Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8N3X1

- FNBP4_HUMAN

UniProt

Q8N3X1 - FNBP4_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Formin-binding protein 4

Gene

FNBP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Enzyme and pathway databases

SignaLinkiQ8N3X1.

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-binding protein 4
Alternative name(s):
Formin-binding protein 30
Gene namesi
Name:FNBP4
Synonyms:FBP30, KIAA1014
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:19752. FNBP4.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: HPA
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

Orphaneti1106. Microphthalmia with limb anomalies.
PharmGKBiPA134971679.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10171017Formin-binding protein 4PRO_0000289863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Phosphoserine2 Publications
Modified residuei116 – 1161Phosphoserine2 Publications
Modified residuei172 – 1721Phosphothreonine1 Publication
Modified residuei290 – 2901N6-acetyllysineBy similarity
Modified residuei432 – 4321Phosphoserine5 Publications
Modified residuei435 – 4351Phosphoserine1 Publication
Modified residuei464 – 4641Phosphoserine1 Publication
Modified residuei479 – 4791Phosphothreonine1 Publication
Modified residuei499 – 4991Phosphoserine1 Publication
Modified residuei508 – 5081Phosphoserine3 Publications
Modified residuei963 – 9631Phosphoserine1 Publication
Modified residuei964 – 9641Phosphoserine1 Publication
Modified residuei965 – 9651Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8N3X1.
PaxDbiQ8N3X1.
PRIDEiQ8N3X1.

PTM databases

PhosphoSiteiQ8N3X1.

Miscellaneous databases

PMAP-CutDBQ8N3X1.

Expressioni

Gene expression databases

BgeeiQ8N3X1.
CleanExiHS_FNBP4.
ExpressionAtlasiQ8N3X1. baseline and differential.
GenevestigatoriQ8N3X1.

Organism-specific databases

HPAiHPA039485.
HPA040029.

Interactioni

Subunit structurei

Binds FMN1. Interacts with the Arg/Gly-rich-flanked Pro-rich of KHDRBS1/SAM68. Arginine methylation in these regions has no effect on this binding.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HTTP428586EBI-310600,EBI-466029

Protein-protein interaction databases

BioGridi116941. 13 interactions.
IntActiQ8N3X1. 4 interactions.
MINTiMINT-127221.
STRINGi9606.ENSP00000263773.

Structurei

3D structure databases

ProteinModelPortaliQ8N3X1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini214 – 24835WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini595 – 62935WW 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi630 – 6356Poly-Glu
Compositional biasi701 – 73131Pro-richAdd
BLAST
Compositional biasi905 – 92521Pro-richAdd
BLAST

Domaini

These WW domains interact with Arg/Gly-rich-flanked Pro-rich domains found in several WW domain-binding proteins (WBPs). The N-terminal WW domain has the greater ligand-binding ability (By similarity).By similarity

Sequence similaritiesi

Contains 2 WW domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG46362.
GeneTreeiENSGT00390000003450.
HOGENOMiHOG000168238.
HOVERGENiHBG066308.
InParanoidiQ8N3X1.
OMAiKMPPPEK.
OrthoDBiEOG75F4GV.
PhylomeDBiQ8N3X1.
TreeFamiTF331046.

Family and domain databases

InterProiIPR001202. WW_dom.
[Graphical view]
PfamiPF00397. WW. 2 hits.
[Graphical view]
SMARTiSM00456. WW. 2 hits.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 2 hits.
PROSITEiPS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8N3X1-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGKKSRAVPG RRPILQLSPP GPRGSTPGRD PEPEPDTEPD STAAVPSQPA
60 70 80 90 100
PSAATTTTTA VTAAAASDDS PSEDEQEAVQ EVPRVVQNPP KPVMTTRPTA
110 120 130 140 150
VKATGGLCLL GAYADSDDDD NDVSEKLAQS KETNGNQSTD IDSTLANFLA
160 170 180 190 200
EIDAITAPQP AAPVGASAPP PTPPRPEPKE AATSTLSSST SNGTDSTQTS
210 220 230 240 250
GWQYDTQCSL AGVGIEMGDW QEVWDENTGC YYYWNTQTNE VTWELPQYLA
260 270 280 290 300
TQVQGLQHYQ PSSVPGAETS FVVNTDIYSK EKTISVSSSK SGPVIAKREV
310 320 330 340 350
KKEVNEGIQA LSNSEEEKKG VAASLLAPLL PEGIKEEEER WRRKVICKEE
360 370 380 390 400
PVSEVKETST TVEEATTIVK PQEIMLDNIE DPSQEDLCSV VQSGESEEEE
410 420 430 440 450
EQDTLELELV LERKKAELRA LEEGDGSVSG SSPRSDISQP ASQDGMRRLM
460 470 480 490 500
SKRGKWKMFV RATSPESTSR SSSKTGRDTP ENGETAIGAE NSEKIDENSD
510 520 530 540 550
KEMEVEESPE KIKVQTTPKV EEEQDLKFQI GELANTLTSK FEFLGINRQS
560 570 580 590 600
ISNFHVLLLQ TETRIADWRE GALNGNYLKR KLQDAAEQLK QYEINATPKG
610 620 630 640 650
WSCHWDRDHR RYFYVNEQSG ESQWEFPDGE EEEEESQAQE NRDETLAKQT
660 670 680 690 700
LKDKTGTDSN STESSETSTG SLCKESFSGQ VSSSSLMPLT PFWTLLQSNV
710 720 730 740 750
PVLQPPLPLE MPPPPPPPPE SPPPPPPPPP PAEDGEIQEV EMEDEGSEEP
760 770 780 790 800
PAPGTEEDTP LKPSAQTTVV TSQSSVDSTI SSSSSTKGIK RKATEISTAV
810 820 830 840 850
VQRSATIGSS PVLYSQSAIA TGHQAAGIGN QATGIGHQTI PVSLPAAGMG
860 870 880 890 900
HQARGMSLQS NYLGLAAAPA IMSYAECSVP IGVTAPSLQP VQARGAVPTA
910 920 930 940 950
TIIEPPPPPP PPPPPPPPAP KMPPPEKTKK GRKDKAKKSK TKMPSLVKKW
960 970 980 990 1000
QSIQRELDEE DNSSSSEEDR ESTAQKRIEE WKQQQLVSGM AERNANFEAL
1010
PEDWRARLKR RKMAPNT
Length:1,017
Mass (Da):110,266
Last modified:November 30, 2010 - v3
Checksum:i510DC8011B5973AD
GO
Isoform 2 (identifier: Q8N3X1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     73-73: E → EGK

Show »
Length:1,019
Mass (Da):110,451
Checksum:i2D60B6B14CC4CE16
GO

Sequence cautioni

The sequence BAA76858.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 562Missing in BAA76858. (PubMed:10231032)Curated
Sequence conflicti55 – 562Missing in AAH37404. (PubMed:15489334)Curated
Sequence conflicti55 – 562Missing in CAB70761. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti125 – 1251E → G.
Corresponds to variant rs34962598 [ dbSNP | Ensembl ].
VAR_032623
Natural varianti794 – 7941T → A.
Corresponds to variant rs35040940 [ dbSNP | Ensembl ].
VAR_032624

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei73 – 731E → EGK in isoform 2. 1 PublicationVSP_040292

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB023231 mRNA. Translation: BAA76858.2. Different initiation.
AC021443 Genomic DNA. No translation available.
BC037404 mRNA. Translation: AAH37404.1.
AL137480 mRNA. Translation: CAB70761.1.
AK022987 mRNA. Translation: BAB14348.1.
CCDSiCCDS41644.1. [Q8N3X1-1]
PIRiT46422.
RefSeqiNP_056123.2. NM_015308.2. [Q8N3X1-1]
XP_005252890.1. XM_005252833.1. [Q8N3X1-2]
UniGeneiHs.6834.

Genome annotation databases

EnsembliENST00000263773; ENSP00000263773; ENSG00000109920. [Q8N3X1-1]
GeneIDi23360.
KEGGihsa:23360.
UCSCiuc001ngj.3. human. [Q8N3X1-1]

Polymorphism databases

DMDMi313104235.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB023231 mRNA. Translation: BAA76858.2 . Different initiation.
AC021443 Genomic DNA. No translation available.
BC037404 mRNA. Translation: AAH37404.1 .
AL137480 mRNA. Translation: CAB70761.1 .
AK022987 mRNA. Translation: BAB14348.1 .
CCDSi CCDS41644.1. [Q8N3X1-1 ]
PIRi T46422.
RefSeqi NP_056123.2. NM_015308.2. [Q8N3X1-1 ]
XP_005252890.1. XM_005252833.1. [Q8N3X1-2 ]
UniGenei Hs.6834.

3D structure databases

ProteinModelPortali Q8N3X1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116941. 13 interactions.
IntActi Q8N3X1. 4 interactions.
MINTi MINT-127221.
STRINGi 9606.ENSP00000263773.

PTM databases

PhosphoSitei Q8N3X1.

Polymorphism databases

DMDMi 313104235.

Proteomic databases

MaxQBi Q8N3X1.
PaxDbi Q8N3X1.
PRIDEi Q8N3X1.

Protocols and materials databases

DNASUi 23360.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263773 ; ENSP00000263773 ; ENSG00000109920 . [Q8N3X1-1 ]
GeneIDi 23360.
KEGGi hsa:23360.
UCSCi uc001ngj.3. human. [Q8N3X1-1 ]

Organism-specific databases

CTDi 23360.
GeneCardsi GC11M049910.
H-InvDB HIX0201592.
HGNCi HGNC:19752. FNBP4.
HPAi HPA039485.
HPA040029.
MIMi 615265. gene.
neXtProti NX_Q8N3X1.
Orphaneti 1106. Microphthalmia with limb anomalies.
PharmGKBi PA134971679.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46362.
GeneTreei ENSGT00390000003450.
HOGENOMi HOG000168238.
HOVERGENi HBG066308.
InParanoidi Q8N3X1.
OMAi KMPPPEK.
OrthoDBi EOG75F4GV.
PhylomeDBi Q8N3X1.
TreeFami TF331046.

Enzyme and pathway databases

SignaLinki Q8N3X1.

Miscellaneous databases

ChiTaRSi FNBP4. human.
GeneWikii FNBP4.
GenomeRNAii 23360.
NextBioi 45391.
PMAP-CutDB Q8N3X1.
PROi Q8N3X1.
SOURCEi Search...

Gene expression databases

Bgeei Q8N3X1.
CleanExi HS_FNBP4.
ExpressionAtlasi Q8N3X1. baseline and differential.
Genevestigatori Q8N3X1.

Family and domain databases

InterProi IPR001202. WW_dom.
[Graphical view ]
Pfami PF00397. WW. 2 hits.
[Graphical view ]
SMARTi SM00456. WW. 2 hits.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 2 hits.
PROSITEi PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Cervix.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1017 (ISOFORM 1).
    Tissue: Testis.
  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.
    , 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] OF 457-1017 (ISOFORMS 1/2).
  7. "Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains."
    Bedford M.T., Frankel A., Yaffe M.B., Clarke S., Leder P., Richard S.
    J. Biol. Chem. 275:16030-16036(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KHDRBS1.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-432; SER-963; SER-964 AND SER-965, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; SER-435; SER-499 AND SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-116; SER-432; SER-464; THR-479 AND SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFNBP4_HUMAN
AccessioniPrimary (citable) accession number: Q8N3X1
Secondary accession number(s): Q9H985, Q9NT81, Q9Y2L7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: November 30, 2010
Last modified: October 29, 2014
This is version 101 of the entry and version 3 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 11
    Human chromosome 11: 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

External Data

Dasty 3