CPIN1_HUMAN
ID CPIN1_HUMAN Reviewed; 312 AA.
AC Q6FI81; A8K8B6; O75206; O75207; Q9H0W1; Q9P1L7;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Anamorsin {ECO:0000255|HAMAP-Rule:MF_03115};
DE AltName: Full=Cytokine-induced apoptosis inhibitor 1 {ECO:0000255|HAMAP-Rule:MF_03115};
DE AltName: Full=Fe-S cluster assembly protein DRE2 homolog {ECO:0000255|HAMAP-Rule:MF_03115};
GN Name=CIAPIN1 {ECO:0000255|HAMAP-Rule:MF_03115}; ORFNames=CUA001, PRO0915;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal tumor;
RA Yang Y., Xu X., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal liver;
RX PubMed=11483580; DOI=10.1101/gr.175501;
RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y.,
RA Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.;
RT "Gene expression profiling in human fetal liver and identification of
RT tissue- and developmental-stage-specific genes through compiled expression
RT profiles and efficient cloning of full-length cDNAs.";
RL Genome Res. 11:1392-1403(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Placenta, Skin, and Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=14970183; DOI=10.1084/jem.20031858;
RA Shibayama H., Takai E., Matsumura I., Kouno M., Morii E., Kitamura Y.,
RA Takeda J., Kanakura Y.;
RT "Identification of a cytokine-induced antiapoptotic molecule anamorsin
RT essential for definitive hematopoiesis.";
RL J. Exp. Med. 199:581-592(2004).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=16957168; DOI=10.1369/jhc.6a6960.2006;
RA Hao Z., Li X., Qiao T., Du R., Zhang G., Fan D.;
RT "Subcellular localization of CIAPIN1.";
RL J. Histochem. Cytochem. 54:1437-1444(2006).
RN [11]
RP LACK OF METHYLTRANSFERASE ACTIVITY.
RX PubMed=17935775; DOI=10.1016/j.ijbiomac.2007.08.009;
RA Hao Z., Li X., Qiao T., Fan D.;
RT "Successful expression and purification of human CIAPIN1 in baculovirus-
RT insect cell system and application of this system to investigation of its
RT potential methyltransferase activity.";
RL Int. J. Biol. Macromol. 42:27-32(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-183, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-307, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP COFACTOR.
RX PubMed=23989406; DOI=10.1007/s00775-013-1033-1;
RA Banci L., Ciofi-Baffoni S., Mikolajczyk M., Winkelmann J., Bill E.,
RA Pandelia M.E.;
RT "Human anamorsin binds [2Fe-2S] clusters with unique electronic
RT properties.";
RL J. Biol. Inorg. Chem. 18:883-893(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-136; SER-177; SER-183;
RP SER-305 AND SER-307, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
RN [19]
RP INTERACTION WITH NDOR1, DOMAIN, FUNCTION, AND COFACTOR.
RX PubMed=23596212; DOI=10.1073/pnas.1302378110;
RA Banci L., Bertini I., Calderone V., Ciofi-Baffoni S., Giachetti A.,
RA Jaiswal D., Mikolajczyk M., Piccioli M., Winkelmann J.;
RT "Molecular view of an electron transfer process essential for iron-sulfur
RT protein biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:7136-7141(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP COFACTOR.
RX PubMed=26613676; DOI=10.1021/jacs.5b10592;
RA Banci L., Camponeschi F., Ciofi-Baffoni S., Muzzioli R.;
RT "Elucidating the molecular function of human BOLA2 in GRX3-dependent
RT anamorsin maturation pathway.";
RL J. Am. Chem. Soc. 137:16133-16143(2015).
RN [22]
RP COFACTOR.
RX PubMed=27519415; DOI=10.1074/jbc.m116.744946;
RA Frey A.G., Palenchar D.J., Wildemann J.D., Philpott C.C.;
RT "A glutaredoxin-BolA complex serves as an iron-sulfur cluster chaperone for
RT the cytosolic cluster assembly machinery.";
RL J. Biol. Chem. 291:22344-22356(2016).
RN [23]
RP COFACTOR.
RX PubMed=27672211; DOI=10.1093/jb/mvw054;
RA Zhang Y., Yang C., Dancis A., Nakamaru-Ogiso E.;
RT "EPR studies of wild type and mutant Dre2 identify essential [2Fe--2S] and
RT [4Fe--4S] clusters and their cysteine ligands.";
RL J. Biochem. 161:67-78(2017).
RN [24]
RP STRUCTURE BY NMR OF 1-171.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal domain in human cytokine-induced
RT apoptosis inhibitor anamorsin.";
RL Submitted (APR-2008) to the PDB data bank.
RN [25]
RP STRUCTURE BY NMR OF 1-172, COFACTOR, INTERACTION WITH CHCHD4, SUBUNIT,
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=21700214; DOI=10.1016/j.chembiol.2011.03.015;
RA Banci L., Bertini I., Ciofi-Baffoni S., Boscaro F., Chatzi A.,
RA Mikolajczyk M., Tokatlidis K., Winkelmann J.;
RT "Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-
RT dependent mitochondrial protein trapping machinery.";
RL Chem. Biol. 18:794-804(2011).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-172.
RX PubMed=24123282; DOI=10.1002/prot.24443;
RA Song G., Cheng C., Li Y., Shaw N., Xiao Z.C., Liu Z.J.;
RT "Crystal structure of the N-terminal methyltransferase-like domain of
RT anamorsin.";
RL Proteins 82:1066-1071(2014).
RN [27]
RP SUBCELLULAR LOCATION.
RX PubMed=29848660; DOI=10.1242/jcs.211433;
RA Ben-Shimon L., Paul V.D., David-Kadoch G., Volpe M., Stuempfig M., Bill E.,
RA Muehlenhoff U., Lill R., Ben-Aroya S.;
RT "Fe-S cluster coordination of the chromokinesin KIF4A alters its
RT subcellular localization during mitosis.";
RL J. Cell Sci. 131:0-0(2018).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein
CC assembly (CIA) machinery required for the maturation of
CC extramitochondrial Fe-S proteins. Part of an electron transfer chain
CC functioning in an early step of cytosolic Fe-S biogenesis, facilitating
CC the de novo assembly of a [4Fe-4S] cluster on the scaffold complex
CC NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the
CC FAD- and FMN-containing protein NDOR1 (PubMed:23596212). NDOR1-CIAPIN1
CC are also required for the assembly of the diferric tyrosyl radical
CC cofactor of ribonucleotide reductase (RNR), probably by providing
CC electrons for reduction during radical cofactor maturation in the
CC catalytic small subunit (By similarity). Has anti-apoptotic effects in
CC the cell. Involved in negative control of cell death upon cytokine
CC withdrawal. Promotes development of hematopoietic cells (By
CC similarity). {ECO:0000250|UniProtKB:P36152,
CC ECO:0000250|UniProtKB:Q8WTY4, ECO:0000255|HAMAP-Rule:MF_03115,
CC ECO:0000269|PubMed:23596212}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03115,
CC ECO:0000269|PubMed:21700214, ECO:0000269|PubMed:23596212,
CC ECO:0000269|PubMed:23989406, ECO:0000269|PubMed:26613676,
CC ECO:0000269|PubMed:27519415};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03115,
CC ECO:0000269|PubMed:27672211};
CC Note=In the presence of oxygen, the A site-bound [2Fe-2S] cluster is
CC labile and the B site-bound [4Fe-4S] cluster is readily converted into
CC a [2Fe-2S] cluster, a reason why recombinant protein is often isolated
CC with a single [2Fe-2S] cluster. {ECO:0000255|HAMAP-Rule:MF_03115,
CC ECO:0000305|PubMed:27672211};
CC -!- SUBUNIT: Monomer. Interacts with NDOR1; its oxidized form can be
CC reduced by NDOR1. Interacts with CHCHD4 and may be a substrate for
CC CHCHD4 chaperone activity. {ECO:0000269|PubMed:21700214,
CC ECO:0000269|PubMed:23596212}.
CC -!- INTERACTION:
CC Q6FI81; Q9H3K6: BOLA2B; NbExp=2; IntAct=EBI-750511, EBI-1642537;
CC Q6FI81; P54284: CACNB3; NbExp=5; IntAct=EBI-750511, EBI-1184651;
CC Q6FI81; O76003: GLRX3; NbExp=22; IntAct=EBI-750511, EBI-374781;
CC Q6FI81; P50222: MEOX2; NbExp=3; IntAct=EBI-750511, EBI-748397;
CC Q6FI81; Q9UHB4: NDOR1; NbExp=14; IntAct=EBI-750511, EBI-10249760;
CC Q6FI81-1; O76003: GLRX3; NbExp=2; IntAct=EBI-16172762, EBI-374781;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03115,
CC ECO:0000269|PubMed:16957168, ECO:0000269|PubMed:29848660}. Nucleus
CC {ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000269|PubMed:16957168}.
CC Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03115,
CC ECO:0000269|PubMed:21700214}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6FI81-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6FI81-2; Sequence=VSP_012360;
CC Name=3;
CC IsoId=Q6FI81-3; Sequence=VSP_012361;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in heart,
CC liver and pancreas. {ECO:0000269|PubMed:14970183}.
CC -!- DOMAIN: The twin Cx2C motifs are involved in the recognition by the
CC mitochondrial CHCHD4/MIA40-GFER/ERV1 disulfide relay system. The
CC formation of 2 disulfide bonds in the Cx2C motifs through
CC dithiol/disulfide exchange reactions effectively traps the protein in
CC the mitochondrial intermembrane space. {ECO:0000255|HAMAP-
CC Rule:MF_03115}.
CC -!- DOMAIN: The C-terminal domain binds 2 Fe-S clusters but is otherwise
CC mostly in an intrinsically disordered conformation. {ECO:0000255|HAMAP-
CC Rule:MF_03115}.
CC -!- DOMAIN: The N-terminal domain has structural similarity with S-
CC adenosyl-L-methionine-dependent methyltransferases, but does not bind
CC S-adenosyl-L-methionine. It is required for correct assembly of the 2
CC Fe-S clusters. {ECO:0000255|HAMAP-Rule:MF_03115,
CC ECO:0000269|PubMed:21700214, ECO:0000269|PubMed:24123282}.
CC -!- MISCELLANEOUS: 'Ana-mors-in' means 'anti-death molecule' in Latin.
CC -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000255|HAMAP-
CC Rule:MF_03115}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24312.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF248964; AAG44562.1; -; mRNA.
DR EMBL; AL136613; CAB66548.1; -; mRNA.
DR EMBL; AF116609; AAF71034.1; -; mRNA.
DR EMBL; CR533545; CAG38576.1; -; mRNA.
DR EMBL; AK292281; BAF84970.1; -; mRNA.
DR EMBL; AC004382; AAC24311.1; -; Genomic_DNA.
DR EMBL; AC004382; AAC24312.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471092; EAW82923.1; -; Genomic_DNA.
DR EMBL; BC002568; AAH02568.1; -; mRNA.
DR EMBL; BC024196; AAH24196.1; -; mRNA.
DR EMBL; BC067303; AAH67303.1; -; mRNA.
DR EMBL; BC071740; AAH71740.1; -; mRNA.
DR CCDS; CCDS10781.2; -. [Q6FI81-1]
DR CCDS; CCDS76876.1; -. [Q6FI81-3]
DR RefSeq; NP_001295276.1; NM_001308347.1. [Q6FI81-3]
DR RefSeq; NP_001295287.1; NM_001308358.1.
DR RefSeq; NP_064709.2; NM_020313.3. [Q6FI81-1]
DR PDB; 2LD4; NMR; -; A=1-172.
DR PDB; 2YUI; NMR; -; A=1-170.
DR PDB; 4M7R; X-ray; 1.80 A; A/B=1-172.
DR PDBsum; 2LD4; -.
DR PDBsum; 2YUI; -.
DR PDBsum; 4M7R; -.
DR AlphaFoldDB; Q6FI81; -.
DR BMRB; Q6FI81; -.
DR SMR; Q6FI81; -.
DR BioGRID; 121328; 67.
DR DIP; DIP-61697N; -.
DR IntAct; Q6FI81; 17.
DR MINT; Q6FI81; -.
DR STRING; 9606.ENSP00000377914; -.
DR ChEMBL; CHEMBL4523341; -.
DR GlyGen; Q6FI81; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6FI81; -.
DR PhosphoSitePlus; Q6FI81; -.
DR BioMuta; CIAPIN1; -.
DR DMDM; 57012667; -.
DR EPD; Q6FI81; -.
DR jPOST; Q6FI81; -.
DR MassIVE; Q6FI81; -.
DR MaxQB; Q6FI81; -.
DR PaxDb; Q6FI81; -.
DR PeptideAtlas; Q6FI81; -.
DR PRIDE; Q6FI81; -.
DR ProteomicsDB; 66295; -. [Q6FI81-1]
DR ProteomicsDB; 66296; -. [Q6FI81-2]
DR ProteomicsDB; 66297; -. [Q6FI81-3]
DR TopDownProteomics; Q6FI81-1; -. [Q6FI81-1]
DR Antibodypedia; 28857; 418 antibodies from 32 providers.
DR DNASU; 57019; -.
DR Ensembl; ENST00000394391.9; ENSP00000377914.4; ENSG00000005194.15. [Q6FI81-1]
DR Ensembl; ENST00000567518.5; ENSP00000456114.1; ENSG00000005194.15. [Q6FI81-3]
DR GeneID; 57019; -.
DR KEGG; hsa:57019; -.
DR MANE-Select; ENST00000394391.9; ENSP00000377914.4; NM_020313.4; NP_064709.2.
DR UCSC; uc002ell.2; human. [Q6FI81-1]
DR CTD; 57019; -.
DR DisGeNET; 57019; -.
DR GeneCards; CIAPIN1; -.
DR HGNC; HGNC:28050; CIAPIN1.
DR HPA; ENSG00000005194; Low tissue specificity.
DR MIM; 608943; gene.
DR neXtProt; NX_Q6FI81; -.
DR OpenTargets; ENSG00000005194; -.
DR PharmGKB; PA134978864; -.
DR VEuPathDB; HostDB:ENSG00000005194; -.
DR eggNOG; KOG4020; Eukaryota.
DR GeneTree; ENSGT00390000011417; -.
DR HOGENOM; CLU_064393_2_0_1; -.
DR InParanoid; Q6FI81; -.
DR OMA; QRVAIIW; -.
DR OrthoDB; 1588798at2759; -.
DR PhylomeDB; Q6FI81; -.
DR TreeFam; TF314449; -.
DR PathwayCommons; Q6FI81; -.
DR Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
DR SignaLink; Q6FI81; -.
DR BioGRID-ORCS; 57019; 600 hits in 1089 CRISPR screens.
DR ChiTaRS; CIAPIN1; human.
DR EvolutionaryTrace; Q6FI81; -.
DR GeneWiki; CIAPIN1; -.
DR GenomeRNAi; 57019; -.
DR Pharos; Q6FI81; Tbio.
DR PRO; PR:Q6FI81; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6FI81; protein.
DR Bgee; ENSG00000005194; Expressed in oocyte and 203 other tissues.
DR ExpressionAtlas; Q6FI81; baseline and differential.
DR Genevisible; Q6FI81; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030097; P:hemopoiesis; IEA:UniProtKB-UniRule.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR DisProt; DP01137; -.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03115; Anamorsin; 1.
DR InterPro; IPR007785; Anamorsin.
DR InterPro; IPR046408; CIAPIN1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13273; PTHR13273; 1.
DR Pfam; PF05093; CIAPIN1; 2.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; 4Fe-4S; Alternative splicing; Apoptosis; Cytoplasm;
KW Iron; Iron-sulfur; Metal-binding; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..312
FT /note="Anamorsin"
FT /id="PRO_0000079288"
FT REGION 6..172
FT /note="N-terminal SAM-like domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 173..224
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 237..251
FT /note="Fe-S binding site A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 274..288
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 274..277
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 285..288
FT /note="Cx2C motif 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 237
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 246
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 249
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 251
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 274
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 277
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 285
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 288
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOD_RES 136
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WTY4"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..204
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11483580"
FT /id="VSP_012360"
FT VAR_SEQ 53..66
FT /note="SAHKESSFDIILSG -> C (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_012361"
FT VARIANT 34
FT /note="A -> E (in dbSNP:rs11557672)"
FT /id="VAR_033747"
FT VARIANT 52
FT /note="Q -> E (in dbSNP:rs11557674)"
FT /id="VAR_033748"
FT CONFLICT 142
FT /note="S -> F (in Ref. 2; CAB66548 and 4; CAG38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="Y -> C (in Ref. 4; CAG38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="P -> T (in Ref. 2; CAB66548 and 4; CAG38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="H -> N (in Ref. 2; CAB66548 and 4; CAG38576)"
FT /evidence="ECO:0000305"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:4M7R"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:4M7R"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:4M7R"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:4M7R"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4M7R"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4M7R"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:4M7R"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4M7R"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2YUI"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:4M7R"
FT STRAND 87..102
FT /evidence="ECO:0007829|PDB:4M7R"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2LD4"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:4M7R"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:4M7R"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:4M7R"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:4M7R"
SQ SEQUENCE 312 AA; 33582 MW; 70A71D44074ABFBA CRC64;
MADFGISAGQ FVAVVWDKSS PVEALKGLVD KLQALTGNEG RVSVENIKQL LQSAHKESSF
DIILSGLVPG STTLHSAEIL AEIARILRPG GCLFLKEPVE TAVDNNSKVK TASKLCSALT
LSGLVEVKEL QREPLTPEEV QSVREHLGHE SDNLLFVQIT GKKPNFEVGS SRQLKLSITK
KSSPSVKPAV DPAAAKLWTL SANDMEDDSM DLIDSDELLD PEDLKKPDPA SLRAASCGEG
KKRKACKNCT CGLAEELEKE KSREQMSSQP KSACGNCYLG DAFRCASCPY LGMPAFKPGE
KVLLSDSNLH DA
