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FKBP12-associated protein 1 homolog

 FAP1H_SCHPO             Reviewed;        1077 AA.
O74853;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
20-JUN-2018, entry version 127.
RecName: Full=FKBP12-associated protein 1 homolog;
Name=fap1; ORFNames=SPCC18.03;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the
fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: May play a role in transcription regulation.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
Golgi apparatus {ECO:0000269|PubMed:16823372}. Nucleus
{ECO:0000250}.
-!- SIMILARITY: Belongs to the NFX1 family. {ECO:0000305}.
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EMBL; CU329672; CAA21417.1; -; Genomic_DNA.
PIR; T41146; T41146.
RefSeq; NP_588382.1; NM_001023373.2.
ProteinModelPortal; O74853; -.
STRING; 4896.SPCC18.03.1; -.
iPTMnet; O74853; -.
MaxQB; O74853; -.
PaxDb; O74853; -.
PRIDE; O74853; -.
EnsemblFungi; SPCC18.03.1; SPCC18.03.1:pep; SPCC18.03.
GeneID; 2538928; -.
KEGG; spo:SPCC18.03; -.
EuPathDB; FungiDB:SPCC18.03; -.
PomBase; SPCC18.03; -.
InParanoid; O74853; -.
KO; K12236; -.
OMA; HPCNILC; -.
OrthoDB; EOG092C0AK7; -.
PhylomeDB; O74853; -.
PRO; PR:O74853; -.
Proteomes; UP000002485; Chromosome III.
GO; GO:0005829; C:cytosol; HDA:PomBase.
GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:PomBase.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:PomBase.
GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
CDD; cd06006; R3H_unknown_2; 1.
Gene3D; 3.30.1370.50; -; 1.
InterPro; IPR034078; NFX1_fam.
InterPro; IPR001374; R3H_dom.
InterPro; IPR036867; R3H_dom_sf.
InterPro; IPR034077; R3H_FAP1.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR000967; Znf_NFX1.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
PANTHER; PTHR12360; PTHR12360; 1.
Pfam; PF01424; R3H; 1.
Pfam; PF01422; zf-NF-X1; 8.
SMART; SM00393; R3H; 1.
SMART; SM00438; ZnF_NFX; 8.
SUPFAM; SSF82708; SSF82708; 1.
PROSITE; PS51061; R3H; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Golgi apparatus; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 1077 FKBP12-associated protein 1 homolog.
/FTId=PRO_0000317322.
DOMAIN 835 897 R3H. {ECO:0000255|PROSITE-
ProRule:PRU00382}.
ZN_FING 197 247 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
ZN_FING 290 308 NF-X1-type 1.
ZN_FING 348 367 NF-X1-type 2.
ZN_FING 420 441 NF-X1-type 3.
ZN_FING 485 503 NF-X1-type 4.
ZN_FING 541 558 NF-X1-type 5.
ZN_FING 595 614 NF-X1-type 6.
ZN_FING 708 729 NF-X1-type 7.
ZN_FING 738 760 NF-X1-type 8.
MOD_RES 33 33 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
SEQUENCE 1077 AA; 121088 MW; B96B3B8B871A10C0 CRC64;
METSKNPSDL PKKPANVKKN RRRFQKSQKK SISPSSGSEL PNFKTTISQN NEEVKTSLKE
DSSKFHPSAS APIFVPTSSV QLNVSKNNGH KASDIVDAVS SKDEELRKHA KGEGKRSKNR
KRSSKHSEKQ AVDLKSSNSS QETSSSKGSV NNKSERSREA KSRMPKNSKE IKKGLDLSKL
DMTSRMIVEL KNRLYECSVC TDTINPSTSI WSCGTCYHVF HLSCIRKWCK NSIEQRNEDA
WRCPYCQSNQ TETSLHYLCW CGKQEKPEFV KNLVPHSCGD PCGKTRGQDC EHPCPLLCHP
GPCPPCTATV EKFCLCGKES IHARCSNISK VNTEPFRCEN VCDELLPCGE HTCKKRCHSG
LCGACFEPIN AKCYCGLHSK TYPCSSLPSP SISKKDENGS VKEWFGYYSC NNPCTLFFDC
GLHKCSKTCH PISETRAHCP FATDVLTKCP CGKEDISFLL KGHERKSCSD PIPTCENICG
KLLSCGHRCK YKCHLGSCGT CSETLTIPCR CTANEVQVTC EQLQNGFIPT CERLCTILLS
CGRHQCNKKC CSGYSKAQTR LARRPKGAKL RYHLLTEEFE EEHICFRPCN KKLSCGNHFC
QHMCHRGPCP RCLEASFEEL PCTCGRTRLY PPVACGTPIP DCPYLCVLPK SCHHPQVKHN
CHPTSEPCPP CPYFVKKRCL CGKHILENQP CYRENVRCGE LCNKLLSCKT HFCEKLCHPD
GECESSCKKE CGKRRMYCEH VCQSPCHAGH PCDERIPCKA PLEVSCECGR IRKKVTCDAS
YDNPDPQHKV SCTLECSQQQ RNKLFAEALN IKTDRRSNDV AQYTKSLLVF YGKHSDFADE
VESLLRNFVN NKASSFRFPS MRREQRAFVH MFAKLLGLES VSFDPEPKRN VMVYNKGEAK
LPNMLLKEAN LYHLQHPEIP LKPDSLLGPE EENATASHID GSSNASDSGY NAFVLKELLK
EVNDESAIFS VLDDIVDFNH LTWSILFGEN YIILKPLNTD LIVNKTGKLV ALRPLVNRRL
ADAGIASRCE ICEINDKNEI VKTRSQRIHS KKKAFLSLVP DKSIGVINRY KELATEL


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