Q9NZB8 (MOCS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Molybdenum cofactor biosynthesis protein 1

Alternative name(s):
Cell migration-inducing gene 11 protein
Molybdenum cofactor synthesis-step 1 protein A-B

Including the following 2 domains:

1. Cyclic pyranopterin monophosphate synthase
   EC=4.1.99.18
   Alternative name(s):
   Molybdenum cofactor biosynthesis protein A
2. Cyclic pyranopterin monophosphate synthase accessory protein
   Alternative name(s):
   Molybdenum cofactor biosynthesis protein C

Gene names

Name:	MOCS1
ORF Names:	MIG11

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	636 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Isoform MOCS1A and isoform MOCS1B probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z). Ref.8
Catalytic activity	GTP = cyclic pyranopterin monophosphate + diphosphate. Ref.8
Cofactor	Binds 2 4Fe-4S clusters. Binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate. Ref.10
Pathway	Cofactor biosynthesis; molybdopterin biosynthesis.
Subunit structure	Isoform MOCS1A and isoform MOCS1B probably form a heterooligomer Probable.
Tissue specificity	Isoform MOCS1A and isoform 2 are widely expressed. Ref.1 Ref.9
Post-translational modification	Isoform MOCS1A, isoform 2 and isoform 3 are probably thiocarboxylated at their C-terminus. Thiocarboxylation probably plays a central role in molybdenum cofactor biosynthesis, since mutagenesis of the last 2 Gly residues of isoform MOCS1A abolishes the catalytic activity of the enzyme. Thiocarboxylation is absent in isoform MOCS1B, which lacks the C-terminal Gly residue.
Involvement in disease	Molybdenum cofactor deficiency type A (MOCOD type A) [MIM:252150]: Autosomal recessive disease which leads to the pleiotropic loss of all molybdoenzyme activities and is characterized by severe neurological damage, neonatal seizures and early childhood death. Note: The disease is caused by mutations affecting the gene represented in this entry.
Miscellaneous	The MOCS1 locus has initially been reported to produce MOCS1A and MOCS1B from non-overlapping reading frames within a bicistronic transcript. However, only isoform MOCS1A seems to be translated from the bicistronic transcript. Isoform MOCS1B seems to be translated from a monocistronic mRNA that is derived by alternative splicing.
Sequence similarities	In the C-terminal section; belongs to the MoaC family. In the N-terminal section; belongs to the MoaA/NifB/PqqE family.
Sequence caution	The sequence AAB87524.1 differs from that shown. Reason: Alternative splicing in the MOCS1A-MOCS1B joining region. The sequence AAS00489.1 differs from that shown. Reason: Erroneous initiation. The sequence CAC44526.1 differs from that shown. Reason: Alternative splicing in the MOCS1A-MOCS1B joining region. The sequence CAI20007.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI20012.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI20013.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	4Fe-4S GTP-binding Iron Iron-sulfur Metal-binding Nucleotide-binding S-adenosyl-L-methionine
Molecular function	Lyase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Mo-molybdopterin cofactor biosynthetic process Inferred from direct assay Ref.10. Source: UniProtKB water-soluble vitamin metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome molybdopterin synthase complex Inferred from electronic annotation. Source: InterPro nucleus Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from direct assay Ref.10. Source: UniProtKB GTP binding Inferred from electronic annotation. Source: UniProtKB-KW lyase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: So far, the different types of MOCS1A and MOCS1B isoforms have been investigated independently and several combinations might be possible.

Isoform MOCS1B (identifier: Q9NZB8-1)

Also known as: MOCS1B Type-II;

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.

Note: Multidomain protein with inactive MOCS1A and active MOCS1B.

Isoform MOCS1A (identifier: Q9NZB8-5)

Also known as: MOCS1A Type/Iad;

The sequence of this isoform differs from the canonical sequence as follows:
     384-385: EL → GG
     386-636: Missing.

Note: Contains a 1-thioglycine at position 385 (Probable).

Isoform 2 (identifier: Q9NZB8-6)

Also known as: MOCS1A Type-Ibcd;

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MAARPLSRML...PGESARAASE → MWKSWKLRTD...PCFLPGLSSQ
     384-385: EL → GG
     386-636: Missing.

Note: Contains a 1-thioglycine at position 385 (Probable).

Isoform 3 (identifier: Q9NZB8-3)

Also known as: MOCS1A Type-Ibd;

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MAARPLSRMLRRLLRSSARSCSSGAPVTQPCPGESARAASE → MWKSWKLRTDVR
     384-385: EL → GG
     386-636: Missing.

Note: Contains a 1-thioglycine at position 356 (Probable).

Isoform 4 (identifier: Q9NZB8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.
     368-368: G → E
     369-636: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 6 (identifier: Q9NZB8-2)

Also known as: MOCS1B Type-III;

The sequence of this isoform differs from the canonical sequence as follows:
     368-383: Missing.

Note: Multidomain protein with inactive MOCS1A and active MOCS1B.

Isoform 7 (identifier: Q9NZB8-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.
     368-383: Missing.

Isoform 8 (identifier: Q9NZB8-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MAARPLSRML...PGESARAASE → MWKSWKLRTD...PCFLPGLSSQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 636	636	Molybdenum cofactor biosynthesis protein 1		PRO_0000097870
Regions
	Region	1 – 383	383	Molybdenum cofactor biosynthesis protein A
	Region	317 – 319	3	GTP binding By similarity
	Region	414 – 636	223	Molybdenum cofactor biosynthesis protein C
Sites
	Active site	606	1	For molybdenum cofactor biosynthesis protein C activity Potential
	Metal binding	80	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) Probable
	Metal binding	84	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) Probable
	Metal binding	87	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) Probable
	Metal binding	312	1	Iron-sulfur 2 (4Fe-4S-substrate) Probable
	Metal binding	315	1	Iron-sulfur 2 (4Fe-4S-substrate) Probable
	Metal binding	329	1	Iron-sulfur 2 (4Fe-4S-substrate) Probable
	Binding site	73	1	GTP By similarity
	Binding site	86	1	S-adenosyl-L-methionine By similarity
	Binding site	123	1	GTP By similarity
	Binding site	127	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	154	1	GTP By similarity
	Binding site	178	1	S-adenosyl-L-methionine By similarity
	Binding site	215	1	GTP By similarity
	Binding site	249	1	S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	198	1	N6-acetyllysine Ref.11
Natural variations
	Alternative sequence	1 – 87	87	Missing in isoform 4 and isoform 7.		VSP_036821
	Alternative sequence	1 – 41	41	MAARP…RAASE → MWKSWKLRTDVRVREGAGGS PCASSQPGSRGPCFLPGLSS Q in isoform 2 and isoform 8.		VSP_036822
	Alternative sequence	1 – 41	41	MAARP…RAASE → MWKSWKLRTDVR in isoform 3.		VSP_036823
	Alternative sequence	368 – 383	16	Missing in isoform 6 and isoform 7.		VSP_007439
	Alternative sequence	368	1	G → E in isoform 4.		VSP_036824
	Alternative sequence	369 – 636	268	Missing in isoform 4.		VSP_036825
	Alternative sequence	384 – 385	2	EL → GG in isoform MOCS1A, isoform 2 and isoform 3.		VSP_036826
	Alternative sequence	386 – 636	251	Missing in isoform MOCS1A, isoform 2 and isoform 3.		VSP_036827
	Natural variant	67	1	R → W in MOCOD type A. Ref.14		VAR_054823
	Natural variant	73	1	R → W in MOCOD type A. Ref.12		VAR_015658
	Natural variant	80	1	C → G in MOCOD type A. Ref.14		VAR_054824
	Natural variant	84	1	C → F in MOCOD type A. Ref.14		VAR_054825
	Natural variant	123	1	R → W in MOCOD type A. Ref.13		VAR_054826
	Natural variant	126	1	G → D in MOCOD type A. Ref.12		VAR_015659
	Natural variant	127	1	G → D in MOCOD type A. Ref.12		VAR_015660
	Natural variant	319	1	R → Q in MOCOD type A. Ref.12		VAR_015661
	Natural variant	324	1	G → E in MOCOD type A. Ref.12		VAR_015662
	Natural variant	324	1	G → R in MOCOD type A. Ref.13		VAR_054827
	Natural variant	390	1	P → H. Corresponds to variant rs11969769 [ dbSNP | Ensembl ].		VAR_056131
	Natural variant	452	1	R → L. Corresponds to variant rs11969206 [ dbSNP | Ensembl ].		VAR_061346
Experimental info
	Mutagenesis	80	1	C → S: Impairs precursor Z synthesis. Ref.10
	Mutagenesis	84	1	C → S: Impairs precursor Z synthesis. Ref.10
	Mutagenesis	87	1	C → S: Impairs precursor Z synthesis. Ref.10
	Mutagenesis	312	1	C → S: Impairs precursor Z synthesis. Ref.10
	Mutagenesis	315	1	C → S: Impairs precursor Z synthesis. Ref.10
	Mutagenesis	329	1	C → S: Impairs precursor Z synthesis. Ref.10
	Sequence conflict	233	1	A → V in BAG51799. Ref.3
	Sequence conflict	233	1	A → V in BAG62053. Ref.3
	Sequence conflict	239	1	L → H in AAB87523. Ref.2
	Sequence conflict	421	1	A → G in BAG51799. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform MOCS1B (MOCS1B Type-II) [UniParc]. Last modified May 16, 2003. Version 3. Checksum: 6774A563BAC42120	FASTA	636	70,105
	10 20 30 40 50 60 MAARPLSRML RRLLRSSARS CSSGAPVTQP CPGESARAAS EEVSRRRQFL REHAAPFSAF 70 80 90 100 110 120 LTDSFGRQHS YLRISLTEKC NLRCQYCMPE EGVPLTPKAN LLTTEEILTL ARLFVKEGID 130 140 150 160 170 180 KIRLTGGEPL IRPDVVDIVA QLQRLEGLRT IGVTTNGINL ARLLPQLQKA GLSAINISLD 190 200 210 220 230 240 TLVPAKFEFI VRRKGFHKVM EGIHKAIELG YNPVKVNCVV MRGLNEDELL DFAALTEGLP 250 260 270 280 290 300 LDVRFIEYMP FDGNKWNFKK MVSYKEMLDT VRQQWPELEK VPEEESSTAK AFKIPGFQGQ 310 320 330 340 350 360 ISFITSMSEH FCGTCNRLRI TADGNLKVCL FGNSEVSLRD HLRAGASEQE LLRIIGAAVG 370 380 390 400 410 420 RKKRQHAGMF SISQMKNRPM ILIELFLMFP NSPPANPSIF SWDPLHVQGL RPRMSFSSQV 430 440 450 460 470 480 ATLWKGCRVP QTPPLAQQRL GSGSFQRHYT SRADSDANSK CLSPGSWASA APSGPQLTSE 490 500 510 520 530 540 QLTHVDSEGR AAMVDVGRKP DTERVAVASA VVLLGPVAFK LVQQNQLKKG DALVVAQLAG 550 560 570 580 590 600 VQAAKVTSQL IPLCHHVALS HIQVQLELDS TRHAVKIQAS CRARGPTGVE MEALTSAAVA 610 620 630 ALTLYDMCKA VSRDIVLEEI KLISKTGGQR GDFHRA
	Isoform MOCS1A (MOCS1A Type/Iad) [UniParc]. Checksum: 77AB231D6DBB267E	FASTA	385	43,088
	10 20 30 40 50 60 MAARPLSRML RRLLRSSARS CSSGAPVTQP CPGESARAAS EEVSRRRQFL REHAAPFSAF 70 80 90 100 110 120 LTDSFGRQHS YLRISLTEKC NLRCQYCMPE EGVPLTPKAN LLTTEEILTL ARLFVKEGID 130 140 150 160 170 180 KIRLTGGEPL IRPDVVDIVA QLQRLEGLRT IGVTTNGINL ARLLPQLQKA GLSAINISLD 190 200 210 220 230 240 TLVPAKFEFI VRRKGFHKVM EGIHKAIELG YNPVKVNCVV MRGLNEDELL DFAALTEGLP 250 260 270 280 290 300 LDVRFIEYMP FDGNKWNFKK MVSYKEMLDT VRQQWPELEK VPEEESSTAK AFKIPGFQGQ 310 320 330 340 350 360 ISFITSMSEH FCGTCNRLRI TADGNLKVCL FGNSEVSLRD HLRAGASEQE LLRIIGAAVG 370 380 RKKRQHAGMF SISQMKNRPM ILIGG
	Isoform 2 (MOCS1A Type-Ibcd) [UniParc]. Checksum: 8E43CD0F611F8804	FASTA	385	43,150
	10 20 30 40 50 60 MWKSWKLRTD VRVREGAGGS PCASSQPGSR GPCFLPGLSS QEVSRRRQFL REHAAPFSAF 70 80 90 100 110 120 LTDSFGRQHS YLRISLTEKC NLRCQYCMPE EGVPLTPKAN LLTTEEILTL ARLFVKEGID 130 140 150 160 170 180 KIRLTGGEPL IRPDVVDIVA QLQRLEGLRT IGVTTNGINL ARLLPQLQKA GLSAINISLD 190 200 210 220 230 240 TLVPAKFEFI VRRKGFHKVM EGIHKAIELG YNPVKVNCVV MRGLNEDELL DFAALTEGLP 250 260 270 280 290 300 LDVRFIEYMP FDGNKWNFKK MVSYKEMLDT VRQQWPELEK VPEEESSTAK AFKIPGFQGQ 310 320 330 340 350 360 ISFITSMSEH FCGTCNRLRI TADGNLKVCL FGNSEVSLRD HLRAGASEQE LLRIIGAAVG 370 380 RKKRQHAGMF SISQMKNRPM ILIGG
	Isoform 3 (MOCS1A Type-Ibd) [UniParc]. Checksum: 99F4B6D6B6A7B885	FASTA	356	40,378
	10 20 30 40 50 60 MWKSWKLRTD VREVSRRRQF LREHAAPFSA FLTDSFGRQH SYLRISLTEK CNLRCQYCMP 70 80 90 100 110 120 EEGVPLTPKA NLLTTEEILT LARLFVKEGI DKIRLTGGEP LIRPDVVDIV AQLQRLEGLR 130 140 150 160 170 180 TIGVTTNGIN LARLLPQLQK AGLSAINISL DTLVPAKFEF IVRRKGFHKV MEGIHKAIEL 190 200 210 220 230 240 GYNPVKVNCV VMRGLNEDEL LDFAALTEGL PLDVRFIEYM PFDGNKWNFK KMVSYKEMLD 250 260 270 280 290 300 TVRQQWPELE KVPEEESSTA KAFKIPGFQG QISFITSMSE HFCGTCNRLR ITADGNLKVC 310 320 330 340 350 LFGNSEVSLR DHLRAGASEQ ELLRIIGAAV GRKKRQHAGM FSISQMKNRP MILIGG
	Isoform 4 [UniParc]. Checksum: 0397D4D12A8C191B	FASTA	281	31,453
	10 20 30 40 50 60 MPEEGVPLTP KANLLTTEEI LTLARLFVKE GIDKIRLTGG EPLIRPDVVD IVAQLQRLEG 70 80 90 100 110 120 LRTIGVTTNG INLARLLPQL QKAGLSAINI SLDTLVPAKF EFIVRRKGFH KVMEGIHKAI 130 140 150 160 170 180 ELGYNPVKVN CVVMRGLNED ELLDFAALTE GLPLDVRFIE YMPFDGNKWN FKKMVSYKEM 190 200 210 220 230 240 LDTVRQQWPE LEKVPEEESS TAKAFKIPGF QGQISFITSM SEHFCGTCNR LRITADGNLK 250 260 270 280 VCLFGNSEVS LRDHLRAGAS EQELLRIIGA AVGRKKRQHA E
	Isoform 6 (MOCS1B Type-III) [UniParc]. Checksum: 23CB32E0E6F8535D	FASTA	620	68,257
	10 20 30 40 50 60 MAARPLSRML RRLLRSSARS CSSGAPVTQP CPGESARAAS EEVSRRRQFL REHAAPFSAF 70 80 90 100 110 120 LTDSFGRQHS YLRISLTEKC NLRCQYCMPE EGVPLTPKAN LLTTEEILTL ARLFVKEGID 130 140 150 160 170 180 KIRLTGGEPL IRPDVVDIVA QLQRLEGLRT IGVTTNGINL ARLLPQLQKA GLSAINISLD 190 200 210 220 230 240 TLVPAKFEFI VRRKGFHKVM EGIHKAIELG YNPVKVNCVV MRGLNEDELL DFAALTEGLP 250 260 270 280 290 300 LDVRFIEYMP FDGNKWNFKK MVSYKEMLDT VRQQWPELEK VPEEESSTAK AFKIPGFQGQ 310 320 330 340 350 360 ISFITSMSEH FCGTCNRLRI TADGNLKVCL FGNSEVSLRD HLRAGASEQE LLRIIGAAVG 370 380 390 400 410 420 RKKRQHAELF LMFPNSPPAN PSIFSWDPLH VQGLRPRMSF SSQVATLWKG CRVPQTPPLA 430 440 450 460 470 480 QQRLGSGSFQ RHYTSRADSD ANSKCLSPGS WASAAPSGPQ LTSEQLTHVD SEGRAAMVDV 490 500 510 520 530 540 GRKPDTERVA VASAVVLLGP VAFKLVQQNQ LKKGDALVVA QLAGVQAAKV TSQLIPLCHH 550 560 570 580 590 600 VALSHIQVQL ELDSTRHAVK IQASCRARGP TGVEMEALTS AAVAALTLYD MCKAVSRDIV 610 620 LEEIKLISKT GGQRGDFHRA
	Isoform 7 [UniParc]. Checksum: FBE48E29A35248D4	FASTA	533	58,455
	10 20 30 40 50 60 MPEEGVPLTP KANLLTTEEI LTLARLFVKE GIDKIRLTGG EPLIRPDVVD IVAQLQRLEG 70 80 90 100 110 120 LRTIGVTTNG INLARLLPQL QKAGLSAINI SLDTLVPAKF EFIVRRKGFH KVMEGIHKAI 130 140 150 160 170 180 ELGYNPVKVN CVVMRGLNED ELLDFAALTE GLPLDVRFIE YMPFDGNKWN FKKMVSYKEM 190 200 210 220 230 240 LDTVRQQWPE LEKVPEEESS TAKAFKIPGF QGQISFITSM SEHFCGTCNR LRITADGNLK 250 260 270 280 290 300 VCLFGNSEVS LRDHLRAGAS EQELLRIIGA AVGRKKRQHA ELFLMFPNSP PANPSIFSWD 310 320 330 340 350 360 PLHVQGLRPR MSFSSQVATL WKGCRVPQTP PLAQQRLGSG SFQRHYTSRA DSDANSKCLS 370 380 390 400 410 420 PGSWASAAPS GPQLTSEQLT HVDSEGRAAM VDVGRKPDTE RVAVASAVVL LGPVAFKLVQ 430 440 450 460 470 480 QNQLKKGDAL VVAQLAGVQA AKVTSQLIPL CHHVALSHIQ VQLELDSTRH AVKIQASCRA 490 500 510 520 530 RGPTGVEMEA LTSAAVAALT LYDMCKAVSR DIVLEEIKLI SKTGGQRGDF HRA
	Isoform 8 [UniParc]. Checksum: D78D063A89E6131D	FASTA	636	70,167
	10 20 30 40 50 60 MWKSWKLRTD VRVREGAGGS PCASSQPGSR GPCFLPGLSS QEVSRRRQFL REHAAPFSAF 70 80 90 100 110 120 LTDSFGRQHS YLRISLTEKC NLRCQYCMPE EGVPLTPKAN LLTTEEILTL ARLFVKEGID 130 140 150 160 170 180 KIRLTGGEPL IRPDVVDIVA QLQRLEGLRT IGVTTNGINL ARLLPQLQKA GLSAINISLD 190 200 210 220 230 240 TLVPAKFEFI VRRKGFHKVM EGIHKAIELG YNPVKVNCVV MRGLNEDELL DFAALTEGLP 250 260 270 280 290 300 LDVRFIEYMP FDGNKWNFKK MVSYKEMLDT VRQQWPELEK VPEEESSTAK AFKIPGFQGQ 310 320 330 340 350 360 ISFITSMSEH FCGTCNRLRI TADGNLKVCL FGNSEVSLRD HLRAGASEQE LLRIIGAAVG 370 380 390 400 410 420 RKKRQHAGMF SISQMKNRPM ILIELFLMFP NSPPANPSIF SWDPLHVQGL RPRMSFSSQV 430 440 450 460 470 480 ATLWKGCRVP QTPPLAQQRL GSGSFQRHYT SRADSDANSK CLSPGSWASA APSGPQLTSE 490 500 510 520 530 540 QLTHVDSEGR AAMVDVGRKP DTERVAVASA VVLLGPVAFK LVQQNQLKKG DALVVAQLAG 550 560 570 580 590 600 VQAAKVTSQL IPLCHHVALS HIQVQLELDS TRHAVKIQAS CRARGPTGVE MEALTSAAVA 610 620 630 ALTLYDMCKA VSRDIVLEEI KLISKTGGQR GDFHRA

References

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[1]	"Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency." Reiss J.P., Cohen N., Dorche C., Mandel H., Mendel R.R., Stallmeyer B., Zabot M.-T., Dierks T. Nat. Genet. 20:51-53(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS MOCS1A; 2 AND 8), INVOLVEMENT IN MOCOD TYPE A, TISSUE SPECIFICITY.
[2]	Larin D., Ross B.M., Gilliam T.C. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MOCS1A AND MOCS1B).
[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] (ISOFORMS MOCS1A AND 7). Tissue: Placenta.
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 4). Tissue: Colon and Kidney.
[6]	"Diverse splicing mechanisms fuse the evolutionarily conserved bicistronic MOCS1A and MOCS1B open reading frames." Gray T.A., Nicholls R.D. RNA 6:928-936(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 283-636 (ISOFORM 6), NUCLEOTIDE SEQUENCE [MRNA] OF 377-636 (ISOFORM MOCS1B).
[7]	"Identification of a human migration-inducing gene." Kim J.W. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 386-636.
[8]	"Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor biosynthesis." Haenzelmann P., Schwarz G., Mendel R.R. J. Biol. Chem. 277:18303-18312(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, ALTERNATIVE SPLICING (ISOFORMS MOCS1A AND MOCS1B).
[9]	"The bicistronic MOCS1 gene has alternative start codons on two mutually exclusive exons." Gross-Hardt S., Reiss J. Mol. Genet. Metab. 76:340-343(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS MOCS1A; 2 AND 3), TISSUE SPECIFICITY.
[10]	"Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis." Haenzelmann P., Hernandez H.L., Menzel C., Garcia-Serres R., Huynh B.H., Johnson M.K., Mendel R.R., Schindelin H. J. Biol. Chem. 279:34721-34732(2004) [PubMed] [Europe PMC] [Abstract] Cited for: COFACTOR, CHARACTERIZATION OF IRON-SULFUR CLUSTER-BINDING, MUTAGENESIS OF CYS-80; CYS-84; CYS-87; CYS-312; CYS-315 AND CYS-329.
[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-198, MASS SPECTROMETRY.
[12]	"Genomic structure and mutational spectrum of the bicistronic MOCS1 gene defective in molybdenum cofactor deficiency type A." Reiss J.P., Christensen E., Kurlemann G., Zabot M.-T., Dorche C. Hum. Genet. 103:639-644(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MOCOD TYPE A TRP-73; ASP-126; ASP-127; GLN-319 AND GLU-324.
[13]	"Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH." Reiss J., Johnson J.L. Hum. Mutat. 21:569-576(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MOCOD TYPE A TRP-123 AND ARG-324.
[14]	"Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation that abolishes the binding ability of molybdopterin synthase." Leimkuehler S., Charcosset M., Latour P., Dorche C., Kleppe S., Scaglia F., Szymczak I., Schupp P., Hahnewald R., Reiss J. Hum. Genet. 117:565-570(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MOCOD TYPE A TRP-67; GLY-80 AND PHE-84.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ224328 mRNA. Translation: CAA11897.1. AJ224328 mRNA. Translation: CAA11898.1. AJ404969 Genomic DNA. Translation: CAC44526.1. Sequence problems. AJ293577, AJ293578, AJ293579 Genomic DNA. Translation: CAC44527.1. AF034374 mRNA. Translation: AAB87523.1. AF034374 mRNA. Translation: AAB87524.1. Sequence problems. AK300300 mRNA. Translation: BAG62053.1. AK056740 mRNA. Translation: BAG51799.1. AL136089 Genomic DNA. Translation: CAI20007.1. Sequence problems. AL136089 Genomic DNA. Translation: CAI20011.1. AL136089 Genomic DNA. Translation: CAI20012.1. Sequence problems. AL136089 Genomic DNA. Translation: CAI20013.1. Sequence problems. AL136089 Genomic DNA. Translation: CAI20014.1. AL136089 Genomic DNA. Translation: CAI20015.1. BC036839 mRNA. Translation: AAH36839.1. AF214022 mRNA. Translation: AAF67857.1. AF214023 mRNA. Translation: AAF67858.1. AY423726 mRNA. Translation: AAS00489.1. Different initiation.
IPI	IPI00180672. IPI00289462. IPI00289463. IPI00413557. IPI00514315. IPI00746947. IPI00925345. IPI00926940.
RefSeq	NP_001068566.1. NM_001075098.3. NP_005934.2. NM_005943.5.
UniGene	Hs.718492.
3D structure databases
ProteinModelPortal	Q9NZB8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NZB8. 1 interaction.
PTM databases
PhosphoSite	Q9NZB8.
Polymorphism databases
DMDM	30913216.
Proteomic databases
PaxDb	Q9NZB8.
PRIDE	Q9NZB8.
Protocols and materials databases
DNASU	4337.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000308559; ENSP00000309843; ENSG00000124615. ENST00000340692; ENSP00000344794; ENSG00000124615. ENST00000373175; ENSP00000362270; ENSG00000124615. ENST00000373181; ENSP00000362277; ENSG00000124615. ENST00000373186; ENSP00000362282; ENSG00000124615. ENST00000373188; ENSP00000362284; ENSG00000124615. ENST00000373195; ENSP00000362291; ENSG00000124615. ENST00000425303; ENSP00000416478; ENSG00000124615. ENST00000432280; ENSP00000410809; ENSG00000124615.
GeneID	4337.
KEGG	hsa:4337.
UCSC	uc003opa.3. human. uc003opb.3. human. uc003opd.3. human. uc003ope.3. human.
Organism-specific databases
CTD	4337.
GeneCards	GC06M039920.
HGNC	HGNC:7190. MOCS1.
HPA	HPA045783.
MIM	252150. phenotype. 603707. gene.
neXtProt	NX_Q9NZB8.
Orphanet	99732. Sulfite oxidase deficiency due to molybdenum cofactor deficiency.
PharmGKB	PA30900.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2896.
InParanoid	Q9NZB8.
KO	K03639.
OMA	HRKFYYL.
OrthoDB	EOG4NP732.
PhylomeDB	Q9NZB8.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00344.
Gene expression databases
ArrayExpress	Q9NZB8.
Bgee	Q9NZB8.
CleanEx	HS_MOCS1.
Genevestigator	Q9NZB8.
GermOnline	ENSG00000124615. Homo sapiens.
Family and domain databases
Gene3D	3.20.20.70. 1 hit. 3.30.70.640. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR023045. Mo_CF_biosynth-C. IPR023046. Mo_CF_biosynth-C_bac. IPR013483. MoaA. IPR000385. MoaA_NifB_PqqE_Fe-S-bd_CS. IPR010505. Mob_synth_C. IPR002820. Mopterin_CF_biosynth-C_dom. IPR007197. rSAM. [Graphical view]
Pfam	PF01967. MoaC. 1 hit. PF06463. Mob_synth_C. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view]
SMART	SM00729. Elp3. 1 hit. [Graphical view]
SUPFAM	SSF55040. MoaC. 1 hit.
TIGRFAMs	TIGR02666. moaA. 1 hit. TIGR00581. moaC. 1 hit.
PROSITE	PS01305. MOAA_NIFB_PQQE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	4337.
NextBio	17062.
SOURCE	Search...

Entry information

Entry name

MOCS1_HUMAN

Accession

Primary (citable) accession number: Q9NZB8
Secondary accession number(s): B3KPT7 , B4DTP1, O14940, O14941, O75710, Q5J7W0, Q5TCE1, Q5TCE2, Q5TCE6, Q5TCE9, Q5TCF0, Q5TCF1, Q8N418, Q9NZB7, Q9UEM1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	May 16, 2003
Last modified:	May 1, 2013
This is version 112 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.