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P38435

- VKGC_HUMAN

UniProt

P38435 - VKGC_HUMAN

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Protein

Vitamin K-dependent gamma-carboxylase

Gene

GGCX

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

Functioni

Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide.1 Publication

Catalytic activityi

[Peptidyl]-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O = [peptidyl]-glutamate + CO2 + O2 + phylloquinone.

pH dependencei

Optimum pH is 7.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei218 – 2181Proton acceptor1 Publication

GO - Molecular functioni

  1. gamma-glutamyl carboxylase activity Source: ProtInc

GO - Biological processi

  1. blood coagulation Source: ProtInc
  2. cellular protein metabolic process Source: Reactome
  3. cellular protein modification process Source: ProtInc
  4. peptidyl-glutamic acid carboxylation Source: Reactome
  5. post-translational protein modification Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciMetaCyc:HS03897-MONOMER.
ReactomeiREACT_1050. Gamma-carboxylation of protein precursors.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K-dependent gamma-carboxylase (EC:4.1.1.90)
Alternative name(s):
Gamma-glutamyl carboxylase
Peptidyl-glutamate 4-carboxylase
Vitamin K gamma glutamyl carboxylase
Gene namesi
Name:GGCX
Synonyms:GC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4247. GGCX.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 6059CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei61 – 8121HelicalSequence AnalysisAdd
BLAST
Topological domaini82 – 11332LumenalSequence AnalysisAdd
BLAST
Transmembranei114 – 13421HelicalSequence AnalysisAdd
BLAST
Topological domaini135 – 1362CytoplasmicSequence Analysis
Transmembranei137 – 15721HelicalSequence AnalysisAdd
BLAST
Topological domaini158 – 292135LumenalSequence AnalysisAdd
BLAST
Transmembranei293 – 31321HelicalSequence AnalysisAdd
BLAST
Topological domaini314 – 36148CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei362 – 38221HelicalSequence AnalysisAdd
BLAST
Topological domaini383 – 758376LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: ProtInc
  3. membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Combined deficiency of vitamin K-dependent clotting factors 1 (VKCFD1) [MIM:277450]: VKCFD leads to a bleeding tendency that is usually reversed by oral administration of vitamin K.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti394 – 3941L → R in VKCFD1; affects glutamate binding. 1 Publication
VAR_005781
Natural varianti485 – 4851R → P in VKCFD1. 1 Publication
VAR_021826
Natural varianti501 – 5011W → S in VKCFD1. 1 Publication
Corresponds to variant rs28928872 [ dbSNP | Ensembl ].
VAR_015218
Pseudoxanthoma elasticum-like disorder with multiple coagulation factor deficiency (PXEL-MCFD) [MIM:610842]: Characterized by hyperlaxity of the skin involving the entire body. Important phenotypic differences with classical PXE include much more severe skin laxity with spreading toward the trunk and limbs with thick, leathery skin folds rather than confinement to flexural areas, and no decrease in visual acuity. Moreover, detailed electron microscopic analyzes revealed that alterations of elastic fibers as well as their mineralization are slightly different from those in classic PXE.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti299 – 2991F → S in PXEL-MCFD. 1 Publication
VAR_032979
Natural varianti476 – 4761R → C in PXEL-MCFD. 1 Publication
VAR_032980
Natural varianti476 – 4761R → H in PXEL-MCFD. 1 Publication
VAR_032981
Natural varianti493 – 4931W → S in PXEL-MCFD. 1 Publication
VAR_032982
Natural varianti558 – 5581G → R in PXEL-MCFD. 1 Publication
VAR_032983

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi160 – 1601H → A: No effect on activity. 1 Publication
Mutagenesisi218 – 2181K → A: No activity. 1 Publication
Mutagenesisi287 – 2871H → A: No effect on activity. 1 Publication
Mutagenesisi381 – 3811H → A: No effect on activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi277450. phenotype.
610842. phenotype.
Orphaneti91135. Body skin hyperlaxity due to vitamin K-dependent coagulation factor deficiency.
98434. Hereditary combined deficiency of vitamin K-dependent clotting factors.
PharmGKBiPA28660.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 758757Vitamin K-dependent gamma-carboxylasePRO_0000191823Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Disulfide bondi99 ↔ 4501 Publication
Glycosylationi459 – 4591N-linked (GlcNAc...)1 Publication
Glycosylationi550 – 5501N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP38435.
PaxDbiP38435.
PRIDEiP38435.

PTM databases

PhosphoSiteiP38435.

Expressioni

Gene expression databases

BgeeiP38435.
CleanExiHS_GC.
HS_GGCX.
ExpressionAtlasiP38435. baseline and differential.
GenevestigatoriP38435.

Organism-specific databases

HPAiHPA018284.

Interactioni

Subunit structurei

Monomer. May interact with CALU (By similarity).By similarity

Protein-protein interaction databases

BioGridi108945. 3 interactions.
STRINGi9606.ENSP00000233838.

Structurei

3D structure databases

ProteinModelPortaliP38435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG83578.
GeneTreeiENSGT00390000014909.
HOGENOMiHOG000007593.
HOVERGENiHBG012798.
InParanoidiP38435.
KOiK10106.
OMAiSPSCYMY.
OrthoDBiEOG7B5WV9.
PhylomeDBiP38435.
TreeFamiTF323879.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR011020. HTTM.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
IPR007782. VKG_COase.
[Graphical view]
PANTHERiPTHR12639. PTHR12639. 1 hit.
PfamiPF05090. VKG_Carbox. 1 hit.
[Graphical view]
SMARTiSM00752. HTTM. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

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: P38435-1) [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
MAVSAGSART SPSSDKVQKD KAELISGPRQ DSRIGKLLGF EWTDLSSWRR
60 70 80 90 100
LVTLLNRPTD PASLAVFRFL FGFLMVLDIP QERGLSSLDR KYLDGLDVCR
110 120 130 140 150
FPLLDALRPL PLDWMYLVYT IMFLGALGMM LGLCYRISCV LFLLPYWYVF
160 170 180 190 200
LLDKTSWNNH SYLYGLLAFQ LTFMDANHYW SVDGLLNAHR RNAHVPLWNY
210 220 230 240 250
AVLRGQIFIV YFIAGVKKLD ADWVEGYSME YLSRHWLFSP FKLLLSEELT
260 270 280 290 300
SLLVVHWGGL LLDLSAGFLL FFDVSRSIGL FFVSYFHCMN SQLFSIGMFS
310 320 330 340 350
YVMLASSPLF CSPEWPRKLV SYCPRRLQQL LPLKAAPQPS VSCVYKRSRG
360 370 380 390 400
KSGQKPGLRH QLGAAFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD
410 420 430 440 450
MMVHSRSHQH VKITYRDGRT GELGYLNPGV FTQSRRWKDH ADMLKQYATC
460 470 480 490 500
LSRLLPKYNV TEPQIYFDIW VSINDRFQQR IFDPRVDIVQ AAWSPFQRTS
510 520 530 540 550
WVQPLLMDLS PWRAKLQEIK SSLDNHTEVV FIADFPGLHL ENFVSEDLGN
560 570 580 590 600
TSIQLLQGEV TVELVAEQKN QTLREGEKMQ LPAGEYHKVY TTSPSPSCYM
610 620 630 640 650
YVYVNTTELA LEQDLAYLQE LKEKVENGSE TGPLPPELQP LLEGEVKGGP
660 670 680 690 700
EPTPLVQTFL RRQQRLQEIE RRRNTPFHER FFRFLLRKLY VFRRSFLMTC
710 720 730 740 750
ISLRNLILGR PSLEQLAQEV TYANLRPFEA VGELNPSNTD SSHSNPPESN

PDPVHSEF
Length:758
Mass (Da):87,561
Last modified:December 20, 2005 - v2
Checksum:i720D5B08E9B558C8
GO
Isoform 2 (identifier: P38435-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     15-71: Missing.

Note: No experimental confirmation available.

Show »
Length:701
Mass (Da):80,989
Checksum:iCA7D806186E791B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti400 – 4001D → N in AAA91834. 1 PublicationCurated
Sequence conflicti659 – 6591F → S in BAG59837. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti299 – 2991F → S in PXEL-MCFD. 1 Publication
VAR_032979
Natural varianti325 – 3251R → Q.1 Publication
Corresponds to variant rs699664 [ dbSNP | Ensembl ].
VAR_005780
Natural varianti394 – 3941L → R in VKCFD1; affects glutamate binding. 1 Publication
VAR_005781
Natural varianti476 – 4761R → C in PXEL-MCFD. 1 Publication
VAR_032980
Natural varianti476 – 4761R → H in PXEL-MCFD. 1 Publication
VAR_032981
Natural varianti485 – 4851R → P in VKCFD1. 1 Publication
VAR_021826
Natural varianti493 – 4931W → S in PXEL-MCFD. 1 Publication
VAR_032982
Natural varianti501 – 5011W → S in VKCFD1. 1 Publication
Corresponds to variant rs28928872 [ dbSNP | Ensembl ].
VAR_015218
Natural varianti558 – 5581G → R in PXEL-MCFD. 1 Publication
VAR_032983

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei15 – 7157Missing in isoform 2. 1 PublicationVSP_046179Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81592 mRNA. Translation: AAA58643.1.
U65896 Genomic DNA. Translation: AAB39832.1.
L17128 mRNA. Translation: AAA91834.1.
AK297397 mRNA. Translation: BAG59837.1.
AC016753 Genomic DNA. Translation: AAY24340.1.
BC013979 mRNA. Translation: AAH13979.1.
CCDSiCCDS1978.1. [P38435-1]
CCDS46353.1. [P38435-2]
PIRiA39283.
RefSeqiNP_000812.2. NM_000821.5. [P38435-1]
NP_001135741.1. NM_001142269.2. [P38435-2]
UniGeneiHs.77719.

Genome annotation databases

EnsembliENST00000233838; ENSP00000233838; ENSG00000115486. [P38435-1]
ENST00000430215; ENSP00000408045; ENSG00000115486. [P38435-2]
GeneIDi2677.
KEGGihsa:2677.
UCSCiuc002sps.3. human. [P38435-1]

Polymorphism databases

DMDMi84028279.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81592 mRNA. Translation: AAA58643.1 .
U65896 Genomic DNA. Translation: AAB39832.1 .
L17128 mRNA. Translation: AAA91834.1 .
AK297397 mRNA. Translation: BAG59837.1 .
AC016753 Genomic DNA. Translation: AAY24340.1 .
BC013979 mRNA. Translation: AAH13979.1 .
CCDSi CCDS1978.1. [P38435-1 ]
CCDS46353.1. [P38435-2 ]
PIRi A39283.
RefSeqi NP_000812.2. NM_000821.5. [P38435-1 ]
NP_001135741.1. NM_001142269.2. [P38435-2 ]
UniGenei Hs.77719.

3D structure databases

ProteinModelPortali P38435.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108945. 3 interactions.
STRINGi 9606.ENSP00000233838.

Chemistry

ChEMBLi CHEMBL2012.
DrugBanki DB01125. Anisindione.
DB00100. Coagulation Factor IX.
DB00036. Coagulation factor VIIa.
DB00055. Drotrecogin alfa.
DB00170. Menadione.
DB01022. Phylloquinone.
GuidetoPHARMACOLOGYi 1268.

PTM databases

PhosphoSitei P38435.

Polymorphism databases

DMDMi 84028279.

Proteomic databases

MaxQBi P38435.
PaxDbi P38435.
PRIDEi P38435.

Protocols and materials databases

DNASUi 2677.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000233838 ; ENSP00000233838 ; ENSG00000115486 . [P38435-1 ]
ENST00000430215 ; ENSP00000408045 ; ENSG00000115486 . [P38435-2 ]
GeneIDi 2677.
KEGGi hsa:2677.
UCSCi uc002sps.3. human. [P38435-1 ]

Organism-specific databases

CTDi 2677.
GeneCardsi GC02M085771.
HGNCi HGNC:4247. GGCX.
HPAi HPA018284.
MIMi 137167. gene.
277450. phenotype.
610842. phenotype.
neXtProti NX_P38435.
Orphaneti 91135. Body skin hyperlaxity due to vitamin K-dependent coagulation factor deficiency.
98434. Hereditary combined deficiency of vitamin K-dependent clotting factors.
PharmGKBi PA28660.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG83578.
GeneTreei ENSGT00390000014909.
HOGENOMi HOG000007593.
HOVERGENi HBG012798.
InParanoidi P38435.
KOi K10106.
OMAi SPSCYMY.
OrthoDBi EOG7B5WV9.
PhylomeDBi P38435.
TreeFami TF323879.

Enzyme and pathway databases

BioCyci MetaCyc:HS03897-MONOMER.
Reactomei REACT_1050. Gamma-carboxylation of protein precursors.

Miscellaneous databases

ChiTaRSi GGCX. human.
GeneWikii Gamma-glutamyl_carboxylase.
GenomeRNAii 2677.
NextBioi 10570.
PROi P38435.
SOURCEi Search...

Gene expression databases

Bgeei P38435.
CleanExi HS_GC.
HS_GGCX.
ExpressionAtlasi P38435. baseline and differential.
Genevestigatori P38435.

Family and domain databases

Gene3Di 2.60.120.10. 1 hit.
InterProi IPR011020. HTTM.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
IPR007782. VKG_COase.
[Graphical view ]
PANTHERi PTHR12639. PTHR12639. 1 hit.
Pfami PF05090. VKG_Carbox. 1 hit.
[Graphical view ]
SMARTi SM00752. HTTM. 1 hit.
[Graphical view ]
SUPFAMi SSF51182. SSF51182. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the cDNA for human gamma-glutamyl carboxylase."
    Wu S.-M., Cheung W.-F., Frazier D., Stafford D.W.
    Science 254:1634-1636(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-325.
  2. "Genomic sequence and transcription start site for the human gamma-glutamyl carboxylase."
    Wu S.-M., Stafford D.W., Frazier L.D., Fu Y.Y., High K.A., Chu K., Sanchez-Vega B., Solera J.
    Blood 89:4058-4062(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Ying L., Lipsky J.J.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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: Brain.
  5. "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].
  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] (ISOFORM 1).
    Tissue: Brain.
  7. "A topological study of the human gamma-glutamyl carboxylase."
    Tie J., Wu S.-M., Jin D., Nicchitta C.V., Stafford D.W.
    Blood 96:973-978(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
  8. "A novel fluorescence assay to study propeptide interaction with gamma-glutamyl carboxylase."
    Presnell S.R., Tripathy A., Lentz B.R., Jin D.Y., Stafford D.W.
    Biochemistry 40:11723-11733(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROPEPTIDE INTERACTION, MONOMER.
  9. "Determination of disulfide bond assignment of human vitamin K-dependent gamma-glutamyl carboxylase by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry."
    Tie J.K., Mutucumarana V.P., Straight D.L., Carrick K.L., Pope R.M., Stafford D.W.
    J. Biol. Chem. 278:45468-45475(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND.
  10. "The vitamin K-dependent carboxylase."
    Berkner K.L.
    Annu. Rev. Nutr. 25:127-149(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  11. "Bronsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation."
    Rishavy M.A., Hallgren K.W., Yakubenko A.V., Shtofman R.L., Runge K.W., Berkner K.L.
    Biochemistry 45:13239-13248(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-160; LYS-218; HIS-287 AND HIS-381, ACTIVE SITE, FUNCTION, PH DEPENDENCE, REACTION MECHANISM.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "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-459 AND ASN-550.
    Tissue: Liver.
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "A missense mutation in gamma-glutamyl carboxylase gene causes combined deficiency of all vitamin K-dependent blood coagulation factors."
    Brenner B., Sanchez-Vega B., Wu S.M., Lanir N., Stafford D.W., Solera J.
    Blood 92:4554-4559(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VKCFD1 ARG-394.
  16. "Novel mutation in the gamma-glutamyl carboxylase gene resulting in congenital combined deficiency of all vitamin K-dependent blood coagulation factors."
    Spronk H.M.H., Farah R.A., Buchanan G.R., Vermeer C., Soute B.A.M.
    Blood 96:3650-3652(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VKCFD1 SER-501.
  17. "Expression and characterization of the naturally occurring mutation L394R in human gamma-glutamyl carboxylase."
    Mutucumarana V.P., Stafford D.W., Stanley T.B., Jin D.-Y., Solera J., Brenner B., Azerad R., Wu S.-M.
    J. Biol. Chem. 275:32572-32577(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT VKCFD1 ARG-394.
  18. "Compound heterozygous mutations in the gamma-glutamyl carboxylase gene cause combined deficiency of all vitamin K-dependent blood coagulation factors."
    Rost S., Fregin A., Koch D., Compes M., Mueller C.R., Oldenburg J.
    Br. J. Haematol. 126:546-549(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VKCFD1 PRO-485.
  19. "Pseudoxanthoma elasticum-like phenotype with cutis laxa and multiple coagulation factor deficiency represents a separate genetic entity."
    Vanakker O.M., Martin L., Gheduzzi D., Leroy B.P., Loeys B.L., Guerci V.I., Matthys D., Terry S.F., Coucke P.J., Pasquali-Ronchetti I., De Paepe A.
    J. Invest. Dermatol. 127:581-587(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PXEL-MCFD SER-299; CYS-476; HIS-476; SER-493 AND ARG-558.

Entry informationi

Entry nameiVKGC_HUMAN
AccessioniPrimary (citable) accession number: P38435
Secondary accession number(s): B4DMC5
, E9PEE1, Q14415, Q6GU45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: December 20, 2005
Last modified: October 29, 2014
This is version 138 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

Miscellaneous

The vitamin K-dependent protein substrates of carboxylase have usually a propeptide that binds to a high-affinity site on the carboxylase. CO2, O2 and reduced vitamin K are cosubstrates.

Keywords - Technical termi

Complete proteome, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3