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Protein

Glycine dehydrogenase (decarboxylating), mitochondrial

Gene

GLDC

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

Functioni

The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO2 is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (GCSH).

Catalytic activityi

Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO2.

Cofactori

Enzyme regulationi

Stimulated by lipoic acid. Inhibited in presence of methylamine (By similarity).By similarity

GO - Molecular functioni

  • electron carrier activity Source: UniProtKB
  • glycine dehydrogenase (decarboxylating) activity Source: ProtInc
  • lyase activity Source: InterPro
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  • glycine catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS00622-MONOMER.
SABIO-RKP23378.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine dehydrogenase (decarboxylating), mitochondrial (EC:1.4.4.2)
Alternative name(s):
Glycine cleavage system P protein
Glycine decarboxylase
Glycine dehydrogenase (aminomethyl-transferring)
Gene namesi
Name:GLDC
Synonyms:GCSP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:4313. GLDC.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Non-ketotic hyperglycinemia (NKH)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAutosomal recessive disease characterized by accumulation of a large amount of glycine in body fluid and by severe neurological symptoms.

See also OMIM:605899
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti283 – 2831A → P in NKH. 1 Publication
VAR_016849
Natural varianti515 – 5151R → S in NKH. 1 Publication
Corresponds to variant rs121964976 [ dbSNP | Ensembl ].
VAR_016851
Natural varianti564 – 5641S → I in NKH; common mutation in Finland. 1 Publication
VAR_004979
Natural varianti756 – 7561Missing in NKH. 1 Publication
VAR_009939

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi605899. phenotype.
Orphaneti289863. Atypical glycine encephalopathy.
289860. Infantile glycine encephalopathy.
289857. Neonatal glycine encephalopathy.
PharmGKBiPA28716.

Chemistry

DrugBankiDB00145. Glycine.

Polymorphism and mutation databases

BioMutaiGLDC.
DMDMi229462870.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionSequence AnalysisAdd
BLAST
Chaini36 – 1020985Glycine dehydrogenase (decarboxylating), mitochondrialPRO_0000010740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei447 – 4471N6-acetyllysineBy similarity
Modified residuei514 – 5141N6-acetyllysineBy similarity
Modified residuei648 – 6481N6-acetyllysineBy similarity
Modified residuei664 – 6641N6-acetyllysineBy similarity
Modified residuei754 – 7541N6-(pyridoxal phosphate)lysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP23378.
PaxDbiP23378.
PRIDEiP23378.

PTM databases

PhosphoSiteiP23378.

Expressioni

Gene expression databases

BgeeiP23378.
CleanExiHS_GLDC.
GenevestigatoriP23378.

Organism-specific databases

HPAiHPA002318.
HPA052887.

Interactioni

Subunit structurei

Interacts with GCSH (By similarity). Homodimer. The glycine cleavage system is composed of four proteins: P (GLDC), T (GCST), L (DLD) and H (GCSH).By similarity

Protein-protein interaction databases

BioGridi108993. 15 interactions.
IntActiP23378. 6 interactions.
MINTiMINT-7554996.
STRINGi9606.ENSP00000370737.

Structurei

3D structure databases

ProteinModelPortaliP23378.
SMRiP23378. Positions 46-1005.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GcvP family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1003.
GeneTreeiENSGT00390000017970.
HOGENOMiHOG000239369.
HOVERGENiHBG005820.
InParanoidiP23378.
KOiK00281.
OMAiRAESEMT.
OrthoDBiEOG7FJGZQ.
PhylomeDBiP23378.
TreeFamiTF300678.

Family and domain databases

Gene3Di3.40.640.10. 2 hits.
HAMAPiMF_00711. GcvP.
InterProiIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR003437. GcvP.
IPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11773. PTHR11773. 1 hit.
PfamiPF01212. Beta_elim_lyase. 1 hit.
PF02347. GDC-P. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 3 hits.
TIGRFAMsiTIGR00461. gcvP. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P23378-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSCARAWGL RLGRGVGGGR RLAGGSGPCW APRSRDSSSG GGDSAAAGAS
60 70 80 90 100
RLLERLLPRH DDFARRHIGP GDKDQREMLQ TLGLASIDEL IEKTVPANIR
110 120 130 140 150
LKRPLKMEDP VCENEILATL HAISSKNQIW RSYIGMGYYN CSVPQTILRN
160 170 180 190 200
LLENSGWITQ YTPYQPEVSQ GRLESLLNYQ TMVCDITGLD MANASLLDEG
210 220 230 240 250
TAAAEALQLC YRHNKRRKFL VDPRCHPQTI AVVQTRAKYT GVLTELKLPC
260 270 280 290 300
EMDFSGKDVS GVLFQYPDTE GKVEDFTELV ERAHQSGSLA CCATDLLALC
310 320 330 340 350
ILRPPGEFGV DIALGSSQRF GVPLGYGGPH AAFFAVRESL VRMMPGRMVG
360 370 380 390 400
VTRDATGKEV YRLALQTREQ HIRRDKATSN ICTAQALLAN MAAMFAIYHG
410 420 430 440 450
SHGLEHIARR VHNATLILSE GLKRAGHQLQ HDLFFDTLKI QCGCSVKEVL
460 470 480 490 500
GRAAQRQINF RLFEDGTLGI SLDETVNEKD LDDLLWIFGC ESSAELVAES
510 520 530 540 550
MGEECRGIPG SVFKRTSPFL THQVFNSYHS ETNIVRYMKK LENKDISLVH
560 570 580 590 600
SMIPLGSCTM KLNSSSELAP ITWKEFANIH PFVPLDQAQG YQQLFRELEK
610 620 630 640 650
DLCELTGYDQ VCFQPNSGAQ GEYAGLATIR AYLNQKGEGH RTVCLIPKSA
660 670 680 690 700
HGTNPASAHM AGMKIQPVEV DKYGNIDAVH LKAMVDKHKE NLAAIMITYP
710 720 730 740 750
STNGVFEENI SDVCDLIHQH GGQVYLDGAN MNAQVGICRP GDFGSDVSHL
760 770 780 790 800
NLHKTFCIPH GGGGPGMGPI GVKKHLAPFL PNHPVISLKR NEDACPVGTV
810 820 830 840 850
SAAPWGSSSI LPISWAYIKM MGGKGLKQAT ETAILNANYM AKRLETHYRI
860 870 880 890 900
LFRGARGYVG HEFILDTRPF KKSANIEAVD VAKRLQDYGF HAPTMSWPVA
910 920 930 940 950
GTLMVEPTES EDKAELDRFC DAMISIRQEI ADIEEGRIDP RVNPLKMSPH
960 970 980 990 1000
SLTCVTSSHW DRPYSREVAA FPLPFVKPEN KFWPTIARID DIYGDQHLVC
1010 1020
TCPPMEVYES PFSEQKRASS
Length:1,020
Mass (Da):112,730
Last modified:May 5, 2009 - v2
Checksum:i8FAEA7D56BEB17B2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti396 – 3961A → R in AAA36463 (PubMed:1993704).Curated
Sequence conflicti396 – 3961A → R in BAA14286 (PubMed:1993704).Curated
Sequence conflicti441 – 4411Q → H in AAA36478 (PubMed:1996985).Curated
Sequence conflicti441 – 4411Q → H in AAA36463 (PubMed:1993704).Curated
Sequence conflicti441 – 4411Q → H in BAA14286 (PubMed:1993704).Curated
Sequence conflicti608 – 6081Y → H in AAA36478 (PubMed:1996985).Curated
Sequence conflicti976 – 9761V → M in AAA36463 (PubMed:1993704).Curated
Sequence conflicti976 – 9761V → M in BAA14286 (PubMed:1993704).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti283 – 2831A → P in NKH. 1 Publication
VAR_016849
Natural varianti329 – 3291P → T in one non-ketotic hyperglycinemia patient. 1 Publication
VAR_016850
Natural varianti515 – 5151R → S in NKH. 1 Publication
Corresponds to variant rs121964976 [ dbSNP | Ensembl ].
VAR_016851
Natural varianti564 – 5641S → I in NKH; common mutation in Finland. 1 Publication
VAR_004979
Natural varianti756 – 7561Missing in NKH. 1 Publication
VAR_009939

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63635 mRNA. Translation: AAA36478.1.
M64590 mRNA. Translation: AAA36463.1.
D90239 mRNA. Translation: BAA14286.1.
AK314156 mRNA. Translation: BAG36841.1.
AL353718, AL162411 Genomic DNA. Translation: CAQ07607.1.
AL162411, AL353718 Genomic DNA. Translation: CAQ10367.1.
CH471071 Genomic DNA. Translation: EAW58740.1.
BC111993 mRNA. Translation: AAI11994.1.
BC111995 mRNA. Translation: AAI11996.1.
CCDSiCCDS34987.1.
PIRiJN0124.
RefSeqiNP_000161.2. NM_000170.2.
UniGeneiHs.584238.

Genome annotation databases

EnsembliENST00000321612; ENSP00000370737; ENSG00000178445.
GeneIDi2731.
KEGGihsa:2731.
UCSCiuc003zkc.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63635 mRNA. Translation: AAA36478.1.
M64590 mRNA. Translation: AAA36463.1.
D90239 mRNA. Translation: BAA14286.1.
AK314156 mRNA. Translation: BAG36841.1.
AL353718, AL162411 Genomic DNA. Translation: CAQ07607.1.
AL162411, AL353718 Genomic DNA. Translation: CAQ10367.1.
CH471071 Genomic DNA. Translation: EAW58740.1.
BC111993 mRNA. Translation: AAI11994.1.
BC111995 mRNA. Translation: AAI11996.1.
CCDSiCCDS34987.1.
PIRiJN0124.
RefSeqiNP_000161.2. NM_000170.2.
UniGeneiHs.584238.

3D structure databases

ProteinModelPortaliP23378.
SMRiP23378. Positions 46-1005.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108993. 15 interactions.
IntActiP23378. 6 interactions.
MINTiMINT-7554996.
STRINGi9606.ENSP00000370737.

Chemistry

DrugBankiDB00145. Glycine.

PTM databases

PhosphoSiteiP23378.

Polymorphism and mutation databases

BioMutaiGLDC.
DMDMi229462870.

Proteomic databases

MaxQBiP23378.
PaxDbiP23378.
PRIDEiP23378.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321612; ENSP00000370737; ENSG00000178445.
GeneIDi2731.
KEGGihsa:2731.
UCSCiuc003zkc.3. human.

Organism-specific databases

CTDi2731.
GeneCardsiGC09M006522.
GeneReviewsiGLDC.
H-InvDBHIX0034882.
HGNCiHGNC:4313. GLDC.
HPAiHPA002318.
HPA052887.
MIMi238300. gene.
605899. phenotype.
neXtProtiNX_P23378.
Orphaneti289863. Atypical glycine encephalopathy.
289860. Infantile glycine encephalopathy.
289857. Neonatal glycine encephalopathy.
PharmGKBiPA28716.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1003.
GeneTreeiENSGT00390000017970.
HOGENOMiHOG000239369.
HOVERGENiHBG005820.
InParanoidiP23378.
KOiK00281.
OMAiRAESEMT.
OrthoDBiEOG7FJGZQ.
PhylomeDBiP23378.
TreeFamiTF300678.

Enzyme and pathway databases

BioCyciMetaCyc:HS00622-MONOMER.
SABIO-RKP23378.

Miscellaneous databases

GeneWikiiGlycine_dehydrogenase_(decarboxylating).
GenomeRNAii2731.
NextBioi10764.
PROiP23378.
SOURCEiSearch...

Gene expression databases

BgeeiP23378.
CleanExiHS_GLDC.
GenevestigatoriP23378.

Family and domain databases

Gene3Di3.40.640.10. 2 hits.
HAMAPiMF_00711. GcvP.
InterProiIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR003437. GcvP.
IPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11773. PTHR11773. 1 hit.
PfamiPF01212. Beta_elim_lyase. 1 hit.
PF02347. GDC-P. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 3 hits.
TIGRFAMsiTIGR00461. gcvP. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural and expression analyses of normal and mutant mRNA encoding glycine decarboxylase: three-base deletion in mRNA causes nonketotic hyperglycinemia."
    Kure S., Narisawa K., Tada K.
    Biochem. Biophys. Res. Commun. 174:1176-1182(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT NKH PHE-756 DEL.
  2. "The glycine cleavage system. Molecular cloning of the chicken and human glycine decarboxylase cDNAs and some characteristics involved in the deduced protein structures."
    Kume A., Koyata H., Sakakibara T., Ishiguro Y., Kure S., Hiraga K.
    J. Biol. Chem. 266:3323-3329(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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].
    Tissue: Brain.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Identification of a common mutation in Finnish patients with nonketotic hyperglycinemia."
    Kure S., Takayanagi M., Narisawa K., Tada K., Leisti J.
    J. Clin. Invest. 90:160-164(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NKH ILE-564.
  11. "Recurrent mutations in P- and T-proteins of the glycine cleavage complex and a novel T-protein mutation (N145I): a strategy for the molecular investigation of patients with nonketotic hyperglycinemia (NKH)."
    Toone J.R., Applegarth D.A., Coulter-Mackie M.B., James E.R.
    Mol. Genet. Metab. 72:322-325(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NKH SER-515.
  12. "Nonketotic hyperglycinemia (glycine encephalopathy): laboratory diagnosis."
    Applegarth D.A., Toone J.R.
    Mol. Genet. Metab. 74:139-146(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NKH PRO-283, VARIANT THR-329.

Entry informationi

Entry nameiGCSP_HUMAN
AccessioniPrimary (citable) accession number: P23378
Secondary accession number(s): Q2M2F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: May 5, 2009
Last modified: April 29, 2015
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.