CPLM-017697

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-017697

UniProt Accession

FAD1_HUMAN; Q8NFF5; Q8N5J1; Q8N686; Q8WU93; Q8WUJ4; Q96CR8; Q99764; Q9HBN6

Genbank Protein ID

DQ458779; AF481877; AF520568; AF218022; AL451085; AL451085; AL451085; AL451085; CH471121; CH471121; CH471121; CH471121; BC011378; BC014012; BC020253; BC021096; BC032323; U79241

Genbank Nucleotide ID

ABE65383.1; AAO49318.1; AAM77338.1; AAG17264.1; CAI13259.1; CAI13260.1; CAI13261.1; CAI13262.1; EAW53154.1; EAW53155.1; EAW53158.1; EAW53159.1; AAH11378.1; AAH14012.2; AAH20253.1; AAH21096.2; AAH32323.1; AAB50199.1

Protein Name

FAD synthase

Protein Synonyms/Alias

FAD pyrophosphorylase; FMN adenylyltransferase; Flavin adenine dinucleotide synthase; Molybdenum cofactor biosynthesis protein-like region; FAD synthase region

Gene Name

FLAD1

Gene Synonyms/Alias

PP591

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
210	PKLEAATKALGGEGW	ubiquitination	[1]
219	LGGEGWEKLSLVPSS	ubiquitination	[1]

Reference

[1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]

Functional Description

Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.

Sequence Annotation

REGION 114 205 Molybdenum cofactor biosynthesis protein-
REGION 398 555 FAD synthase.
MOD_RES 106 106 Phosphoserine.
MOD_RES 563 563 Phosphoserine.

Keyword

Alternative splicing; ATP-binding; Complete proteome; FAD; FMN; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Reference proteome; Transferase.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

587 AA

Protein Sequence

MGWDLGTRLF QRQEQRSRLS RIWLEKTRVF LEGSTRTPAL PHCLFWLLQV PSTQDPLFPG 60
YGPQCPVDLA GPPCLRPLFG GLGGYWRALQ RGREGRTMTS RASELSPGRS VTAGIIIVGD 120
EILKGHTQDT NTFFLCRTLR SLGVQVCRVS VVPDEVATIA AEVTSFSNRF THVLTAGGIG 180
PTHDDVTFEA VAQAFGDELK PHPKLEAATK ALGGEGWEKL SLVPSSARLH YGTDPCTGQP 240
FRFPLVSVRN VYLFPGIPEL LRRVLEGMKG LFQNPAVQFH SKELYVAADE ASIAPILAEA 300
QAHFGRRLGL GSYPDWGSNY YQVKLTLDSE EEGPLEECLA YLTARLPQGS LVPYMPNAVE 360
QASEAVYKLA ESGSSLGKKV AGALQTIETS LAQYSLTQLC VGFNGGKDCT ALLHLFHAAV 420
QRKLPDVPNP LQILYIRSIS PFPELEQFLQ DTIKRYNLQM LEAEGSMKQA LGELQARHPQ 480
LEAVLMGTRR TDPYSCSLCP FSPTDPGWPA FMRINPLLDW TYRDIWDFLR QLFVPYCILY 540
DRGYTSLGSR ENTVRNPALK CLSPGGHPTY RPAYLLENEE EERNSRT 587

Gene Ontology

GO:0005829; C:cytosol; TAS:Reactome.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0003919; F:FMN adenylyltransferase activity; IEA:EC.
GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:InterPro.
GO:0006771; P:riboflavin metabolic process; TAS:Reactome.

Interpro

IPR012183; FAD_synth_Mopterin-bd.
IPR001453; Mopterin-bd_dom.
IPR002500; PAPS_reduct.
IPR014729; Rossmann-like_a/b/a_fold.

Pfam

PF00994; MoCF_biosynth
PF01507; PAPS_reduct

SMART

SM00852; MoCF_biosynth

PROSITE

PRINTS