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Protein

Zinc finger CCCH domain-containing protein 7B

Gene

ZC3H7B

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

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri500 – 52425C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri632 – 65423C3H1-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri770 – 79829C3H1-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri858 – 88225C2H2-typeAdd
BLAST
Zinc fingeri902 – 93029C3H1-type 4PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger CCCH domain-containing protein 7B
Alternative name(s):
Rotavirus 'X'-associated non-structural protein
Short name:
RoXaN
Gene namesi
Name:ZC3H7B
Synonyms:KIAA1031
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:30869. ZC3H7B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi257 – 2593DSS → AAA: Almost no effect on NSP3 binding. 1 Publication
Mutagenesisi268 – 2703LDD → AAA: Complete loss of NSP3 binding. 1 Publication

Organism-specific databases

PharmGKBiPA142670533.

Polymorphism and mutation databases

DMDMi20455239.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 993993Zinc finger CCCH domain-containing protein 7BPRO_0000106322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei233 – 2331PhosphoserineCombined sources
Modified residuei380 – 3801PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UGR2.
MaxQBiQ9UGR2.
PaxDbiQ9UGR2.
PRIDEiQ9UGR2.

PTM databases

iPTMnetiQ9UGR2.
PhosphoSiteiQ9UGR2.

Expressioni

Gene expression databases

BgeeiQ9UGR2.
CleanExiHS_ZC3H7B.
GenevisibleiQ9UGR2. HS.

Organism-specific databases

HPAiHPA001784.

Interactioni

Subunit structurei

Interacts (via LD motif) with rotavirus A NSP3 (via the coiled-coil region).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q007216EBI-948845,EBI-1263962From a different organism.

Protein-protein interaction databases

BioGridi116866. 9 interactions.
IntActiQ9UGR2. 8 interactions.
MINTiMINT-4992901.
STRINGi9606.ENSP00000263243.

Structurei

3D structure databases

ProteinModelPortaliQ9UGR2.
SMRiQ9UGR2. Positions 33-182, 896-949.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati36 – 6934TPR 1Add
BLAST
Repeati82 – 11534TPR 2Add
BLAST
Repeati116 – 14934TPR 3Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili922 – 95635Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi264 – 2729LD motif; interaction with NSP3

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi982 – 9898Poly-Ala

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.Curated
Contains 4 C3H1-type zinc fingers.PROSITE-ProRule annotation
Contains 3 TPR repeats.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri500 – 52425C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri632 – 65423C3H1-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri770 – 79829C3H1-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri858 – 88225C2H2-typeAdd
BLAST
Zinc fingeri902 – 93029C3H1-type 4PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, TPR repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IN1T. Eukaryota.
ENOG410YBKB. LUCA.
GeneTreeiENSGT00390000018542.
HOVERGENiHBG058699.
InParanoidiQ9UGR2.
OMAiDIETDCY.
OrthoDBiEOG7GBFW5.
PhylomeDBiQ9UGR2.
TreeFamiTF329017.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
4.10.1000.10. 3 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF13181. TPR_8. 1 hit.
PF00642. zf-CCCH. 2 hits.
[Graphical view]
SMARTiSM00028. TPR. 2 hits.
SM00356. ZnF_C3H1. 4 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF90229. SSF90229. 2 hits.
PROSITEiPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
PS50103. ZF_C3H1. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UGR2-1) [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
MERQKRKADI EKGLQFIQST LPLKQEEYEA FLLKLVQNLF AEGNDLFREK
60 70 80 90 100
DYKQALVQYM EGLNVADYAA SDQVALPREL LCKLHVNRAA CYFTMGLYEK
110 120 130 140 150
ALEDSEKALG LDSESIRALF RKARALNELG RHKEAYECSS RCSLALPHDE
160 170 180 190 200
SVTQLGQELA QKLGLRVRKA YKRPQELETF SLLSNGTAAG VADQGTSNGL
210 220 230 240 250
GSIDDIETGN VPDTREQVEI GAPRDCYVDP RGSPALLPST PTMPLFPHVL
260 270 280 290 300
DLLAPLDSSR TLPSTDSLDD FSDGDVFGPE LDTLLDSLSL VQGGLSGSGV
310 320 330 340 350
PSELPQLIPV FPGGTPLLPP VVGGSIPVSS PLPPASFGLV MDPSKKLAAS
360 370 380 390 400
VLDALDPPGP TLDPLDLLPY SETRLDALDS FGSTRGSLDK PDSFMEETNS
410 420 430 440 450
QDHRPPSGAQ KPAPSPEPCM PNTALLIKNP LAATHEFKQA CQLCYPKTGP
460 470 480 490 500
RAGDYTYREG LEHKCKRDIL LGRLRSSEDQ TWKRIRPRPT KTSFVGSYYL
510 520 530 540 550
CKDMINKQDC KYGDNCTFAY HQEEIDVWTE ERKGTLNRDL LFDPLGGVKR
560 570 580 590 600
GSLTIAKLLK EHQGIFTFLC EICFDSKPRI ISKGTKDSPS VCSNLAAKHS
610 620 630 640 650
FYNNKCLVHI VRSTSLKYSK IRQFQEHFQF DVCRHEVRYG CLREDSCHFA
660 670 680 690 700
HSFIELKVWL LQQYSGMTHE DIVQESKKYW QQMEAHAGKA SSSMGAPRTH
710 720 730 740 750
GPSTFDLQMK FVCGQCWRNG QVVEPDKDLK YCSAKARHCW TKERRVLLVM
760 770 780 790 800
SKAKRKWVSV RPLPSIRNFP QQYDLCIHAQ NGRKCQYVGN CSFAHSPEER
810 820 830 840 850
DMWTFMKENK ILDMQQTYDM WLKKHNPGKP GEGTPISSRE GEKQIQMPTD
860 870 880 890 900
YADIMMGYHC WLCGKNSNSK KQWQQHIQSE KHKEKVFTSD SDASGWAFRF
910 920 930 940 950
PMGEFRLCDR LQKGKACPDG DKCRCAHGQE ELNEWLDRRE VLKQKLAKAR
960 970 980 990
KDMLLCPRDD DFGKYNFLLQ EDGDLAGATP EAPAAAATAT TGE
Note: No experimental confirmation available.
Length:993
Mass (Da):111,578
Last modified:May 1, 2000 - v1
Checksum:iB81E9E67772FFE1B
GO
Isoform 2 (identifier: Q9UGR2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-224: Missing.

Show »
Length:977
Mass (Da):109,858
Checksum:iBE3F8AEEC89D096D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 392NL → LE in BAA82983 (PubMed:10470851).Curated
Sequence conflicti88 – 881R → K in AAF05541 (Ref. 4) Curated
Sequence conflicti232 – 2321G → A in AAF05541 (Ref. 4) Curated
Sequence conflicti247 – 2471P → T in AAI52559 (PubMed:15489334).Curated
Sequence conflicti386 – 3861G → V in AAF05541 (Ref. 4) Curated
Sequence conflicti406 – 4061P → T in AAI52559 (PubMed:15489334).Curated
Sequence conflicti676 – 6761S → F in AAF05541 (Ref. 4) Curated
Sequence conflicti918 – 9181P → L in AAI52559 (PubMed:15489334).Curated
Sequence conflicti971 – 9711E → G in BAG37501 (PubMed:14702039).Curated
Sequence conflicti971 – 9711E → G in AAI52559 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti379 – 3791D → N.
Corresponds to variant rs9607793 [ dbSNP | Ensembl ].
VAR_054313

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei209 – 22416Missing in isoform 2. 4 PublicationsVSP_006552Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK315009 mRNA. Translation: BAG37501.1.
AL035659 Genomic DNA. Translation: CAI23515.1.
BC024313 mRNA. Translation: AAH24313.2.
BC152558 mRNA. Translation: AAI52559.1.
AF188530 mRNA. Translation: AAF05541.1.
AB028954 mRNA. Translation: BAA82983.1.
CCDSiCCDS14013.1. [Q9UGR2-2]
RefSeqiNP_060060.3. NM_017590.5. [Q9UGR2-2]
UniGeneiHs.592188.

Genome annotation databases

EnsembliENST00000352645; ENSP00000345793; ENSG00000100403. [Q9UGR2-2]
GeneIDi23264.
KEGGihsa:23264.
UCSCiuc003azw.5. human. [Q9UGR2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK315009 mRNA. Translation: BAG37501.1.
AL035659 Genomic DNA. Translation: CAI23515.1.
BC024313 mRNA. Translation: AAH24313.2.
BC152558 mRNA. Translation: AAI52559.1.
AF188530 mRNA. Translation: AAF05541.1.
AB028954 mRNA. Translation: BAA82983.1.
CCDSiCCDS14013.1. [Q9UGR2-2]
RefSeqiNP_060060.3. NM_017590.5. [Q9UGR2-2]
UniGeneiHs.592188.

3D structure databases

ProteinModelPortaliQ9UGR2.
SMRiQ9UGR2. Positions 33-182, 896-949.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116866. 9 interactions.
IntActiQ9UGR2. 8 interactions.
MINTiMINT-4992901.
STRINGi9606.ENSP00000263243.

PTM databases

iPTMnetiQ9UGR2.
PhosphoSiteiQ9UGR2.

Polymorphism and mutation databases

DMDMi20455239.

Proteomic databases

EPDiQ9UGR2.
MaxQBiQ9UGR2.
PaxDbiQ9UGR2.
PRIDEiQ9UGR2.

Protocols and materials databases

DNASUi23264.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000352645; ENSP00000345793; ENSG00000100403. [Q9UGR2-2]
GeneIDi23264.
KEGGihsa:23264.
UCSCiuc003azw.5. human. [Q9UGR2-1]

Organism-specific databases

CTDi23264.
GeneCardsiZC3H7B.
H-InvDBHIX0016515.
HGNCiHGNC:30869. ZC3H7B.
HPAiHPA001784.
neXtProtiNX_Q9UGR2.
PharmGKBiPA142670533.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IN1T. Eukaryota.
ENOG410YBKB. LUCA.
GeneTreeiENSGT00390000018542.
HOVERGENiHBG058699.
InParanoidiQ9UGR2.
OMAiDIETDCY.
OrthoDBiEOG7GBFW5.
PhylomeDBiQ9UGR2.
TreeFamiTF329017.

Miscellaneous databases

ChiTaRSiZC3H7B. human.
GeneWikiiRoxan_(protein).
GenomeRNAii23264.
PROiQ9UGR2.

Gene expression databases

BgeeiQ9UGR2.
CleanExiHS_ZC3H7B.
GenevisibleiQ9UGR2. HS.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
4.10.1000.10. 3 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF13181. TPR_8. 1 hit.
PF00642. zf-CCCH. 2 hits.
[Graphical view]
SMARTiSM00028. TPR. 2 hits.
SM00356. ZnF_C3H1. 4 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF90229. SSF90229. 2 hits.
PROSITEiPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
PS50103. ZF_C3H1. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 2).
    Tissue: Trachea.
  2. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 370-993.
    Tissue: Lung.
  4. "RoXaN: a tetratricopeptide cellular protein interacting with rotavirus non-structural protein NSP3."
    Lindenbaum P.
    Thesis (2000), University of Paris XI, France
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-780 (ISOFORM 2), INTERACTION WITH ROTAVIRUS A NSP3.
  5. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-993 (ISOFORM 2).
    Tissue: Brain.
  6. "RoXaN, a novel cellular protein containing TPR, LD, and zinc finger motifs, forms a ternary complex with eukaryotic initiation factor 4G and rotavirus NSP3."
    Vitour D., Lindenbaum P., Vende P., Becker M.M., Poncet D.
    J. Virol. 78:3851-3862(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROTAVIRUS A NSP3, MUTAGENESIS OF 257-ASP--SER-259 AND 268-LEU--ASP-270.
  7. "Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN."
    Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C., Bolte S., Arold S.T., Poncet D.
    J. Virol. 82:11283-11293(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ROTAVIRUS A NSP3.
  8. "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-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiZ3H7B_HUMAN
AccessioniPrimary (citable) accession number: Q9UGR2
Secondary accession number(s): A7YY88
, B2RCA4, Q5TFX9, Q8TBT9, Q9H8B6, Q9UGQ9, Q9UGR0, Q9UGR1, Q9UK03, Q9UPW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 145 of the entry and version 1 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 22
    Human chromosome 22: 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. 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.