. 2 Publications
VAR_006696
Natural varianti385 – 3851M → I in patients with PROC deficiency. 1 Publication
VAR_006697
Natural varianti388 – 3881A → T in patients with PROC deficiency. 1 Publication
VAR_006698
Natural varianti388 – 3881A → V in patients with PROC deficiency. 1 Publication
VAR_006699
Natural varianti392 – 3921G → R in THPH3; Osaka-9. 1 Publication
VAR_006700
Natural varianti394 – 3941R → W in patients with PROC deficiency.
VAR_006701
Natural varianti401 – 4011D → N in THPH3; La Jolla-2/Osaka-7 and -8. 1 Publication
VAR_006702
Natural varianti418 – 4181G → D in THPH4; Hong Kong-2. 1 Publication
VAR_006703
Natural varianti423 – 4231G → S in THPH3. 1 Publication
VAR_006704
Natural varianti426 – 4261C → Y in THPH3. 1 Publication
VAR_006705
Natural varianti433 – 4331G → S in patients with PROC deficiency; Purmerend.
VAR_006706
Natural varianti436 – 4361T → N in THPH3. 1 Publication
VAR_006707
Natural varianti441 – 4411Y → H in THPH3; Osaka-4. 1 Publication
VAR_006708
Natural varianti444 – 4441W → C in THPH3. 1 Publication
VAR_006709
Natural varianti445 – 4451I → M in patients with PROC deficiency.
VAR_006710

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAAGRRTCSISTTRPCASAS RM in isoform 2. VSP_054393
Alternative sequencei133 – 1331R → RGEGERWMLAGGGAGLGPGW GRGTSTSCPRPPLPA in isoform 2. VSP_054394

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061C → Q in AAA60164. 1 Publication
Sequence conflicti445 – 4451I → IL in AAA60165. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02750 mRNA. Translation: CAA26528.1.
M11228 Genomic DNA. Translation: AAA60166.1.
M12712
, M12683, M12684, M12685, M12686, M12687 Genomic DNA. Translation: AAA60165.1.
AF378903 Genomic DNA. Translation: AAK56377.1.
AK298454 mRNA. Translation: BAG60669.1.
AC068282 Genomic DNA. Translation: AAY15044.1.
CH471103 Genomic DNA. Translation: EAW95320.1.
BC034377 mRNA. Translation: AAH34377.1.
S58668 Genomic DNA. Translation: AAB26335.1.
K02059 mRNA. Translation: AAA60164.1.
S76088 Genomic DNA. No translation available.
S76090 Genomic DNA. No translation available.
CCDSiCCDS2145.1. [P04070-1]
PIRiA22331. KXHU.
RefSeqiNP_000303.1. NM_000312.3. [P04070-1]
XP_005263773.1. XM_005263716.2. [P04070-2]
UniGeneiHs.224698.

Genome annotation databases

EnsembliENST00000234071; ENSP00000234071; ENSG00000115718.
ENST00000422777; ENSP00000409543; ENSG00000115718.
ENST00000453608; ENSP00000404030; ENSG00000115718.
GeneIDi5624.
KEGGihsa:5624.
UCSCiuc002tok.3. human. [P04070-1]

Polymorphism databases

DMDMi131067.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Protein C entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02750 mRNA. Translation: CAA26528.1 .
M11228 Genomic DNA. Translation: AAA60166.1 .
M12712
, M12683 , M12684 , M12685 , M12686 , M12687 Genomic DNA. Translation: AAA60165.1 .
AF378903 Genomic DNA. Translation: AAK56377.1 .
AK298454 mRNA. Translation: BAG60669.1 .
AC068282 Genomic DNA. Translation: AAY15044.1 .
CH471103 Genomic DNA. Translation: EAW95320.1 .
BC034377 mRNA. Translation: AAH34377.1 .
S58668 Genomic DNA. Translation: AAB26335.1 .
K02059 mRNA. Translation: AAA60164.1 .
S76088 Genomic DNA. No translation available.
S76090 Genomic DNA. No translation available.
CCDSi CCDS2145.1. [P04070-1 ]
PIRi A22331. KXHU.
RefSeqi NP_000303.1. NM_000312.3. [P04070-1 ]
XP_005263773.1. XM_005263716.2. [P04070-2 ]
UniGenei Hs.224698.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AUT X-ray 2.80 C 212-461 [» ]
L 84-197 [» ]
1LQV X-ray 1.60 C/D 43-75 [» ]
1PCU model - A 175-450 [» ]
2PCT model - A 175-450 [» ]
3F6U X-ray 2.80 H 212-451 [» ]
L 91-188 [» ]
3JTC X-ray 1.60 C/D 43-75 [» ]
4DT7 X-ray 1.90 E/F 204-223 [» ]
ProteinModelPortali P04070.
SMRi P04070. Positions 43-451.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111608. 5 interactions.
IntActi P04070. 3 interactions.
MINTi MINT-8247437.
STRINGi 9606.ENSP00000234071.

Chemistry

BindingDBi P04070.
ChEMBLi CHEMBL4444.
DrugBanki DB00025. Antihemophilic Factor.
DB00055. Drotrecogin alfa.
DB00170. Menadione.
DB00464. Sodium Tetradecyl Sulfate.

Protein family/group databases

MEROPSi S01.218.

PTM databases

PhosphoSitei P04070.
UniCarbKBi P04070.

Polymorphism databases

DMDMi 131067.

Proteomic databases

MaxQBi P04070.
PaxDbi P04070.
PeptideAtlasi P04070.
PRIDEi P04070.

Protocols and materials databases

DNASUi 5624.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000234071 ; ENSP00000234071 ; ENSG00000115718 .
ENST00000422777 ; ENSP00000409543 ; ENSG00000115718 .
ENST00000453608 ; ENSP00000404030 ; ENSG00000115718 .
GeneIDi 5624.
KEGGi hsa:5624.
UCSCi uc002tok.3. human. [P04070-1 ]

Organism-specific databases

CTDi 5624.
GeneCardsi GC02P128176.
HGNCi HGNC:9451. PROC.
HPAi CAB016721.
CAB016792.
HPA005550.
MIMi 176860. phenotype.
612283. gene.
612304. phenotype.
neXtProti NX_P04070.
Orphaneti 745. Hereditary thrombophilia due to congenital protein C deficiency.
PharmGKBi PA33799.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251821.
HOVERGENi HBG013304.
KOi K01344.
PhylomeDBi P04070.
TreeFami TF327329.

Enzyme and pathway databases

Reactomei REACT_1050. Gamma-carboxylation of protein precursors.
REACT_12051. Cell surface interactions at the vascular wall.
REACT_1439. Common Pathway.
REACT_1906. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Miscellaneous databases

EvolutionaryTracei P04070.
GeneWikii Protein_C.
GenomeRNAii 5624.
NextBioi 21860.
PMAP-CutDB P04070.
PROi P04070.
SOURCEi Search...

Gene expression databases

ArrayExpressi P04070.
Bgeei P04070.
CleanExi HS_PROC.
Genevestigatori P04070.

Family and domain databases

Gene3Di 4.10.740.10. 1 hit.
InterProi IPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001143. Factor_X. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTi SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEi PS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
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. "The structure and evolution of a 461 amino acid human protein C precursor and its messenger RNA, based upon the DNA sequence of cloned human liver cDNAs."
    Beckmann R.J., Schmidt R.J., Santerre R.F., Plutzky J., Crabtree G.R., Long G.L.
    Nucleic Acids Res. 13:5233-5247(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The nucleotide sequence of the gene for human protein C."
    Foster D.C., Yoshitake S., Davie E.W.
    Proc. Natl. Acad. Sci. U.S.A. 82:4673-4677(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], HYDROXYLATION AT ASP-113, GLYCOSYLATION AT ASN-290; ASN-355 AND ASN-371, GAMMA-CARBOXYGLUTAMATION AT GLU-48; GLU-49; GLU-56; GLU-58; GLU-61; GLU-62; GLU-67; GLU-68 AND GLU-71.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. SeattleSNPs variation discovery resource
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Tissue: Liver.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Colon.
  9. "Protein C Osaka 10 with aberrant propeptide processing: loss of anticoagulant activity due to an amino acid substitution in the protein C precursor."
    Miyata T., Zheng Y.-Z., Sakata T., Kato H.
    Thromb. Haemost. 74:1003-1008(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 42-57, VARIANT THPH3 SER-42.
    Tissue: Blood.
  10. "An abnormal protein C (protein C Yonago) with an amino acid substitution of Gly for Arg-15 caused by a single base mutation of C to G in codon 57 (CGG-->GGG). Deteriorated calcium-dependent conformation of the gamma-carboxyglutamic acid domain relevant to a thrombotic tendency."
    Mimuro J., Muramatsu S., Kaneko M., Yoshitake S., Iijima K., Nakamura K., Sakata Y., Matsuda M.
    Int. J. Hematol. 57:9-14(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-64, VARIANT PROC DEFICIENCY GLY-57.
  11. "Characterization of a cDNA coding for human protein C."
    Foster D.C., Davie E.W.
    Proc. Natl. Acad. Sci. U.S.A. 81:4766-4770(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-461 (ISOFORM 1).
  12. "Homozygous type I protein C deficiency in two unrelated families exhibiting thrombophilia related to Ala136-->Pro or Arg286-->His mutations."
    Long G.L., Tomczak J.A., Rainville I.R., Dreyfus M., Schramm W., Schwarz H.P.
    Thromb. Haemost. 72:526-533(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-178 AND 267-332, VARIANTS THPH4 PRO-178 AND HIS-328.
  13. "Beta protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites."
    Miletich J.P., Broze G.J. Jr.
    J. Biol. Chem. 265:11397-11404(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-371.
  14. "O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C."
    Harris R.J., Ling V.T., Spellman M.W.
    J. Biol. Chem. 267:5102-5107(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: HYDROXYLATION.
  15. "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-290.
    Tissue: Plasma.
  16. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
    Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-19, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen."
    Fisher C.L., Greengard J.S., Griffin J.H.
    Protein Sci. 3:588-599(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 175-450.
  18. "The 2.8 A crystal structure of Gla-domainless activated protein C."
    Mather T., Oganessyan V., Hof P., Huber R., Foundling S., Esmon C., Bode W.
    EMBO J. 15:6822-6831(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 84-461.
  19. "Protein C deficiency: a database of mutations."
    Reitsma P.H., Poort S.R., Bernardi F., Gandrille S., Long G.L., Sala N., Cooper D.N.
    Thromb. Haemost. 69:77-84(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON PROC VARIANTS.
  20. "Hereditary thrombophilia: identification of nonsense and missense mutations in the protein C gene."
    Romeo G., Hassan H.J., Staempfli S., Roncuzzi L., Cianetti L., Leonardi A., Vicente V., Mannucci P.M., Bertina R.M., Peschle C., Cortese R.
    Proc. Natl. Acad. Sci. U.S.A. 84:2829-2832(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH3 CYS-444.
  21. "Protein C London 1: recurrent mutation at Arg-169 (CGG-->TGG) in the protein C gene causing thrombosis."
    Grundy C.B., Chitolie A., Talbot S., Bevan D., Kakkar V.V., Cooper D.N.
    Nucleic Acids Res. 17:10513-10513(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH3 TRP-211.
  22. "The spectrum of genetic defects in a panel of 40 Dutch families with symptomatic protein C deficiency type I: heterogeneity and founder effects."
    Reitsma P.H., Poort S.R., Allaart C.F., Briet E., Bertina R.M.
    Blood 78:890-894(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH3 CYS-272.
  23. "Protein CVermont: symptomatic type II protein C deficiency associated with two GLA domain mutations."
    Bovill E.G., Tomczak J.A., Grant B., Bhushan F., Pillemer E., Rainville I.R., Long G.L.
    Blood 79:1456-1465(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THPH3 ALA-62 AND MET-76.
  24. "Protein C deficiency Hong Kong 1 and 2: hereditary protein C deficiency caused by two mutant alleles, a 5-nucleotide deletion and a missense mutation."
    Sugahara Y., Miura O., Yuen P., Aoki N.
    Blood 80:126-133(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH4 ASP-418.
  25. "A novel homozygous missense mutation in the protein C (PROC) gene causing recurrent venous thrombosis."
    Grundy C.B., Chisholm M., Kakkar V.V., Cooper D.N.
    Hum. Genet. 89:683-684(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH4 LEU-289.
  26. "Two different missense mutations at Arg 178 of the protein C (PROC) gene causing recurrent venous thrombosis."
    Grundy C.B., Schulman S., Tengborn L., Kakkar V.V., Cooper D.N.
    Hum. Genet. 89:685-686(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THPH3 GLN-220 AND TRP-220.
  27. "Two novel mutations responsible for hereditary type I protein C deficiency: characterization by denaturing gradient gel electrophoresis."
    Gandrille S., Vidaud M., Aiach M., Alhenc-Gelas M., Fischer A.M., Gouault-Heilman M., Toulon P., Fiessinger J.-N., Goossens M.
    Hum. Mutat. 1:491-500(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH3 GLN-220.
  28. "Homozygous protein C deficiency: identification of a novel missense mutation that causes impaired secretion of the mutant protein C."
    Yamamoto K., Matsushita T., Sugiura I., Takamatsu J., Iwasaki E., Wada H., Deguchi K., Shirakawa S., Saito H.
    J. Lab. Clin. Med. 119:682-689(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH4 SER-334.
  29. "Five novel mutations located in exons III and IX of the protein C gene in patients presenting with defective protein C anticoagulant activity."
    Gandrille S., Alhenc-Gelas M., Gaussem P., Aillaud M.-F., Dupuy E., Juhan-Vague I., Aiach M.
    Blood 82:159-168(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TRP-38; CYS-42; HIS-42; GLN-271 AND ASN-294.
  30. "Twelve novel and two recurrent mutations in 14 Austrian families with hereditary protein C deficiency."
    Poort S.R., Pabinger-Fasching I., Mannhalter C., Reitsma P.H., Bertina R.M.
    Blood Coagul. Fibrinolysis 4:273-280(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLY-14; GLN-211; TYR-244; GLN-253; LEU-321; CYS-328; ILE-385; THR-388 AND VAL-388.
  31. "A Gla domain mutation (Arg 15-->Trp) in the protein C (PROC) gene causing type 2 protein C deficiency and recurrent venous thrombosis."
    Millar D.S., Grundy C.B., Bignell P., Moffat E.H., Martin R., Kakkar V.V., Cooper D.N.
    Blood Coagul. Fibrinolysis 4:345-347(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH3 TRP-57.
  32. "Genetic mutations in ten unrelated American patients with symptomatic type 1 protein C deficiency."
    Tsay W., Greengard J.S., Montgomery R.R., McPherson R.A., Fucci J.C., Koerper M.A., Coughlin J., Griffin J.H.
    Blood Coagul. Fibrinolysis 4:791-796(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THPH3 ARG-145; LEU-210; TRP-211; THR-243; LEU-321; MET-340 AND TYR-426.
  33. "Symptomatic type II protein C deficiency caused by a missense mutation (Gly 381-->Ser) in the substrate-binding pocket."
    Marchetti G., Patracchini P., Gemmati D., Castaman G., Rodeghiero F., Wacey A., Cooper D.N., Tuddenham E.G., Bernardi F.
    Br. J. Haematol. 84:285-289(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH3 SER-423.
  34. "First de novo mutations in the protein C gene of two patients with type I deficiency: a missense mutation and a splice site deletion."
    Gandrille S., Jude B., Alhenc-Gelas M., Emmerich J., Aiach M.
    Blood 84:2566-2570(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRO-312.
  35. "A homozygous deletion/insertion mutation in the protein C (PROC) gene causing neonatal Purpura fulminans: prenatal diagnosis in an at-risk pregnancy."
    Millar D.S., Allgrove J., Rodeck C., Kakkar V.V., Cooper D.N.
    Blood Coagul. Fibrinolysis 5:647-649(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH4 144-ASN-GLY-145 DELINS LYS.
  36. "A novel homozygous missense mutation (Val 325-->Ala) in the protein C gene causing neonatal purpura fulminans."
    Witt I., Beck S., Seydewitz H.H., Tasangil C., Schenck W.
    Blood Coagul. Fibrinolysis 5:651-653(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THPH4 ALA-367.
  37. "Six missense mutations associated with type I and type II protein C deficiency and implications obtained from molecular modelling."
    Zheng Y.-Z., Sakata T., Matsusue T., Umeyama H., Kato H., Miyata T.
    Blood Coagul. Fibrinolysis 5:687-696(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THPH3 LEU-369; ARG-392; ASN-401 AND HIS-441.
  38. "Influence of six mutations of the protein C gene on the Gla domain conformation and calcium affinity."
    Gaussem P., Gandrille S., Duchemin J., Emmerich J., Alhenc-Gelas M., Aillaud M.-F., Aiach M.
    Thromb. Haemost. 71:748-754(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASP-49.
  39. "Three novel mutations in the protein C (PROC) gene causing venous thrombosis."
    Millar D.S., Bevan D., Chitolie A., Reynaud J., Chisholm M., Kakkar V.V., Cooper D.N.
    Blood Coagul. Fibrinolysis 6:138-140(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CYS-89; PRO-220 AND THR-301.
  40. "Six different point mutations in seven Danish families with symptomatic protein C deficiency."
    Lind B., Schwartz M., Thorsen S.
    Thromb. Haemost. 73:186-193(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THPH3 TRP-57; ARG-114; ARG-324; CYS-328 AND LEU-369, VARIANT THR-43.
  41. "Two novel (R(-11)C; T394D) and two repeat missense mutations in the protein C gene associated with venous thrombosis in six kindreds."
    Ireland H.A., Boisclair M.D., Taylor J., Thompson E., Thein S.L., Girolami A., de Caterina M., Scopacasa F., de Stefano V., Leone G., Finazzi G., Cohen H., Lane D.A.
    Hum. Mutat. 7:176-179(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THPH3 CYS-32 AND ASN-436.
  42. "Type I protein C deficiency in French Canadians: evidence of a founder effect and association of specific protein C gene mutations with plasma protein C levels."
    Couture P., Demers C., Morissette J., Delage R., Jomphe M., Couture L., Simard J.
    Thromb. Haemost. 80:551-556(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THPH3 GLN-220 AND MET-340.

Entry informationi

Entry nameiPROC_HUMAN
AccessioniPrimary (citable) accession number: P04070
Secondary accession number(s): B4DPQ7
, Q15189, Q15190, Q16001, Q53S74, Q9UC55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: September 3, 2014
This is version 197 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Calcium also binds, with stronger affinity to another site, beyond the GLA domain. This GLA-independent binding site is necessary for the recognition of the thrombin-thrombomodulin complex.

Keywords - Technical termi

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

Documents

  1. Human chromosome 2
    Human chromosome 2: 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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