Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

NEDD4 family-interacting protein 1 (Breast cancer-associated protein SGA-1M) (NEDD4 WW domain-binding protein 5) (Putative MAPK-activating protein PM13) (Putative NF-kappa-B-activating protein 164) (Putative NFKB and MAPK-activating protein)

 NFIP1_HUMAN             Reviewed;         221 AA.
Q9BT67; B2RDB8; D3DQF0; Q658T8; Q8N2E3; Q8N2F9;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 122.
RecName: Full=NEDD4 family-interacting protein 1;
AltName: Full=Breast cancer-associated protein SGA-1M;
AltName: Full=NEDD4 WW domain-binding protein 5;
AltName: Full=Putative MAPK-activating protein PM13;
AltName: Full=Putative NF-kappa-B-activating protein 164;
AltName: Full=Putative NFKB and MAPK-activating protein;
Name=NDFIP1; Synonyms=N4WBP5; ORFNames=PSEC0192, PSEC0223;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Petroziello J.M., Westendorf L.E., Gordon K.A., Yamane A.K.,
Cerveny C.G., Wahl A.F., Law C.L.;
"Array analysis of subtractive cDNA libraries identifies SGA-1M: a
novel breast cancer-associated gene.";
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung fibroblast;
PubMed=12761501; DOI=10.1038/sj.onc.1206406;
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
Sugano S.;
"Large-scale identification and characterization of human genes that
activate NF-kappaB and MAPK signaling pathways.";
Oncogene 22:3307-3318(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryo;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-221 (ISOFORM 1).
TISSUE=Stomach;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
TISSUE SPECIFICITY.
PubMed=11748237; DOI=10.1074/jbc.M110443200;
Harvey K.F., Shearwin-Whyatt L.M., Fotia A., Parton R.G., Kumar S.;
"N4WBP5, a potential target for ubiquitination by the Nedd4 family of
proteins, is a novel Golgi-associated protein.";
J. Biol. Chem. 277:9307-9317(2002).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH SLC11A2 AND WWP2.
PubMed=18776082; DOI=10.1182/blood-2008-04-150953;
Foot N.J., Dalton H.E., Shearwin-Whyatt L.M., Dorstyn L., Tan S.S.,
Yang B., Kumar S.;
"Regulation of the divalent metal ion transporter DMT1 and iron
homeostasis by a ubiquitin-dependent mechanism involving Ndfips and
WWP2.";
Blood 112:4268-4275(2008).
[10]
SUBCELLULAR LOCATION.
PubMed=18819914; DOI=10.1074/jbc.M804120200;
Putz U., Howitt J., Lackovic J., Foot N., Kumar S., Silke J.,
Tan S.S.;
"Nedd4 family-interacting protein 1 (Ndfip1) is required for the
exosomal secretion of Nedd4 family proteins.";
J. Biol. Chem. 283:32621-32627(2008).
[11]
FUNCTION, AND UBIQUITINATION.
PubMed=19343052; DOI=10.1038/embor.2009.30;
Mund T., Pelham H.R.;
"Control of the activity of WW-HECT domain E3 ubiquitin ligases by
NDFIP proteins.";
EMBO Rep. 10:501-507(2009).
[12]
FUNCTION, INTERACTION WITH SLC11A2 AND NEDD4L, AND INDUCTION BY COBALT
AND IRON.
PubMed=19706893; DOI=10.1073/pnas.0904880106;
Howitt J., Putz U., Lackovic J., Doan A., Dorstyn L., Cheng H.,
Yang B., Chan-Ling T., Silke J., Kumar S., Tan S.S.;
"Divalent metal transporter 1 (DMT1) regulation by Ndfip1 prevents
metal toxicity in human neurons.";
Proc. Natl. Acad. Sci. U.S.A. 106:15489-15494(2009).
[13]
FUNCTION, INTERACTION WITH NDFIP2; NEDD4 AND PTEN, SUBCELLULAR
LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF 41-PRO-TYR-42;
66-SER-TYR-67 AND 75-SER-TYR-76.
PubMed=20534535; DOI=10.1073/pnas.0911714107;
Mund T., Pelham H.R.;
"Regulation of PTEN/Akt and MAP kinase signaling pathways by the
ubiquitin ligase activators Ndfip1 and Ndfip2.";
Proc. Natl. Acad. Sci. U.S.A. 107:11429-11434(2010).
[14]
FUNCTION, AND INTERACTION WITH MAVS.
PubMed=23087404; DOI=10.4049/jimmunol.1201445;
Wang Y., Tong X., Ye X.;
"Ndfip1 negatively regulates RIG-I-dependent immune signaling by
enhancing E3 ligase Smurf1-mediated MAVS degradation.";
J. Immunol. 189:5304-5313(2012).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[16]
FUNCTION.
PubMed=26319551; DOI=10.1016/j.bbrc.2015.08.099;
Beck A., Shatz-Azoulay H., Vinik Y., Isaac R., Boura-Halfon S.,
Zick Y.;
"Nedd4 family interacting protein 1 (Ndfip1) promotes death of
pancreatic beta cells.";
Biochem. Biophys. Res. Commun. 465:851-856(2015).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KCNH2 AND NEDD4L.
PubMed=26363003; DOI=10.1042/BJ20141282;
Kang Y., Guo J., Yang T., Li W., Zhang S.;
"Regulation of the human ether-a-go-go-related gene (hERG) potassium
channel by Nedd4 family interacting proteins (Ndfips).";
Biochem. J. 472:71-82(2015).
[18]
FUNCTION, AND INTERACTION WITH BRAT1.
PubMed=25631046; DOI=10.1074/jbc.M114.613687;
Low L.H., Chow Y.L., Li Y., Goh C.P., Putz U., Silke J., Ouchi T.,
Howitt J., Tan S.S.;
"Nedd4 family interacting protein 1 (Ndfip1) is required for
ubiquitination and nuclear trafficking of BRCA1-associated ATM
activator 1 (BRAT1) during the DNA damage response.";
J. Biol. Chem. 290:7141-7150(2015).
[19]
INTERACTION WITH UBE2L3.
PubMed=25632008; DOI=10.4049/jimmunol.1402742;
Kathania M., Zeng M., Yadav V.N., Moghaddam S.J., Yang B.,
Venuprasad K.;
"Ndfip1 regulates itch ligase activity and airway inflammation via
UbcH7.";
J. Immunol. 194:2160-2167(2015).
[20]
FUNCTION, AND INTERACTION WITH PTEN.
PubMed=25801959; DOI=10.1093/jmcb/mjv020;
Howitt J., Low L.H., Putz U., Doan A., Lackovic J., Goh C.P.,
Gunnersen J., Silke J., Tan S.S.;
"Ndfip1 represses cell proliferation by controlling Pten localization
and signaling specificity.";
J. Mol. Cell Biol. 7:119-131(2015).
-!- FUNCTION: Activates HECT domain-containing E3 ubiquitin-protein
ligases, including NEDD4 and ITCH, and consequently modulates the
stability of their targets. As a result, controls many cellular
processes. Prevents chronic T-helper cell-mediated inflammation by
activating ITCH and thus controlling JUNB degradation (By
similarity). Promotes pancreatic beta cell death through
degradation of JUNB and inhibition of the unfolded protein
response, leading to reduction of insulin secretion
(PubMed:26319551). Restricts the production of proinflammatory
cytokines in effector Th17 T-cells by promoting ITCH-mediated
ubiquitination and degradation of RORC (By similarity). Together
with NDFIP2, limits the cytokine signaling and expansion of
effector Th2 T-cells by promoting degradation of JAK1, probably by
ITCH- and NEDD4L-mediated ubiquitination (By similarity).
Regulates peripheral T-cell tolerance to self and foreign
antigens, forcing the exit of naive CD4+ T-cells from the cell
cycle before they become effector T-cells (By similarity).
Negatively regulates RLR-mediated antiviral response by promoting
SMURF1-mediated ubiquitination and subsequent degradation of MAVS
(PubMed:23087404). Negatively regulates KCNH2 potassium channel
activity by decreasing its cell-surface expression and interfering
with channel maturation through recruitment of NEDD4L to the Golgi
apparatus where it mediates KCNH2 degradation (PubMed:26363003).
In cortical neurons, mediates the ubiquitination of the divalent
metal transporter SLC11A2/DMT1 by NEDD4L, leading to its down-
regulation and protection of the cells from cobalt and iron
toxicity (PubMed:19706893). Important for normal development of
dendrites and dendritic spines in cortex (By similarity). Enhances
the ubiquitination of BRAT1 mediated by: NEDD4, NEDD4L and ITCH
and is required for the nuclear localization of ubiquitinated
BRAT1 (PubMed:25631046). Enhances the ITCH-mediated ubiquitination
of MAP3K7 by recruiting E2 ubiquitin-conjugating enzyme UBE2L3 to
ITCH (By similarity). Modulates EGFR signaling through multiple
pathways. In particular, may regulate the ratio of AKT1-to-MAPK8
signaling in response to EGF, acting on AKT1 probably through PTEN
destabilization and on MAPK8 through ITCH-dependent MAP2K4
inactivation. As a result, may control cell growth rate
(PubMed:20534535). Inhibits cell proliferation by promoting PTEN
nuclear localization and changing its signaling specificity
(PubMed:25801959). {ECO:0000250|UniProtKB:Q8R0W6,
ECO:0000269|PubMed:19343052, ECO:0000269|PubMed:19706893,
ECO:0000269|PubMed:20534535, ECO:0000269|PubMed:23087404,
ECO:0000269|PubMed:25631046, ECO:0000269|PubMed:25801959,
ECO:0000269|PubMed:26319551, ECO:0000269|PubMed:26363003}.
-!- SUBUNIT: Forms heterodimers with NDFIP2 (PubMed:20534535).
Interacts with several E3 ubiquitin-protein ligases, including
ITCH, NEDD4, NEDD4L and WWP2 (PubMed:18776082, PubMed:19706893,
PubMed:26363003). The interaction with NEDD4, NEDD4L and ITCH
leads to relocalization of these proteins to exosomes and
eventually to exosomal secretion (By similarity). Interacts with
U2SURP (By similarity). Interacts with SLC11A2/DMT1
(PubMed:18776082, PubMed:19706893). Interacts with PTEN
(PubMed:20534535, PubMed:25801959). May interact with
phosphorylated EGFR (PubMed:20534535). Interacts with BRAT1
(PubMed:25631046). Interacts with KCNH2 (PubMed:26363003).
Interacts with MAVS (PubMed:23087404). Part of a complex
containing ITCH, NDFIP1 and MAP3K7 (By similarity). Interacts (via
N-terminus) with UBE2L3; the interaction mediates recruitment of
UBE2L3 to ITCH (PubMed:25632008). {ECO:0000250|UniProtKB:Q8R0W6,
ECO:0000269|PubMed:18776082, ECO:0000269|PubMed:19706893,
ECO:0000269|PubMed:20534535, ECO:0000269|PubMed:23087404,
ECO:0000269|PubMed:25631046, ECO:0000269|PubMed:25632008,
ECO:0000269|PubMed:25801959, ECO:0000269|PubMed:26363003}.
-!- INTERACTION:
P49281:SLC11A2; NbExp=2; IntAct=EBI-11732799, EBI-4319335;
-!- SUBCELLULAR LOCATION: Endosome membrane
{ECO:0000269|PubMed:20534535}; Multi-pass membrane protein
{ECO:0000269|PubMed:20534535}. Golgi apparatus membrane
{ECO:0000269|PubMed:26363003}. Cell junction, synapse, synaptosome
{ECO:0000250|UniProtKB:Q8R0W6}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q5U2S1}. Secreted
{ECO:0000269|PubMed:18819914}. Note=Detected in exosomes and
secreted via the exosomal pathway (PubMed:18819914).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BT67-1; Sequence=Displayed;
Name=2;
IsoId=Q9BT67-2; Sequence=VSP_016474, VSP_016475;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Higher levels are detected
in cerebellum, pituitary, thalamus, kidney, liver, testis,
salivary glands and placenta. Also expressed in fetal brain,
kidney and lung. {ECO:0000269|PubMed:11748237}.
-!- INDUCTION: Increased protein expression in neuronal cells in
response to Co(2+) or Fe(2+) ions. {ECO:0000269|PubMed:19706893}.
-!- DOMAIN: The PPxY motifs are required for E3 ubiquitin-protein
ligase binding and activation and for ubiquitination.
{ECO:0000269|PubMed:23087404}.
-!- PTM: Ubiquitinated by NEDD4 and ITCH; mono-, di- and
polyubiquitinated forms are detected. Ubiquitination regulates its
degradation. {ECO:0000269|PubMed:19343052}.
-!- PTM: Undergoes transient tyrosine phosphorylation following EGF
stimulation, most probably by catalyzed by SRC. Phosphorylation
SRC is enhanced in the presence of NDFIP2 which may act as a
scaffold to recruit SRC to NDFIP1. {ECO:0000269|PubMed:20534535}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AY192728; AAP13460.1; -; mRNA.
EMBL; AB097010; BAC77363.1; -; mRNA.
EMBL; AB097037; BAC77390.1; -; mRNA.
EMBL; AK075495; BAC11652.1; -; mRNA.
EMBL; AK075524; BAC11670.1; -; mRNA.
EMBL; AK315481; BAG37865.1; -; mRNA.
EMBL; CH471062; EAW61888.1; -; Genomic_DNA.
EMBL; CH471062; EAW61889.1; -; Genomic_DNA.
EMBL; BC004317; AAH04317.1; -; mRNA.
EMBL; AL832993; CAH56294.1; -; mRNA.
CCDS; CCDS4273.1; -. [Q9BT67-1]
RefSeq; NP_085048.1; NM_030571.3. [Q9BT67-1]
UniGene; Hs.653510; -.
UniGene; Hs.9788; -.
ProteinModelPortal; Q9BT67; -.
SMR; Q9BT67; -.
BioGrid; 123296; 55.
DIP; DIP-48958N; -.
IntAct; Q9BT67; 3.
MINT; Q9BT67; -.
STRING; 9606.ENSP00000253814; -.
iPTMnet; Q9BT67; -.
PhosphoSitePlus; Q9BT67; -.
SwissPalm; Q9BT67; -.
BioMuta; NDFIP1; -.
DMDM; 74733098; -.
EPD; Q9BT67; -.
MaxQB; Q9BT67; -.
PaxDb; Q9BT67; -.
PeptideAtlas; Q9BT67; -.
PRIDE; Q9BT67; -.
ProteomicsDB; 78953; -.
ProteomicsDB; 78954; -. [Q9BT67-2]
DNASU; 80762; -.
Ensembl; ENST00000253814; ENSP00000253814; ENSG00000131507. [Q9BT67-1]
GeneID; 80762; -.
KEGG; hsa:80762; -.
UCSC; uc003lmi.5; human. [Q9BT67-1]
CTD; 80762; -.
DisGeNET; 80762; -.
EuPathDB; HostDB:ENSG00000131507.10; -.
GeneCards; NDFIP1; -.
HGNC; HGNC:17592; NDFIP1.
HPA; HPA009682; -.
MIM; 612050; gene.
neXtProt; NX_Q9BT67; -.
OpenTargets; ENSG00000131507; -.
PharmGKB; PA134943402; -.
eggNOG; KOG4812; Eukaryota.
eggNOG; ENOG4111M6U; LUCA.
GeneTree; ENSGT00390000012721; -.
HOGENOM; HOG000038752; -.
HOVERGEN; HBG057103; -.
InParanoid; Q9BT67; -.
OMA; IPMQMQV; -.
OrthoDB; EOG091G0IMV; -.
PhylomeDB; Q9BT67; -.
TreeFam; TF324911; -.
ChiTaRS; NDFIP1; human.
GenomeRNAi; 80762; -.
PRO; PR:Q9BT67; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000131507; Expressed in 236 organ(s), highest expression level in primary visual cortex.
CleanEx; HS_NDFIP1; -.
Genevisible; Q9BT67; HS.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO; GO:0050699; F:WW domain binding; IBA:GO_Central.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
GO; GO:0030001; P:metal ion transport; IEA:InterPro.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0032713; P:negative regulation of interleukin-4 production; IEA:Ensembl.
GO; GO:0048294; P:negative regulation of isotype switching to IgE isotypes; IEA:Ensembl.
GO; GO:0051224; P:negative regulation of protein transport; IMP:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0032410; P:negative regulation of transporter activity; IMP:UniProtKB.
GO; GO:0002829; P:negative regulation of type 2 immune response; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0048302; P:regulation of isotype switching to IgG isotypes; IEA:Ensembl.
GO; GO:0045619; P:regulation of lymphocyte differentiation; IEA:Ensembl.
GO; GO:0002761; P:regulation of myeloid leukocyte differentiation; IEA:Ensembl.
GO; GO:0007034; P:vacuolar transport; IEA:InterPro.
InterPro; IPR019325; NEDD4/Bsd2.
PANTHER; PTHR13396; PTHR13396; 1.
Pfam; PF10176; DUF2370; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell junction; Cell projection;
Complete proteome; Endosome; Golgi apparatus; Membrane;
Reference proteome; Repeat; Secreted; Synapse; Synaptosome;
Transmembrane; Transmembrane helix; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 221 NEDD4 family-interacting protein 1.
/FTId=PRO_0000076269.
TOPO_DOM 2 116 Cytoplasmic. {ECO:0000255}.
TRANSMEM 117 137 Helical. {ECO:0000255}.
TOPO_DOM 138 143 Extracellular. {ECO:0000255}.
TRANSMEM 144 164 Helical. {ECO:0000255}.
TOPO_DOM 165 172 Cytoplasmic. {ECO:0000255}.
TRANSMEM 173 193 Helical. {ECO:0000255}.
TOPO_DOM 194 221 Extracellular. {ECO:0000255}.
REGION 2 41 Interaction with UBE2L3.
{ECO:0000250|UniProtKB:Q8R0W6}.
REGION 42 76 Interaction with ITCH.
{ECO:0000250|UniProtKB:Q8R0W6}.
MOTIF 39 42 PPxY motif 1.
MOTIF 64 67 PPxY motif 2.
MOTIF 74 76 PPxY motif 3.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
VAR_SEQ 76 153 YDEAERTKAEATIPLVPGRDEDFVGRDDFDDADQLRIGNDG
IFMLTFFMAFLFNWIGFFLSFCLTTSAAGRYGAISGF ->
CFYDISHLIFFIFYLRNMKKKYTKMVKLLHKSAPAQSDSCK
CPFICCVCISRISIGSRSGYQYIMHRSVGCLKAKQEN (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016474.
VAR_SEQ 154 221 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016475.
MUTAGEN 41 42 PY->AG: Loss of phosphorylation; when
associated with 66-S-Y-67 and 75-S-Y-76.
Greatly decreases NEDD4-binding; when
associated with 66-S-Y-67 and 75-S-Y-76.
No effect on PTEN-binding; when
associated with 66-S-Y-67 and 75-S-Y-76.
{ECO:0000269|PubMed:20534535}.
MUTAGEN 66 67 SY->AG: Loss of phosphorylation; when
associated with 41-P-Y-42 and 75-S-Y-76.
Greatly decreases NEDD4-binding; when
associated with 41-P-Y-42 and 75-S-Y-76.
No effect on PTEN-binding; when
associated with 41-P-Y-42 and 75-S-Y-76.
{ECO:0000269|PubMed:20534535}.
MUTAGEN 75 76 SY->AG: Loss of phosphorylation; when
associated with 41-P-Y-42 and 66-S-Y-67.
Greatly decreases NEDD4-binding; when
associated with 41-P-Y-42 and 66-S-Y-67.
No effect on PTEN-binding; when
associated with 41-P-Y-42 and 66-S-Y-67.
{ECO:0000269|PubMed:20534535}.
CONFLICT 20 20 Q -> W (in Ref. 4; BAC11670).
{ECO:0000305}.
CONFLICT 104 104 F -> L (in Ref. 4; BAC11670).
{ECO:0000305}.
SEQUENCE 221 AA; 24899 MW; 526A579D7B32FCA4 CRC64;
MALALAALAA VEPACGSRYQ QLQNEEESGE PEQAAGDAPP PYSSISAESA AYFDYKDESG
FPKPPSYNVA TTLPSYDEAE RTKAEATIPL VPGRDEDFVG RDDFDDADQL RIGNDGIFML
TFFMAFLFNW IGFFLSFCLT TSAAGRYGAI SGFGLSLIKW ILIVRFSTYF PGYFDGQYWL
WWVFLVLGFL LFLRGFINYA KVRKMPETFS NLPRTRVLFI Y


Related products :

Catalog number Product name Quantity
EIAAB27072 Breast cancer-associated protein SGA-1M,Homo sapiens,Human,N4WBP5,NDFIP1,NEDD4 family-interacting protein 1,NEDD4 WW domain-binding protein 5,PSEC0192,PSEC0223,Putative MAPK-activating protein PM13,Pu
EIAAB27073 Homo sapiens,Human,KIAA1165,N4WBP5A,NDFIP2,NEDD4 family-interacting protein 2,NEDD4 WW domain-binding protein 5A,Putative MAPK-activating protein PM04_PM05_PM06_PM07,Putative NF-kappa-B-activating pro
EIAAB42384 Homo sapiens,Human,Putative MAPK-activating protein PM14,Putative NF-kappa-B-activating protein 20,T2BP,TIFA,TRAF2-binding protein,TRAF-interacting protein with FHA domain-containing protein A
EIAAB10210 CXXC5,CXXC-type zinc finger protein 5,Homo sapiens,HSPC195,Human,Putative MAPK-activating protein PM08,Putative NF-kappa-B-activating protein 102,TCCCIA00297
18-461-10694 Protein GPR89A - Putative MAPK-activating protein PM01; Putative NF-kappa-B-activating protein 90 Polyclonal 0.05 ml
18-461-10696 Protein GPR89A - Putative MAPK-activating protein PM01; Putative NF-kappa-B-activating protein 90 Polyclonal 0.05 ml
18-461-10695 Protein GPR89A - Putative MAPK-activating protein PM01; Putative NF-kappa-B-activating protein 90 Polyclonal 0.05 ml
EIAAB05276 Apyrase homolog,CANT1,Homo sapiens,Human,Putative MAPK-activating protein PM09,Putative NF-kappa-B-activating protein 107,SCAN-1,SHAPY,Soluble calcium-activated nucleotidase 1
EIAAB36911 Adenosine 3'-phospho 5'-phosphosulfate transporter 1,Homo sapiens,Human,PAPS transporter 1,PAPST1,PSEC0149,Putative MAPK-activating protein PM15,Putative NF-kappa-B-activating protein 48,SLC35B2,Solut
EIAAB42479 Homo sapiens,Human,Putative MAPK-activating protein PM10,TIP,TIP41-like protein,TIPRL,Type 2A-interacting protein
EIAAB41046 C22orf5,Homo sapiens,Human,PSEC0108,Putative MAPK-activating protein FM08,TMEM184B,Transmembrane protein 184B
EIAAB45445 Homo sapiens,Human,MDS032,p31,Putative MAPK-activating protein PM26,USE1,USE1L,USE1-like protein,Vesicle transport protein USE1
EIAAB04912 C1orf144,Homo sapiens,Human,Putative MAPK-activating protein PM18_PM20_PM22,UPF0485 protein C1orf144
EIAAB13188 ER lumen protein retaining receptor 1,ERD2.1,Homo sapiens,Human,KDEL endoplasmic reticulum protein retention receptor 1,KDEL receptor 1,KDELR1,Putative MAPK-activating protein PM23
EIAAB43018 Endoplasmic reticulum stress-response protein 25,ERS25,ERS25,Homo sapiens,Human,Putative NF-kappa-B-activating protein 156,TMED4,Transmembrane emp24 domain-containing protein 4
EIAAB27071 Mouse,Mus musculus,N4wbp5,Ndfip1,NEDD4 family-interacting protein 1,NEDD4 WW domain-binding protein 5
EIAAB27074 Kiaa1165,Mouse,Mus musculus,N4wbp5A,Ndfip2,NEDD4 family-interacting protein 2,NEDD4 WW domain-binding protein 5A
EIAAB41676 Homo sapiens,Human,Proline-rich, vinculin and TIR domain-containing protein B,PRVTIRB,Putative NF-kappa-B-activating protein 502H,TICAM1,TICAM-1,TIR domain-containing adapter molecule 1,TIR domain-con
EIAAB45872 ECop,ECOP,EGFR-coamplified and overexpressed protein,GASP,Glioblastoma-amplified secreted protein,Homo sapiens,Human,Putative NF-kappa-B-activating protein 055N,Vesicular, overexpressed in cancer, pro
EIAAB41679 Homo sapiens,Human,Putative NF-kappa-B-activating protein 502,TICAM2,TICAM-2,TIR domain-containing adapter molecule 2,TIRAP3,TIRP,Toll_interleukin-1 receptor domain-containing protein,Toll-like recept
EIAAB42551 Homo sapiens,Human,Putative NF-kappa-B-activating protein 130,TMEM101,Transmembrane protein 101
EIAAB46376 C1orf139,EVI,GPR177,Homo sapiens,Human,Integral membrane protein GPR177,Protein evenness interrupted homolog,Protein wntless homolog,Putative NF-kappa-B-activating protein 373,UNQ85_PRO18667,WLS
18-661-15165 TRIF-related adapter molecule - TICAM2 protein; TIRAP3a; TIRAP3a short form; TIR-containing adapter molecule-2; TIR domain-containing adapter protein; Putative NFkB activating protein Polyclonal 0.1 mg
18-661-15184 TRIF-related adapter molecule - TICAM2 protein; TIRAP3a; TIRAP3a short form; TIR-containing adapter molecule-2; TIR domain-containing adapter protein; Putative NFkB activating protein Polyclonal 0.1 mg
EIAAB10055 CXorf42,Homo sapiens,Human,NF-kappa-B-activating protein pseudogene 1,NKAPP1,Putative uncharacterized protein CXorf42


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur