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P38435 (VKGC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GGCX
Synonyms:GC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length758 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Catalytic activity

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

Subunit structure

Monomer. May interact with CALU By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.7.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.16 Ref.17 Ref.18

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

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.

Sequence similarities

Belongs to the vitamin K-dependent gamma-carboxylase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P38435-1)

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.
Isoform 2 (identifier: P38435-2)

The sequence of this isoform differs from the canonical sequence as follows:
     15-71: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 758757Vitamin K-dependent gamma-carboxylase
PRO_0000191823

Regions

Topological domain2 – 6059Cytoplasmic Potential
Transmembrane61 – 8121Helical; Potential
Topological domain82 – 11332Lumenal Potential
Transmembrane114 – 13421Helical; Potential
Topological domain135 – 1362Cytoplasmic Potential
Transmembrane137 – 15721Helical; Potential
Topological domain158 – 292135Lumenal Potential
Transmembrane293 – 31321Helical; Potential
Topological domain314 – 36148Cytoplasmic Potential
Transmembrane362 – 38221Helical; Potential
Topological domain383 – 758376Lumenal Potential

Sites

Active site2181Proton acceptor Ref.11

Amino acid modifications

Modified residue21N-acetylalanine Ref.12 Ref.14
Glycosylation4591N-linked (GlcNAc...) Ref.13
Glycosylation5501N-linked (GlcNAc...) Ref.13
Disulfide bond99 ↔ 450 Ref.9

Natural variations

Alternative sequence15 – 7157Missing in isoform 2.
VSP_046179
Natural variant2991F → S in PXEL-MCFD. Ref.19
VAR_032979
Natural variant3251R → Q. Ref.1
Corresponds to variant rs699664 [ dbSNP | Ensembl ].
VAR_005780
Natural variant3941L → R in VKCFD1; affects glutamate binding. Ref.15 Ref.17
VAR_005781
Natural variant4761R → C in PXEL-MCFD. Ref.19
VAR_032980
Natural variant4761R → H in PXEL-MCFD. Ref.19
VAR_032981
Natural variant4851R → P in VKCFD1. Ref.18
VAR_021826
Natural variant4931W → S in PXEL-MCFD. Ref.19
VAR_032982
Natural variant5011W → S in VKCFD1. Ref.16
Corresponds to variant rs28928872 [ dbSNP | Ensembl ].
VAR_015218
Natural variant5581G → R in PXEL-MCFD. Ref.19
VAR_032983

Experimental info

Mutagenesis1601H → A: No effect on activity. Ref.11
Mutagenesis2181K → A: No activity. Ref.11
Mutagenesis2871H → A: No effect on activity. Ref.11
Mutagenesis3811H → A: No effect on activity. Ref.11
Sequence conflict4001D → N in AAA91834. Ref.3
Sequence conflict6591F → S in BAG59837. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 720D5B08E9B558C8

FASTA75887,561
        10         20         30         40         50         60 
MAVSAGSART SPSSDKVQKD KAELISGPRQ DSRIGKLLGF EWTDLSSWRR LVTLLNRPTD 

        70         80         90        100        110        120 
PASLAVFRFL FGFLMVLDIP QERGLSSLDR KYLDGLDVCR FPLLDALRPL PLDWMYLVYT 

       130        140        150        160        170        180 
IMFLGALGMM LGLCYRISCV LFLLPYWYVF LLDKTSWNNH SYLYGLLAFQ LTFMDANHYW 

       190        200        210        220        230        240 
SVDGLLNAHR RNAHVPLWNY AVLRGQIFIV YFIAGVKKLD ADWVEGYSME YLSRHWLFSP 

       250        260        270        280        290        300 
FKLLLSEELT SLLVVHWGGL LLDLSAGFLL FFDVSRSIGL FFVSYFHCMN SQLFSIGMFS 

       310        320        330        340        350        360 
YVMLASSPLF CSPEWPRKLV SYCPRRLQQL LPLKAAPQPS VSCVYKRSRG KSGQKPGLRH 

       370        380        390        400        410        420 
QLGAAFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD MMVHSRSHQH VKITYRDGRT 

       430        440        450        460        470        480 
GELGYLNPGV FTQSRRWKDH ADMLKQYATC LSRLLPKYNV TEPQIYFDIW VSINDRFQQR 

       490        500        510        520        530        540 
IFDPRVDIVQ AAWSPFQRTS WVQPLLMDLS PWRAKLQEIK SSLDNHTEVV FIADFPGLHL 

       550        560        570        580        590        600 
ENFVSEDLGN TSIQLLQGEV TVELVAEQKN QTLREGEKMQ LPAGEYHKVY TTSPSPSCYM 

       610        620        630        640        650        660 
YVYVNTTELA LEQDLAYLQE LKEKVENGSE TGPLPPELQP LLEGEVKGGP EPTPLVQTFL 

       670        680        690        700        710        720 
RRQQRLQEIE RRRNTPFHER FFRFLLRKLY VFRRSFLMTC ISLRNLILGR PSLEQLAQEV 

       730        740        750 
TYANLRPFEA VGELNPSNTD SSHSNPPESN PDPVHSEF 

« Hide

Isoform 2 [UniParc].

Checksum: CA7D806186E791B5
Show »

FASTA70180,989

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA39283.
RefSeqNP_000812.2. NM_000821.5.
NP_001135741.1. NM_001142269.2.
UniGeneHs.77719.

3D structure databases

ProteinModelPortalP38435.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108945. 2 interactions.
STRING9606.ENSP00000233838.

Chemistry

ChEMBLCHEMBL2012.
DrugBankDB01125. Anisindione.
DB00100. Coagulation Factor IX.
DB00036. Coagulation factor VIIa.
DB00055. Drotrecogin alfa.
DB00142. L-Glutamic Acid.
DB00170. Menadione.
DB01022. Phytonadione.

PTM databases

PhosphoSiteP38435.

Polymorphism databases

DMDM84028279.

Proteomic databases

PaxDbP38435.
PRIDEP38435.

Protocols and materials databases

DNASU2677.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233838; ENSP00000233838; ENSG00000115486. [P38435-1]
ENST00000430215; ENSP00000408045; ENSG00000115486. [P38435-2]
GeneID2677.
KEGGhsa:2677.
UCSCuc002sps.3. human. [P38435-1]

Organism-specific databases

CTD2677.
GeneCardsGC02M085771.
HGNCHGNC:4247. GGCX.
HPAHPA018284.
MIM137167. gene.
277450. phenotype.
610842. phenotype.
neXtProtNX_P38435.
Orphanet91135. Body skin hyperlaxity due to vitamin K-dependent coagulation factor deficiency.
98434. Hereditary combined deficiency of vitamin K-dependent clotting factors.
PharmGKBPA28660.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG83578.
HOGENOMHOG000007593.
HOVERGENHBG012798.
InParanoidP38435.
KOK10106.
OMASPSCYMY.
OrthoDBEOG7B5WV9.
PhylomeDBP38435.
TreeFamTF323879.

Enzyme and pathway databases

BioCycMetaCyc:HS03897-MONOMER.
ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP38435.
BgeeP38435.
CleanExHS_GC.
HS_GGCX.
GenevestigatorP38435.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR011020. HTTM.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
IPR007782. VKG_COase.
[Graphical view]
PANTHERPTHR12639. PTHR12639. 1 hit.
PfamPF05090. VKG_Carbox. 1 hit.
[Graphical view]
SMARTSM00752. HTTM. 1 hit.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGGCX. human.
GeneWikiGamma-glutamyl_carboxylase.
GenomeRNAi2677.
NextBio10570.
PROP38435.
SOURCESearch...

Entry information

Entry nameVKGC_HUMAN
AccessionPrimary (citable) accession number: P38435
Secondary accession number(s): B4DMC5 expand/collapse secondary AC list , E9PEE1, Q14415, Q6GU45
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM