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Protein

NEDD4-binding protein 1

Gene

N4bp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inhibitor of the E3 ubiquitin-protein ligase ITCH. Acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates.1 Publication

GO - Molecular functioni

GO - Biological processi

  • cellular response to UV Source: BHF-UCL
  • negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • negative regulation of protein ubiquitination Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
NEDD4-binding protein 1
Short name:
N4BP1
Gene namesi
Name:N4bp1
Synonyms:Kiaa0615
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2136825. N4bp1.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: UniProtKB
  • nucleus Source: MGI
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 893893NEDD4-binding protein 1PRO_0000301985Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei241 – 2411PhosphothreonineBy similarity
Modified residuei257 – 2571PhosphoserineBy similarity
Modified residuei269 – 2691PhosphoserineCombined sources
Modified residuei299 – 2991PhosphoserineCombined sources
Modified residuei560 – 5601PhosphoserineCombined sources

Post-translational modificationi

Monoubiquitinated by NEDD4. Polyubiquitinated, leading to its degradation by the proteasome. Sumoylated with SUMO1, abrogating polyubiquitination and subsequent degradation. Desumoylated by SENP1, leading to accumulation in PML nuclear bodies.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6A037.
MaxQBiQ6A037.
PaxDbiQ6A037.
PeptideAtlasiQ6A037.
PRIDEiQ6A037.

PTM databases

iPTMnetiQ6A037.
PhosphoSiteiQ6A037.

Expressioni

Gene expression databases

BgeeiQ6A037.
CleanExiMM_N4BP1.
GenevisibleiQ6A037. MM.

Interactioni

Subunit structurei

Interacts with NEDD4. Interacts with ITCH (via WW domain 2).2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034074.

Structurei

3D structure databases

ProteinModelPortaliQ6A037.
SMRiQ6A037. Positions 614-772.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the N4BP1 family.Curated

Phylogenomic databases

eggNOGiKOG3777. Eukaryota.
ENOG410ZNK1. LUCA.
GeneTreeiENSGT00750000117218.
HOGENOMiHOG000113716.
HOVERGENiHBG059944.
InParanoidiQ6A037.
OMAiMARSHIQ.
OrthoDBiEOG7Q8CMR.
PhylomeDBiQ6A037.
TreeFamiTF315783.

Family and domain databases

InterProiIPR004088. KH_dom_type_1.
IPR021869. RNase_Zc3h12_NYN.
[Graphical view]
PfamiPF11977. RNase_Zc3h12a. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6A037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAARVVLDEF TAPAEKAALL ERSRGRIEAL FGVGLAVLGA LGAEEPLPAR
60 70 80 90 100
IWLQLRGAQE AVHSAKEYIK GICEPELEEK ECYPKAMHCI FVGAQSLFLK
110 120 130 140 150
SLIQDTCADL CVLDTGLLGI RGSAEAVVMA RSHIQQFVKL FESNENLPSN
160 170 180 190 200
QRESEIKREF RQFVEAHADS YTMDLLILPT SLKKELLSLT QGEESLFETD
210 220 230 240 250
DDVITVGDVR PPEYTQSAAT GPSSARDEVV VQEDSRNKAR TPVSELTKHM
260 270 280 290 300
DTVFSSSPDV LFVPVNGLSP DEDALSKDRV CHKRRSSDTE ERHTKKQFSL
310 320 330 340 350
ENVPEGELLP DGKGSAGNEV IDLSDPASNS TNLSPDGKDT TEEMEYNILV
360 370 380 390 400
NFFKTMGYSQ EIVEKVIREY GPSTEPLLLL EEIEKENKRL QEDRDFPPCT
410 420 430 440 450
VYPDASQSRN AGVGSTTNEL TADSTPKKAQ SHTEQSMVER FSQLPFKDSK
460 470 480 490 500
HCTSNCKVNS FRTVPVGQKQ EIWGSKQNSS CTVDLETDGH SASAASASPK
510 520 530 540 550
DISFVSRGAS GHQQRNPAFP ENGFQQQTEP LLPNNTKPAC EKRSGSCSSP
560 570 580 590 600
QPKPNYPPLS PPLPLPQLLP SVTEARLGGS SDHIDSSVTG VQRFRDTLKI
610 620 630 640 650
PYKLELKNEP GRADLKHIVI DGSNVAITHG LKKFFSCRGI AIAVEYFWKL
660 670 680 690 700
GNRNITVFVP QWRTRRDPNI TEQHFLTQLQ ELGILSLTPA RMVFGERIAS
710 720 730 740 750
HDDRFLLHLA DKTGGIIVTN DNFREFVTES VSWREIITKR LLQYTFVGDI
760 770 780 790 800
FMVPDDPLGR NGPRLEEFLR KEAFLRHMQP LLNALPSVGT FDPGFRSPST
810 820 830 840 850
QVANNSHQPP PRIQTSSSPW LPQQSHFTAL ATLPSMQQNP PLPAQRSSAE
860 870 880 890
TSELREALLK IFPDSEQKLK IDQILAAHPY MKDLNALSAL VLD
Length:893
Mass (Da):99,147
Last modified:September 11, 2007 - v2
Checksum:iAC6010E1F339B97A
GO

Sequence cautioni

The sequence BAD32259.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931G → E in BAE27970 (PubMed:16141072).Curated
Sequence conflicti671 – 6711T → P in BAE27970 (PubMed:16141072).Curated
Sequence conflicti724 – 7241R → T in BAE27970 (PubMed:16141072).Curated
Sequence conflicti733 – 7331W → C in BAE27970 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172981 mRNA. Translation: BAD32259.1. Different initiation.
AK134934 mRNA. Translation: BAE22344.1.
AK147522 mRNA. Translation: BAE27970.1.
AK170714 mRNA. Translation: BAE41972.1.
CCDSiCCDS52625.1.
RefSeqiNP_085040.2. NM_030563.2.
UniGeneiMm.25117.
Mm.428374.

Genome annotation databases

EnsembliENSMUST00000034074; ENSMUSP00000034074; ENSMUSG00000031652.
GeneIDi80750.
KEGGimmu:80750.
UCSCiuc009mqo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172981 mRNA. Translation: BAD32259.1. Different initiation.
AK134934 mRNA. Translation: BAE22344.1.
AK147522 mRNA. Translation: BAE27970.1.
AK170714 mRNA. Translation: BAE41972.1.
CCDSiCCDS52625.1.
RefSeqiNP_085040.2. NM_030563.2.
UniGeneiMm.25117.
Mm.428374.

3D structure databases

ProteinModelPortaliQ6A037.
SMRiQ6A037. Positions 614-772.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034074.

PTM databases

iPTMnetiQ6A037.
PhosphoSiteiQ6A037.

Proteomic databases

EPDiQ6A037.
MaxQBiQ6A037.
PaxDbiQ6A037.
PeptideAtlasiQ6A037.
PRIDEiQ6A037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034074; ENSMUSP00000034074; ENSMUSG00000031652.
GeneIDi80750.
KEGGimmu:80750.
UCSCiuc009mqo.2. mouse.

Organism-specific databases

CTDi9683.
MGIiMGI:2136825. N4bp1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3777. Eukaryota.
ENOG410ZNK1. LUCA.
GeneTreeiENSGT00750000117218.
HOGENOMiHOG000113716.
HOVERGENiHBG059944.
InParanoidiQ6A037.
OMAiMARSHIQ.
OrthoDBiEOG7Q8CMR.
PhylomeDBiQ6A037.
TreeFamiTF315783.

Miscellaneous databases

ChiTaRSiN4bp1. mouse.
PROiQ6A037.
SOURCEiSearch...

Gene expression databases

BgeeiQ6A037.
CleanExiMM_N4BP1.
GenevisibleiQ6A037. MM.

Family and domain databases

InterProiIPR004088. KH_dom_type_1.
IPR021869. RNase_Zc3h12_NYN.
[Graphical view]
PfamiPF11977. RNase_Zc3h12a. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreatic islet.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Olfactory bulb.
  3. "Identification of developmentally expressed proteins that functionally interact with Nedd4 ubiquitin ligase."
    Murillas R., Simms K.S., Hatakeyama S., Weissman A.M., Kuehn M.R.
    J. Biol. Chem. 277:2897-2907(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, UBIQUITINATION, INTERACTION WITH NEDD4.
  4. Cited for: FUNCTION, INTERACTION WITH ITCH.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; SER-299 AND SER-560, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Spleen and Testis.
  6. "N4BP1 is a newly identified nucleolar protein that undergoes SUMO-regulated polyubiquitylation and proteasomal turnover at promyelocytic leukemia nuclear bodies."
    Sharma P., Murillas R., Zhang H., Kuehn M.R.
    J. Cell Sci. 123:1227-1234(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, UBIQUITINATION, SUMOYLATION, DESUMOYLATION BY SENP1.

Entry informationi

Entry nameiN4BP1_MOUSE
AccessioniPrimary (citable) accession number: Q6A037
Secondary accession number(s): Q3TCI4, Q3UH87, Q3UY69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: July 6, 2016
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.