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Protein

Adenosine monophosphate-protein transferase FICD

Gene

FICD

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

Functioni

Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. Able to inactivate Rho GTPases in vitro by adding AMP to RhoA, Rac and Cdc42. It is however unclear whether it inactivates GTPases in vivo and physiological substrates probably remain to be identified.2 Publications

Catalytic activityi

ATP + [protein] = diphosphate + [protein]-AMP.1 Publication

Enzyme regulationi

Adenylyltransferase activity is inhibited by the inhibitory helix present at the N-terminus: Glu-234 binds ATP and competes with ATP-binding at Arg-374, thereby preventing adenylyltransferase activity. Activation dissociates ATP-binding from Glu-234, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei234ATPCurated1
Binding sitei374ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi260 – 261ATPBy similarity2
Nucleotide bindingi368 – 370ATPBy similarity3

GO - Molecular functioni

GO - Biological processi

  • negative regulation of GTPase activity Source: UniProtKB
  • protein adenylylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:G66-30679-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosine monophosphate-protein transferase FICD (EC:2.7.7.n1)
Alternative name(s):
AMPylator FICD
FIC domain-containing protein
Huntingtin yeast partner E
Huntingtin-interacting protein 13
Short name:
HIP-13
Huntingtin-interacting protein E
Gene namesi
Name:FICD
Synonyms:HIP13, HYPE
ORF Names:UNQ3041/PRO9857
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:18416. FICD.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei24 – 44HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi234E → G: Promotes adenylyltransferase activity. 1 Publication1
Mutagenesisi363H → A: Abolishes adenylyltransferase. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000198855.
PharmGKBiPA162388517.

Polymorphism and mutation databases

BioMutaiFICD.
DMDMi74761284.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003173011 – 458Adenosine monophosphate-protein transferase FICDAdd BLAST458

Proteomic databases

PaxDbiQ9BVA6.
PeptideAtlasiQ9BVA6.
PRIDEiQ9BVA6.

PTM databases

iPTMnetiQ9BVA6.
PhosphoSitePlusiQ9BVA6.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000198855.
CleanExiHS_FICD.
ExpressionAtlasiQ9BVA6. baseline and differential.
GenevisibleiQ9BVA6. HS.

Organism-specific databases

HPAiHPA021390.

Interactioni

Subunit structurei

Interacts with HD.1 Publication

Protein-protein interaction databases

BioGridi116324. 2 interactors.
DIPiDIP-44884N.
IntActiQ9BVA6. 1 interactor.
MINTiMINT-1537734.
STRINGi9606.ENSP00000446479.

Structurei

Secondary structure

1458
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi108 – 119Combined sources12
Helixi122 – 135Combined sources14
Helixi140 – 151Combined sources12
Turni152 – 154Combined sources3
Helixi156 – 169Combined sources14
Helixi174 – 207Combined sources34
Helixi215 – 220Combined sources6
Helixi222 – 232Combined sources11
Turni233 – 235Combined sources3
Helixi240 – 249Combined sources10
Helixi258 – 277Combined sources20
Turni278 – 280Combined sources3
Helixi287 – 297Combined sources11
Turni299 – 301Combined sources3
Turni303 – 307Combined sources5
Helixi324 – 339Combined sources16
Helixi341 – 345Combined sources5
Helixi348 – 362Combined sources15
Beta strandi365 – 367Combined sources3
Helixi369 – 383Combined sources15
Helixi393 – 395Combined sources3
Helixi396 – 408Combined sources13
Helixi412 – 429Combined sources18
Helixi430 – 432Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4U04X-ray2.48A/B102-445[»]
4U07X-ray2.64A/B102-445[»]
4U0SX-ray2.49A/B102-445[»]
4U0UX-ray2.98A/B102-445[»]
4U0ZX-ray2.95A/B/C/D/E/F/G/H102-445[»]
ProteinModelPortaliQ9BVA6.
SMRiQ9BVA6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati106 – 139TPR 1Add BLAST34
Repeati140 – 173TPR 2Add BLAST34
Domaini285 – 420FidoPROSITE-ProRule annotationAdd BLAST136

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi230 – 235Inhibitory (S/T)XXXE(G/N) motif6

Domaini

The fido domain mediates the adenylyltransferase activity.

Sequence similaritiesi

Belongs to the fic family.Curated
Contains 1 fido domain.PROSITE-ProRule annotation
Contains 2 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3824. Eukaryota.
COG3177. LUCA.
GeneTreeiENSGT00390000008873.
HOGENOMiHOG000008059.
HOVERGENiHBG095654.
InParanoidiQ9BVA6.
OMAiNYAALAH.
OrthoDBiEOG091G0GN7.
PhylomeDBiQ9BVA6.
TreeFamiTF314692.

Family and domain databases

Gene3Di1.10.3290.10. 1 hit.
1.25.40.10. 1 hit.
InterProiIPR003812. Fido.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF02661. Fic. 1 hit.
[Graphical view]
SUPFAMiSSF140931. SSF140931. 1 hit.
SSF48452. SSF48452. 1 hit.
PROSITEiPS51459. FIDO. 1 hit.
PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BVA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLIPMASVM AVTEPKWVSV WSRFLWVTLL SMVLGSLLAL LLPLGAVEEQ
60 70 80 90 100
CLAVLKGLYL LRSKPDRAQH AATKCTSPST ELSITSRGAT LLVAKTKASP
110 120 130 140 150
AGKLEARAAL NQALEMKRQG KREKAQKLFM HALKMDPDFV DALTEFGIFS
160 170 180 190 200
EEDKDIIQAD YLYTRALTIS PYHEKALVNR DRTLPLVEEI DQRYFSIIDS
210 220 230 240 250
KVKKVMSIPK GNSALRRVME ETYYHHIYHT VAIEGNTLTL SEIRHILETR
260 270 280 290 300
YAVPGKSLEE QNEVIGMHAA MKYINTTLVS RIGSVTISDV LEIHRRVLGY
310 320 330 340 350
VDPVEAGRFR TTQVLVGHHI PPHPQDVEKQ MQEFVQWLNS EEAMNLHPVE
360 370 380 390 400
FAALAHYKLV YIHPFIDGNG RTSRLLMNLI LMQAGYPPIT IRKEQRSDYY
410 420 430 440 450
HVLEAANEGD VRPFIRFIAK CTETTLDTLL FATTEYSVAL PEAQPNHSGF

KETLPVKP
Length:458
Mass (Da):51,778
Last modified:July 5, 2004 - v2
Checksum:i8393EAA46D61C48E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358992 mRNA. Translation: AAQ89351.1.
CH471054 Genomic DNA. Translation: EAW97813.1.
BC001342 mRNA. Translation: AAH01342.2.
AF049611 mRNA. Translation: AAC26847.1.
CCDSiCCDS9116.1.
RefSeqiNP_009007.2. NM_007076.2.
UniGeneiHs.661891.

Genome annotation databases

EnsembliENST00000552695; ENSP00000446479; ENSG00000198855.
GeneIDi11153.
KEGGihsa:11153.
UCSCiuc001tmx.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358992 mRNA. Translation: AAQ89351.1.
CH471054 Genomic DNA. Translation: EAW97813.1.
BC001342 mRNA. Translation: AAH01342.2.
AF049611 mRNA. Translation: AAC26847.1.
CCDSiCCDS9116.1.
RefSeqiNP_009007.2. NM_007076.2.
UniGeneiHs.661891.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4U04X-ray2.48A/B102-445[»]
4U07X-ray2.64A/B102-445[»]
4U0SX-ray2.49A/B102-445[»]
4U0UX-ray2.98A/B102-445[»]
4U0ZX-ray2.95A/B/C/D/E/F/G/H102-445[»]
ProteinModelPortaliQ9BVA6.
SMRiQ9BVA6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116324. 2 interactors.
DIPiDIP-44884N.
IntActiQ9BVA6. 1 interactor.
MINTiMINT-1537734.
STRINGi9606.ENSP00000446479.

PTM databases

iPTMnetiQ9BVA6.
PhosphoSitePlusiQ9BVA6.

Polymorphism and mutation databases

BioMutaiFICD.
DMDMi74761284.

Proteomic databases

PaxDbiQ9BVA6.
PeptideAtlasiQ9BVA6.
PRIDEiQ9BVA6.

Protocols and materials databases

DNASUi11153.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000552695; ENSP00000446479; ENSG00000198855.
GeneIDi11153.
KEGGihsa:11153.
UCSCiuc001tmx.2. human.

Organism-specific databases

CTDi11153.
GeneCardsiFICD.
H-InvDBHIX0010965.
HGNCiHGNC:18416. FICD.
HPAiHPA021390.
neXtProtiNX_Q9BVA6.
OpenTargetsiENSG00000198855.
PharmGKBiPA162388517.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3824. Eukaryota.
COG3177. LUCA.
GeneTreeiENSGT00390000008873.
HOGENOMiHOG000008059.
HOVERGENiHBG095654.
InParanoidiQ9BVA6.
OMAiNYAALAH.
OrthoDBiEOG091G0GN7.
PhylomeDBiQ9BVA6.
TreeFamiTF314692.

Enzyme and pathway databases

BioCyciZFISH:G66-30679-MONOMER.

Miscellaneous databases

GenomeRNAii11153.
PROiQ9BVA6.

Gene expression databases

BgeeiENSG00000198855.
CleanExiHS_FICD.
ExpressionAtlasiQ9BVA6. baseline and differential.
GenevisibleiQ9BVA6. HS.

Family and domain databases

Gene3Di1.10.3290.10. 1 hit.
1.25.40.10. 1 hit.
InterProiIPR003812. Fido.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF02661. Fic. 1 hit.
[Graphical view]
SUPFAMiSSF140931. SSF140931. 1 hit.
SSF48452. SSF48452. 1 hit.
PROSITEiPS51459. FIDO. 1 hit.
PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFICD_HUMAN
AccessioniPrimary (citable) accession number: Q9BVA6
Secondary accession number(s): O75406
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 125 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.