Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9GZT8 (GTPC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative GTP cyclohydrolase 1 type 2 NIF3L1

EC=3.5.4.16
Alternative name(s):
Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 1 protein
GTP cyclohydrolase I
NIF3-like protein 1
Gene names
Name:NIF3L1
Synonyms:ALS2CR1
ORF Names:MDS015, My018
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts GTP to dihydroneopterin triphosphate By similarity.

Catalytic activity

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.

Subunit structure

Homodimer. Interacts with COPS2 By similarity. Interacts with THOC7. Ref.10

Subcellular location

Cytoplasm Ref.1 Ref.10.

Sequence similarities

Belongs to the GTP cyclohydrolase I type 2 family.

Sequence caution

The sequence AAG14952.1 differs from that shown. Reason: Frameshift at positions 104 and 109.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9GZT8-1)

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: Q9GZT8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.
Isoform 3 (identifier: Q9GZT8-3)

Also known as: beta;

The sequence of this isoform differs from the canonical sequence as follows:
     243-377: PLLLHTGMGR...ETDRDPLQVV → SLKSKSWPCV...MILWMLLPKE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Putative GTP cyclohydrolase 1 type 2 NIF3L1
PRO_0000147353

Sites

Metal binding931Divalent metal cation 2 By similarity
Metal binding1311Divalent metal cation 1 By similarity
Metal binding3391Divalent metal cation 2 By similarity
Metal binding3431Divalent metal cation 1 By similarity
Metal binding3431Divalent metal cation 2 By similarity

Amino acid modifications

Modified residue1091N6-acetyllysine Ref.11

Natural variations

Alternative sequence1 – 2727Missing in isoform 2.
VSP_029328
Alternative sequence243 – 377135PLLLH…PLQVV → SLKSKSWPCVLVLGAAFCRV LRLTFTSQVRCPIMILWMLL PKE in isoform 3.
VSP_043248
Natural variant3241T → I.
Corresponds to variant rs7917 [ dbSNP | Ensembl ].
VAR_037084

Experimental info

Sequence conflict1091K → E in AAG14952. Ref.5

Sequences

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

Last modified November 13, 2007. Version 2.
Checksum: 41BDCADDD81CA0D8

FASTA37741,968
        10         20         30         40         50         60 
MLSSCVRPVP TTVRFVDSLI CNSSRSFMDL KALLSSLNDF ASLSFAESWD NVGLLVEPSP 

        70         80         90        100        110        120 
PHTVNTLFLT NDLTEEVMEE VLQKKADLIL SYHPPIFRPM KRITWNTWKE RLVIRALENR 

       130        140        150        160        170        180 
VGIYSPHTAY DAAPQGVNNW LAKGLGACTS RPIHPSKAPN YPTEGNHRVE FNVNYTQDLD 

       190        200        210        220        230        240 
KVMSAVKGID GVSVTSFSAR TGNEEQTRIN LNCTQKALMQ VVDFLSRNKQ LYQKTEILSL 

       250        260        270        280        290        300 
EKPLLLHTGM GRLCTLDESV SLATMIDRIK RHLKLSHIRL ALGVGRTLES QVKVVALCAG 

       310        320        330        340        350        360 
SGSSVLQGVE ADLYLTGEMS HHDTLDAASQ GINVILCEHS NTERGFLSDL RDMLDSHLEN 

       370 
KINIILSETD RDPLQVV 

« Hide

Isoform 2 [UniParc].

Checksum: 81F1A5AD35B25ED7
Show »

FASTA35038,984
Isoform 3 (beta) [UniParc].

Checksum: 5084AD8C6E9700EC
Show »

FASTA28532,164

References

« Hide 'large scale' references
[1]"Isolation and characterization of a novel human gene, NIF3L1, and its mouse ortholog, Nif3l1, highly conserved from bacteria to mammals."
Tascou S., Uedelhoven J., Dixkens C., Nayernia K., Engel W., Burfeind P.
Cytogenet. Cell Genet. 90:330-336(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
[2]"Cloning and characterization of three novel genes, ALS2CR1, ALS2CR2, and ALS2CR3, in the juvenile amyotrophic lateral sclerosis (ALS2) critical region at chromosome 2q33-q34: candidate genes for ALS2."
Hadano S., Yanagisawa Y., Skaug J., Fichter K., Nasir J., Martindale D., Koop B.F., Scherer S.W., Nicholson D.W., Rouleau G.A., Ikeda J.-E., Hayden M.R.
Genomics 71:200-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"NIF3L1 interacts with WBSCR14."
Merla G., Reymond A.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]Mao Y.M., Xie Y., Huang X.Y., Ying K., Dai J.L.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal brain.
[5]"Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Hematopoietic stem cell.
[6]"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: Ovarian carcinoma.
[7]"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].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: Skin.
[10]"Identification and characterization of NIF3L1 BP1, a novel cytoplasmic interaction partner of the NIF3L1 protein."
Tascou S., Kang T.W., Trappe R., Engel W., Burfeind P.
Biochem. Biophys. Res. Commun. 309:440-448(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH THOC7, SUBCELLULAR LOCATION.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF283538 mRNA. Translation: AAG44846.1.
AB038949 mRNA. Translation: BAB32499.1.
AY251943 mRNA. Translation: AAP84063.1.
AF060513 mRNA. Translation: AAG43131.1.
AF182416 mRNA. Translation: AAG14952.1. Frameshift.
AK023378 mRNA. Translation: BAB14551.1.
AC005037 Genomic DNA. Translation: AAY14724.1.
CH471063 Genomic DNA. Translation: EAW70224.1.
BC007654 mRNA. Translation: AAH07654.1.
CCDSCCDS42797.1. [Q9GZT8-2]
CCDS46485.1. [Q9GZT8-1]
CCDS46486.1. [Q9GZT8-3]
RefSeqNP_001129511.1. NM_001136039.2. [Q9GZT8-1]
NP_001135827.1. NM_001142355.1. [Q9GZT8-2]
NP_001135828.1. NM_001142356.1. [Q9GZT8-3]
NP_068596.2. NM_021824.3. [Q9GZT8-2]
XP_005246799.1. XM_005246742.2. [Q9GZT8-1]
XP_006712739.1. XM_006712676.1. [Q9GZT8-3]
UniGeneHs.145284.

3D structure databases

ProteinModelPortalQ9GZT8.
SMRQ9GZT8. Positions 52-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121922. 78 interactions.
IntActQ9GZT8. 39 interactions.
MINTMINT-1438019.
STRING9606.ENSP00000386394.

PTM databases

PhosphoSiteQ9GZT8.

Polymorphism databases

DMDM160112850.

Proteomic databases

MaxQBQ9GZT8.
PaxDbQ9GZT8.
PRIDEQ9GZT8.

Protocols and materials databases

DNASU60491.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359683; ENSP00000352711; ENSG00000196290. [Q9GZT8-2]
ENST00000409020; ENSP00000386394; ENSG00000196290. [Q9GZT8-1]
ENST00000409357; ENSP00000387315; ENSG00000196290. [Q9GZT8-1]
ENST00000409588; ENSP00000387021; ENSG00000196290. [Q9GZT8-3]
ENST00000416651; ENSP00000400787; ENSG00000196290. [Q9GZT8-1]
GeneID60491.
KEGGhsa:60491.
UCSCuc002uwl.2. human. [Q9GZT8-1]
uc002uwq.2. human. [Q9GZT8-3]

Organism-specific databases

CTD60491.
GeneCardsGC02P201718.
HGNCHGNC:13390. NIF3L1.
HPAHPA036335.
MIM605778. gene.
neXtProtNX_Q9GZT8.
PharmGKBPA31629.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0327.
HOGENOMHOG000014260.
HOVERGENHBG029337.
InParanoidQ9GZT8.
OMACPHTAVD.
PhylomeDBQ9GZT8.
TreeFamTF324125.

Enzyme and pathway databases

UniPathwayUPA00848; UER00151.

Gene expression databases

ArrayExpressQ9GZT8.
BgeeQ9GZT8.
CleanExHS_NIF3L1.
GenevestigatorQ9GZT8.

Family and domain databases

InterProIPR002678. GTP_cyclohydrolase_I/Nif3.
IPR017222. GTP_cyclohydrolase_I/NIF3_euk.
[Graphical view]
PANTHERPTHR13799. PTHR13799. 1 hit.
PfamPF01784. NIF3. 1 hit.
[Graphical view]
PIRSFPIRSF037490. UCP037490_NIF3_euk. 1 hit.
SUPFAMSSF102705. SSF102705. 1 hit.
TIGRFAMsTIGR00486. YbgI_SA1388. 1 hit.
ProtoNetSearch...

Other

GeneWikiNIF3L1.
GenomeRNAi60491.
NextBio65383.
PROQ9GZT8.
SOURCESearch...

Entry information

Entry nameGTPC1_HUMAN
AccessionPrimary (citable) accession number: Q9GZT8
Secondary accession number(s): Q53TX4 expand/collapse secondary AC list , Q6X735, Q9H2D2, Q9HC18
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 123 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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