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Protein

Guanylate-binding protein 4

Gene

GBP4

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

Functioni

Binds GTP, GDP and GMP. Hydrolyzes GTP very efficiently; GDP rather than GMP is the major reaction product. Plays a role in erythroid differentiation (By similarity).By similarity

Catalytic activityi

GTP + H2O = GDP + phosphate.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi60 – 678GTPBy similarity
Nucleotide bindingi82 – 843GTPBy similarity
Nucleotide bindingi112 – 1165GTPBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-877300. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate-binding protein 4 (EC:3.6.5.-By similarity)
Alternative name(s):
GTP-binding protein 4
Short name:
GBP-4
Guanine nucleotide-binding protein 4
Gene namesi
Name:GBP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:20480. GBP4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134959399.

Polymorphism and mutation databases

BioMutaiGBP4.
DMDMi116242487.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 640640Guanylate-binding protein 4PRO_0000190968Add
BLAST

Proteomic databases

MaxQBiQ96PP9.
PaxDbiQ96PP9.
PeptideAtlasiQ96PP9.
PRIDEiQ96PP9.

PTM databases

iPTMnetiQ96PP9.
PhosphoSiteiQ96PP9.

Expressioni

Inductioni

By IFNG during macrophage activation.1 Publication

Gene expression databases

BgeeiQ96PP9.
CleanExiHS_GBP4.
GenevisibleiQ96PP9. HS.

Organism-specific databases

HPAiHPA030101.

Interactioni

Subunit structurei

Heterodimer with other family members, including GBP1, GBP2 and GBP5 (PubMed:21151871). Dimerization regulates subcellular location.1 Publication

Protein-protein interaction databases

STRINGi9606.ENSP00000359490.

Structurei

3D structure databases

ProteinModelPortaliQ96PP9.
SMRiQ96PP9. Positions 18-597.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 292243GB1/RHD3-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 325325GTPase domain (Globular)By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili499 – 612114Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi53 – 564Poly-Val

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
GeneTreeiENSGT00550000074475.
HOGENOMiHOG000266974.
HOVERGENiHBG001979.
InParanoidiQ96PP9.
OMAiQEYMAQM.
OrthoDBiEOG7BW0J3.
PhylomeDBiQ96PP9.
TreeFamiTF331602.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030386. G_GB1_RHD3_dom.
IPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02263. GBP. 1 hit.
PF02841. GBP_C. 1 hit.
[Graphical view]
SUPFAMiSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96PP9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGERTLHAAV PTPGYPESES IMMAPICLVE NQEEQLTVNS KALEILDKIS
60 70 80 90 100
QPVVVVAIVG LYRTGKSYLM NRLAGKRNGF PLGSTVQSET KGIWMWCVPH
110 120 130 140 150
LSKPNHTLVL LDTEGLGDVE KSNPKNDSWI FALAVLLSSS FVYNSVSTIN
160 170 180 190 200
HQALEQLHYV TELAELIRAK SCPRPDEAED SSEFASFFPD FIWTVRDFTL
210 220 230 240 250
ELKLDGNPIT EDEYLENALK LIPGKNPKIQ NSNMPRECIR HFFRKRKCFV
260 270 280 290 300
FDRPTNDKQY LNHMDEVPEE NLERHFLMQS DNFCSYIFTH AKTKTLREGI
310 320 330 340 350
IVTGKRLGTL VVTYVDAINS GAVPCLENAV TALAQLENPA AVQRAADHYS
360 370 380 390 400
QQMAQQLRLP TDTLQELLDV HAACEREAIA VFMEHSFKDE NHEFQKKLVD
410 420 430 440 450
TIEKKKGDFV LQNEEASAKY CQAELKRLSE HLTESILRGI FSVPGGHNLY
460 470 480 490 500
LEEKKQVEWD YKLVPRKGVK ANEVLQNFLQ SQVVVEESIL QSDKALTAGE
510 520 530 540 550
KAIAAERAMK EAAEKEQELL REKQKEQQQM MEAQERSFQE YMAQMEKKLE
560 570 580 590 600
EERENLLREH ERLLKHKLKV QEEMLKEEFQ KKSEQLNKEI NQLKEKIEST
610 620 630 640
KNEQLRLLKI LDMASNIMIV TLPGASKLLG VGTKYLGSRI
Length:640
Mass (Da):73,165
Last modified:October 17, 2006 - v2
Checksum:i06ABFF47E615DAFC
GO

Sequence cautioni

The sequence BAC85144.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti298 – 2981E → K in AAH70055 (PubMed:15489334).Curated
Sequence conflicti402 – 4109IEKKKGDFV → KKKKKKKKK in AAH17889 (PubMed:15489334).Curated
Sequence conflicti416 – 4161A → P in BAG35327 (PubMed:14702039).Curated
Sequence conflicti502 – 5021A → S in AAH70055 (PubMed:15489334).Curated
Sequence conflicti541 – 5422YM → NI in AAL02054 (Ref. 1) Curated
Sequence conflicti541 – 5422YM → NI in BAC85144 (PubMed:12693554).Curated
Sequence conflicti545 – 5462ME → LK in AAL02054 (Ref. 1) Curated
Sequence conflicti545 – 5462ME → LK in BAC85144 (PubMed:12693554).Curated
Sequence conflicti549 – 5513LEE → MER in AAL02054 (Ref. 1) Curated
Sequence conflicti549 – 5513LEE → MER in BAC85144 (PubMed:12693554).Curated
Sequence conflicti582 – 5821K → R in BAG35327 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti125 – 1251K → E.
Corresponds to variant rs17130745 [ dbSNP | Ensembl ].
VAR_028283
Natural varianti379 – 3791I → V.
Corresponds to variant rs1831240 [ dbSNP | Ensembl ].
VAR_028284
Natural varianti541 – 5411Y → N.
Corresponds to variant rs655260 [ dbSNP | Ensembl ].
VAR_028285
Natural varianti542 – 5421M → I.
Corresponds to variant rs1142886 [ dbSNP | Ensembl ].
VAR_033952
Natural varianti545 – 5451M → I.
Corresponds to variant rs1142889 [ dbSNP | Ensembl ].
VAR_033953
Natural varianti545 – 5451M → L.
Corresponds to variant rs1142888 [ dbSNP | Ensembl ].
VAR_033954
Natural varianti546 – 5461E → K.
Corresponds to variant rs1142890 [ dbSNP | Ensembl ].
VAR_033955
Natural varianti549 – 5491L → M.
Corresponds to variant rs608339 [ dbSNP | Ensembl ].
VAR_028286
Natural varianti551 – 5511E → G.
Corresponds to variant rs561042 [ dbSNP | Ensembl ].
VAR_028288
Natural varianti551 – 5511E → K.
Corresponds to variant rs561037 [ dbSNP | Ensembl ].
VAR_028287

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF288814 mRNA. Translation: AAL02054.1.
AL832576 mRNA. Translation: CAD89936.1.
AK131094 mRNA. Translation: BAC85144.1. Different initiation.
AK312417 mRNA. Translation: BAG35327.1.
BC017889 mRNA. Translation: AAH17889.1.
BC070055 mRNA. Translation: AAH70055.1.
CCDSiCCDS721.1.
RefSeqiNP_443173.2. NM_052941.4.
UniGeneiHs.409925.

Genome annotation databases

EnsembliENST00000355754; ENSP00000359490; ENSG00000162654.
GeneIDi115361.
KEGGihsa:115361.
UCSCiuc001dnb.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF288814 mRNA. Translation: AAL02054.1.
AL832576 mRNA. Translation: CAD89936.1.
AK131094 mRNA. Translation: BAC85144.1. Different initiation.
AK312417 mRNA. Translation: BAG35327.1.
BC017889 mRNA. Translation: AAH17889.1.
BC070055 mRNA. Translation: AAH70055.1.
CCDSiCCDS721.1.
RefSeqiNP_443173.2. NM_052941.4.
UniGeneiHs.409925.

3D structure databases

ProteinModelPortaliQ96PP9.
SMRiQ96PP9. Positions 18-597.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000359490.

PTM databases

iPTMnetiQ96PP9.
PhosphoSiteiQ96PP9.

Polymorphism and mutation databases

BioMutaiGBP4.
DMDMi116242487.

Proteomic databases

MaxQBiQ96PP9.
PaxDbiQ96PP9.
PeptideAtlasiQ96PP9.
PRIDEiQ96PP9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355754; ENSP00000359490; ENSG00000162654.
GeneIDi115361.
KEGGihsa:115361.
UCSCiuc001dnb.4. human.

Organism-specific databases

CTDi115361.
GeneCardsiGBP4.
HGNCiHGNC:20480. GBP4.
HPAiHPA030101.
MIMi612466. gene.
neXtProtiNX_Q96PP9.
PharmGKBiPA134959399.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
GeneTreeiENSGT00550000074475.
HOGENOMiHOG000266974.
HOVERGENiHBG001979.
InParanoidiQ96PP9.
OMAiQEYMAQM.
OrthoDBiEOG7BW0J3.
PhylomeDBiQ96PP9.
TreeFamiTF331602.

Enzyme and pathway databases

ReactomeiR-HSA-877300. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSiGBP4. human.
GenomeRNAii115361.
PROiQ96PP9.
SOURCEiSearch...

Gene expression databases

BgeeiQ96PP9.
CleanExiHS_GBP4.
GenevisibleiQ96PP9. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030386. G_GB1_RHD3_dom.
IPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02263. GBP. 1 hit.
PF02841. GBP_C. 1 hit.
[Graphical view]
SUPFAMiSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human GBP-4 and -5: new members of the IFN-gamma-inducible guanylate binding protein family."
    Avdalovic A., Fu H., Tsurushita N.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spinal cord.
  3. "Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones."
    Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O.
    DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spleen.
  4. "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].
    Tissue: Brain.
  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].
    Tissue: Placenta and Testis.
  6. "Unique features of different members of the human guanylate-binding protein family."
    Tripal P., Bauer M., Naschberger E., Mortinger T., Hohenadl C., Cornali E., Thurau M., Sturzl M.
    J. Interferon Cytokine Res. 27:44-52(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION.
  7. "Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner."
    Britzen-Laurent N., Bauer M., Berton V., Fischer N., Syguda A., Reipschlager S., Naschberger E., Herrmann C., Sturzl M.
    PLoS ONE 5:E14246-E14246(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DIMERIZATION.

Entry informationi

Entry nameiGBP4_HUMAN
AccessioniPrimary (citable) accession number: Q96PP9
Secondary accession number(s): B2R630
, Q05D63, Q6NSL0, Q86T99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: October 17, 2006
Last modified: June 8, 2016
This is version 119 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 1
    Human chromosome 1: 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

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.