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DescriptionRecName: Full=Zinc finger protein 322; AltName: Full=Zinc finger protein 322A; AltName: Full=Zinc finger protein 388; AltName: Full=Zinc finger protein 489;
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MyHits synonymsZN322_HUMAN , Q6U7Q0 , A8K1X3 , Q0VDH6 , Q6B0G2 , Q86W72 , Q9H5I9 , A9A54EC8884BD27D
match map segment
ismart:ZnF_C2H2 iprf:ZINC_FINGER_C2H2_2 ismart:ZnF_C2H2 iprf:ZINC_FINGER_C2H2_2 ismart:ZnF_C2H2 ismart:ZnF_C2H2 ipat:ZINC_FINGER_C2H2_1 iprf:ZINC_FINGER_C2H2_2 ipat:ZINC_FINGER_C2H2_1 ipat:ZINC_FINGER_C2H2_1 ipat:ZINC_FINGER_C2H2_1 ismart:ZnF_C2H2 iprf:ZINC_FINGER_C2H2_2 ismart:ZnF_C2H2 ismart:ZnF_C2H2 ismart:ZnF_C2H2 ipat:ZINC_FINGER_C2H2_1 iprf:ZINC_FINGER_C2H2_2 iprf:ZINC_FINGER_C2H2_2 ismart:ZnF_C2H2 ipat:ZINC_FINGER_C2H2_1 ismart:ZnF_C2H2 ipat:ZINC_FINGER_C2H2_1 iprf:ZINC_FINGER_C2H2_2 iprf:ZINC_FINGER_C2H2_2 iprf:ZINC_FINGER_C2H2_2 iprf:ZINC_FINGER_C2H2_2 ismart:ZnF_C2H2 iprf:ZINC_FINGER_C2H2_2  
Legends: 1, Phosphoserine. {ECO:0000244|PubMed:23186163}; 2, CONFLICT H -> R (in Ref. 1; AAQ85127). {ECO:0000305}; 3, CONFLICT C -> S (in Ref. 2; BAB15637). {ECO:0000305}; 4, CONFLICT N -> H (in Ref. 1; AAQ85127). {ECO:0000305}; 5, CONFLICT C -> R (in Ref. 1; AAQ85127). {ECO:0000305}; 6, CONFLICT A -> V (in Ref. 1; AAQ85127). {ECO:0000305}; 7, ZN_FING C2H2-type 1; atypical. {ECO:0000255|PROSITE-ProRule:PRU00042}; 8, ZN_FING C2H2-type 2. {ECO:0000255|PROSITE- ProRule:PRU00042}; 9, ZN_FING C2H2-type 3. {ECO:0000255|PROSITE- ProRule:PRU00042}; 10, ZN_FING C2H2-type 4. {ECO:0000255|PROSITE- ProRule:PRU00042}; 11, ZN_FING C2H2-type 5. {ECO:0000255|PROSITE- ProRule:PRU00042}; 12, ZN_FING C2H2-type 6. {ECO:0000255|PROSITE- ProRule:PRU00042}; 13, ZN_FING C2H2-type 7. {ECO:0000255|PROSITE- ProRule:PRU00042}; 14, ZN_FING C2H2-type 8. {ECO:0000255|PROSITE- ProRule:PRU00042}; 15, ZN_FING C2H2-type 9. {ECO:0000255|PROSITE- ProRule:PRU00042}; 16, ZN_FING C2H2-type 10; degenerate. {ECO:0000255|PROSITE-ProRule:PRU00042}; 17, ZN_FING C2H2-type 11; degenerate. {ECO:0000255|PROSITE-ProRule:PRU00042}; 18, ismart:ZnF_C2H2 [T]; 19, iprf:ZINC_FINGER_C2H2_2 [T]; 20, ipat:ZINC_FINGER_C2H2_1 [T].
ID   ZN322_HUMAN             Reviewed;         402 AA.
AC   Q6U7Q0; A8K1X3; Q0VDH6; Q6B0G2; Q86W72; Q9H5I9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   10-MAY-2017, entry version 118.
DE   RecName: Full=Zinc finger protein 322;
DE   AltName: Full=Zinc finger protein 322A;
DE   AltName: Full=Zinc finger protein 388;
DE   AltName: Full=Zinc finger protein 489;
GN   Name=ZNF322; Synonyms=ZNF322A, ZNF388, ZNF489;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN TRANSCRIPTIONAL ACTIVATION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryonic heart;
RX   PubMed=15555580; DOI=10.1016/j.bbrc.2004.10.183;
RA   Li Y., Wang Y., Zhang C., Yuan W., Wang J., Zhu C., Chen L., Huang W.,
RA   Zeng W., Wu X., Liu M.;
RT   "ZNF322, a novel human C(2)H(2) Kruppel-like zinc-finger protein,
RT   regulates transcriptional activation in MAPK signaling pathways.";
RL   Biochem. Biophys. Res. Commun. 325:1383-1392(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Hepatoma, and Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Involved in transcriptional regulation as an activator.
CC       {ECO:0000269|PubMed:15555580}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15555580}.
CC       Nucleus {ECO:0000269|PubMed:15555580}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart and
CC       skeletal muscle. {ECO:0000269|PubMed:15555580}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo as early as the 11th week
CC       of gestation. {ECO:0000269|PubMed:15555580}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15637.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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DR   EMBL; AY376736; AAQ85127.1; -; mRNA.
DR   EMBL; AK027046; BAB15637.1; ALT_INIT; mRNA.
DR   EMBL; AK290038; BAF82727.1; -; mRNA.
DR   EMBL; BC050425; AAH50425.2; -; mRNA.
DR   EMBL; BC074772; AAH74772.1; -; mRNA.
DR   EMBL; BC119669; AAI19670.1; -; mRNA.
DR   CCDS; CCDS4617.1; -.
DR   RefSeq; NP_001229726.1; NM_001242797.1.
DR   RefSeq; NP_001229727.1; NM_001242798.1.
DR   RefSeq; NP_001229728.1; NM_001242799.1.
DR   RefSeq; NP_078915.2; NM_024639.4.
DR   UniGene; Hs.126280; -.
DR   UniGene; Hs.530271; -.
DR   UniGene; Hs.709963; -.
DR   ProteinModelPortal; Q6U7Q0; -.
DR   SMR; Q6U7Q0; -.
DR   BioGrid; 122813; 1.
DR   STRING; 9606.ENSP00000418897; -.
DR   iPTMnet; Q6U7Q0; -.
DR   PhosphoSitePlus; Q6U7Q0; -.
DR   BioMuta; ZNF322; -.
DR   DMDM; 82582384; -.
DR   MaxQB; Q6U7Q0; -.
DR   PaxDb; Q6U7Q0; -.
DR   PeptideAtlas; Q6U7Q0; -.
DR   PRIDE; Q6U7Q0; -.
DR   DNASU; 79692; -.
DR   Ensembl; ENST00000415922; ENSP00000418897; ENSG00000181315.
DR   Ensembl; ENST00000456172; ENSP00000478899; ENSG00000181315.
DR   Ensembl; ENST00000471278; ENSP00000419728; ENSG00000181315.
DR   Ensembl; ENST00000607204; ENSP00000483223; ENSG00000181315.
DR   Ensembl; ENST00000622479; ENSP00000482607; ENSG00000181315.
DR   GeneID; 79692; -.
DR   KEGG; hsa:79692; -.
DR   UCSC; uc003nil.4; human.
DR   CTD; 79692; -.
DR   DisGeNET; 79692; -.
DR   GeneCards; ZNF322; -.
DR   HGNC; HGNC:23640; ZNF322.
DR   HPA; HPA043161; -.
DR   HPA; HPA046692; -.
DR   MIM; 610847; gene.
DR   neXtProt; NX_Q6U7Q0; -.
DR   OpenTargets; ENSG00000181315; -.
DR   PharmGKB; PA134861342; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00790000123153; -.
DR   HOGENOM; HOG000234617; -.
DR   HOVERGEN; HBG018163; -.
DR   InParanoid; Q6U7Q0; -.
DR   OMA; STCESGF; -.
DR   OrthoDB; EOG091G02KC; -.
DR   PhylomeDB; Q6U7Q0; -.
DR   TreeFam; TF338126; -.
DR   ChiTaRS; ZNF322; human.
DR   GenomeRNAi; 79692; -.
DR   PRO; PR:Q6U7Q0; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000181315; -.
DR   CleanEx; HS_ZNF322A; -.
DR   ExpressionAtlas; Q6U7Q0; baseline and differential.
DR   Genevisible; Q6U7Q0; HS.
DR   GO; GO:0005813; C:centrosome; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 11.
DR   SUPFAM; SSF57667; SSF57667; 7.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE   1: Evidence at protein level;
KW   Activator; Complete proteome; Cytoplasm; DNA-binding; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    402       Zinc finger protein 322.
FT                                /FTId=PRO_0000047529.
FT   ZN_FING      43     65       C2H2-type 1; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING      71     93       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING      99    121       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     127    149       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     155    177       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     183    205       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     211    233       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     239    261       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     267    289       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     293    315       C2H2-type 10; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     351    373       C2H2-type 11; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   MOD_RES     391    391       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CONFLICT     33     33       H -> R (in Ref. 1; AAQ85127).
FT                                {ECO:0000305}.
FT   CONFLICT     73     73       C -> S (in Ref. 2; BAB15637).
FT                                {ECO:0000305}.
FT   CONFLICT     94     94       N -> H (in Ref. 1; AAQ85127).
FT                                {ECO:0000305}.
FT   CONFLICT    101    101       C -> R (in Ref. 1; AAQ85127).
FT                                {ECO:0000305}.
FT   CONFLICT    373    373       H -> R (in Ref. 1; AAQ85127).
FT                                {ECO:0000305}.
FT   CONFLICT    398    398       A -> V (in Ref. 1; AAQ85127).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       211    233       ismart:ZnF_C2H2 [T]
FT   MYHIT       155    182       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT        71     93       ismart:ZnF_C2H2 [T]
FT   MYHIT       267    290       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       267    289       ismart:ZnF_C2H2 [T]
FT   MYHIT       351    373       ismart:ZnF_C2H2 [T]
FT   MYHIT       101    121       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       293    320       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       185    205       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       129    149       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT        73     93       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       183    205       ismart:ZnF_C2H2 [T]
FT   MYHIT        43     70       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT        99    121       ismart:ZnF_C2H2 [T]
FT   MYHIT       155    177       ismart:ZnF_C2H2 [T]
FT   MYHIT       127    149       ismart:ZnF_C2H2 [T]
FT   MYHIT       241    261       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT        99    126       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       127    154       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       293    315       ismart:ZnF_C2H2 [T]
FT   MYHIT       157    177       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT        43     65       ismart:ZnF_C2H2 [T]
FT   MYHIT       213    233       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       183    210       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       351    378       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       211    238       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       239    266       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       239    261       ismart:ZnF_C2H2 [T]
FT   MYHIT        71     98       iprf:ZINC_FINGER_C2H2_2 [T]
SQ   SEQUENCE   402 AA;  46941 MW;  A9A54EC8884BD27D CRC64;
     MYTSEEKCNQ RTQKRKIYNV CPRKGKKIFI HMHEIIQIDG HIYQCLECKQ NFCENLALIM
     CERTHTGEKP YKCDMCEKTF VQSSDLTSHQ RIHNYEKPYK CSKCEKSFWH HLALSGHQRT
     HAGKKFYTCD ICGKNFGQSS DLLVHQRSHT GEKPYLCSEC DKCFSRSTNL IRHRRTHTGE
     KPFKCLECEK AFSGKSDLIS HQRTHTGERP YKCNKCEKSY RHRSAFIVHK RVHTGEKPYK
     CGACEKCFGQ KSDLIVHQRV HTGEKPYKCL ECMRSFTRSA NLIRHQATHT HTFKCLEYEK
     SFNCSSDLIV HQRIHMEEKP HQWSACESGF LLGMDFVAQQ KMRTQTEELH YKYTVCDKSF
     HQSSALLQHQ TVHIGEKPFV CNVSEKGLEL SPPHASEASQ MS
//