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Protein

Anamorsin

Gene

Ciapin1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis. Electrons are transferred to the Fe-S cluster from NADPH via the FAD- and FMN-containing protein NDOR1 (By similarity). Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells.UniRule annotation1 Publication

Cofactori

[2Fe-2S] clusterUniRule annotationNote: Binds 1 [2Fe-2S] cluster per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi235 – 2351Iron-sulfur (2Fe-2S)UniRule annotation
Metal bindingi244 – 2441Iron-sulfur (2Fe-2S)UniRule annotation
Metal bindingi247 – 2471Iron-sulfur (2Fe-2S)UniRule annotation
Metal bindingi249 – 2491Iron-sulfur (2Fe-2S)UniRule annotation

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • hemopoiesis Source: MGI
  • iron-sulfur cluster assembly Source: UniProtKB-HAMAP
  • negative regulation of apoptotic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
AnamorsinUniRule annotation
Alternative name(s):
Cytokine-induced apoptosis inhibitor 1UniRule annotation
Fe-S cluster assembly protein DRE2 homologUniRule annotation
Gene namesi
Name:Ciapin1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1922083. Ciapin1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • mitochondrial intermembrane space Source: UniProtKB-SubCell
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Death in late gestation due to defective definitive hematopoiesis in the fetal liver, possibly due to initiated apoptosis in erythroid cells during terminal maturation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309AnamorsinPRO_0000079289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei182 – 1821PhosphoserineBy similarity
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei213 – 2131PhosphoserineBy similarity
Modified residuei269 – 2691PhosphoserineCombined sources
Modified residuei302 – 3021PhosphoserineBy similarity
Modified residuei304 – 3041PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8WTY4.
MaxQBiQ8WTY4.
PaxDbiQ8WTY4.
PRIDEiQ8WTY4.

PTM databases

iPTMnetiQ8WTY4.
PhosphoSiteiQ8WTY4.

Expressioni

Developmental stagei

Expressed from early embryogenesis.

Inductioni

By cytokines such as IL3 and THPO.1 Publication

Gene expression databases

BgeeiQ8WTY4.
CleanExiMM_CIAPIN1.
ExpressionAtlasiQ8WTY4. baseline and differential.
GenevisibleiQ8WTY4. MM.

Interactioni

Subunit structurei

Monomer. Interacts with NDOR1. Interacts with CHCHD4.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
Glrx3Q9CQM94EBI-2943068,EBI-4319195

Protein-protein interaction databases

IntActiQ8WTY4. 4 interactions.
MINTiMINT-4091789.
STRINGi10090.ENSMUSP00000125451.

Structurei

3D structure databases

ProteinModelPortaliQ8WTY4.
SMRiQ8WTY4. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 172172N-terminal domainUniRule annotationAdd
BLAST
Regioni173 – 22149LinkerUniRule annotationAdd
BLAST
Regioni222 – 30988Intrinsically disorderedUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi271 – 2744Cx2C motif 1
Motifi282 – 2854Cx2C motif 2

Domaini

The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine.UniRule annotation
The C-terminal domain binds one 2Fe-2S iron-sulfur cluster but is otherwise mostly in an intrinsically disordered conformation.UniRule annotation
The twin Cx2C motifs are involved in the recognition by the mitochondrial CHCHD4/MIA40-GFER/ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.UniRule annotation

Sequence similaritiesi

Belongs to the anamorsin family.UniRule annotation

Phylogenomic databases

eggNOGiKOG4020. Eukaryota.
COG5636. LUCA.
GeneTreeiENSGT00390000011417.
HOVERGENiHBG051104.
InParanoidiQ8WTY4.
OMAiMWTLSAN.
OrthoDBiEOG7WHHC3.
PhylomeDBiQ8WTY4.
TreeFamiTF314449.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_03115. Anamorsin.
InterProiIPR007785. Anamorsin.
IPR013216. Methyltransf_11.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR13273. PTHR13273. 1 hit.
PfamiPF05093. CIAPIN1. 2 hits.
PF08241. Methyltransf_11. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8WTY4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEFGISPGQ LVAVFWDKSS PEEALKKLVA RLQELTGSEG QVFMENVTQL
60 70 80 90 100
LQSSHKESSF DVILSGVVPG STSLHSAEVL AEMARILRPG GCLFLKEPVE
110 120 130 140 150
TAEVNNDKMK TASKLCSALT LSGLVEIKEL QREALSPEEV QSVQEHLGYH
160 170 180 190 200
SDSLRSVRVT GKKPNFEVGS SSQLKLPNKK SSSVKPVVDP AAAKLWTLSA
210 220 230 240 250
NDMEDDSVDL IDSDELLDPE DLKRPDPASL KAPSCGEGKK RKACKNCTCG
260 270 280 290 300
LAEELEREQS KAQSSQPKSA CGNCYLGDAF RCANCPYLGM PAFKPGEQVL

LSNSNLQDA
Length:309
Mass (Da):33,429
Last modified:March 1, 2002 - v1
Checksum:i2F1FCB614767C915
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY523555 mRNA. Translation: AAS09959.1.
AK076116 mRNA. Translation: BAC36196.1.
AK079615 mRNA. Translation: BAC37702.1.
AK088757 mRNA. Translation: BAC40550.1.
AK136821 mRNA. Translation: BAE23137.1.
AK146282 mRNA. Translation: BAE27040.1.
AK163705 mRNA. Translation: BAE37466.1.
AK168252 mRNA. Translation: BAE40202.1.
BC016261 mRNA. Translation: AAH16261.1.
BC021864 mRNA. Translation: AAH21864.1.
BC021949 mRNA. Translation: AAH21949.1.
CCDSiCCDS22549.1.
RefSeqiNP_598902.1. NM_134141.4.
XP_006530623.1. XM_006530560.1.
UniGeneiMm.27582.
Mm.472546.

Genome annotation databases

EnsembliENSMUST00000162538; ENSMUSP00000125451; ENSMUSG00000031781.
GeneIDi109006.
KEGGimmu:109006.
UCSCiuc009mxa.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY523555 mRNA. Translation: AAS09959.1.
AK076116 mRNA. Translation: BAC36196.1.
AK079615 mRNA. Translation: BAC37702.1.
AK088757 mRNA. Translation: BAC40550.1.
AK136821 mRNA. Translation: BAE23137.1.
AK146282 mRNA. Translation: BAE27040.1.
AK163705 mRNA. Translation: BAE37466.1.
AK168252 mRNA. Translation: BAE40202.1.
BC016261 mRNA. Translation: AAH16261.1.
BC021864 mRNA. Translation: AAH21864.1.
BC021949 mRNA. Translation: AAH21949.1.
CCDSiCCDS22549.1.
RefSeqiNP_598902.1. NM_134141.4.
XP_006530623.1. XM_006530560.1.
UniGeneiMm.27582.
Mm.472546.

3D structure databases

ProteinModelPortaliQ8WTY4.
SMRiQ8WTY4. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8WTY4. 4 interactions.
MINTiMINT-4091789.
STRINGi10090.ENSMUSP00000125451.

PTM databases

iPTMnetiQ8WTY4.
PhosphoSiteiQ8WTY4.

Proteomic databases

EPDiQ8WTY4.
MaxQBiQ8WTY4.
PaxDbiQ8WTY4.
PRIDEiQ8WTY4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000162538; ENSMUSP00000125451; ENSMUSG00000031781.
GeneIDi109006.
KEGGimmu:109006.
UCSCiuc009mxa.2. mouse.

Organism-specific databases

CTDi57019.
MGIiMGI:1922083. Ciapin1.

Phylogenomic databases

eggNOGiKOG4020. Eukaryota.
COG5636. LUCA.
GeneTreeiENSGT00390000011417.
HOVERGENiHBG051104.
InParanoidiQ8WTY4.
OMAiMWTLSAN.
OrthoDBiEOG7WHHC3.
PhylomeDBiQ8WTY4.
TreeFamiTF314449.

Miscellaneous databases

ChiTaRSiCiapin1. mouse.
PROiQ8WTY4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WTY4.
CleanExiMM_CIAPIN1.
ExpressionAtlasiQ8WTY4. baseline and differential.
GenevisibleiQ8WTY4. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_03115. Anamorsin.
InterProiIPR007785. Anamorsin.
IPR013216. Methyltransf_11.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR13273. PTHR13273. 1 hit.
PfamiPF05093. CIAPIN1. 2 hits.
PF08241. Methyltransf_11. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a cytokine-induced antiapoptotic molecule anamorsin essential for definitive hematopoiesis."
    Shibayama H., Takai E., Matsumura I., Kouno M., Morii E., Kitamura Y., Takeda J., Kanakura Y.
    J. Exp. Med. 199:581-592(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J, DBA/2J and NOD.
    Tissue: Cerebellum, Diencephalon, Spinal cord and Thymus.
  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].
    Strain: FVB/N.
    Tissue: Liver and Salivary gland.
  4. Cited for: SUBCELLULAR LOCATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCPIN1_MOUSE
AccessioniPrimary (citable) accession number: Q8WTY4
Secondary accession number(s): Q3UJW5, Q8VC24, Q91W83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

'Ana-mors-in' means 'anti-death molecule' in Latin.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.