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Protein moonraker (MNR) (OFD1- and FOPNL-interacting protein)

 MOONR_HUMAN             Reviewed;         967 AA.
Q2KHM9; A8KA11; B7Z479; O94853; Q05D97; Q2KHN0; Q9UG45;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
12-SEP-2018, entry version 91.
RecName: Full=Protein moonraker {ECO:0000303|PubMed:26297806};
Short=MNR {ECO:0000303|PubMed:26297806};
AltName: Full=OFD1- and FOPNL-interacting protein {ECO:0000303|PubMed:26643951};
Name=KIAA0753;
Synonyms=MNR {ECO:0000303|PubMed:26297806},
OFIP {ECO:0000303|PubMed:26643951};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:277-286(1998).
[2]
SEQUENCE REVISION.
Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS ASN-444; PRO-466 AND ARG-896.
TISSUE=Tongue, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS ASN-444; PRO-466 AND ARG-896.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 404-967, AND VARIANTS
ASN-444; PRO-466 AND ARG-896.
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287; SER-409; SER-700
AND SER-826, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[8]
FUNCTION, INTERACTION WITH CEP63, AND SUBCELLULAR LOCATION.
PubMed=24613305; DOI=10.1016/j.cub.2014.01.067;
Firat-Karalar E.N., Rauniyar N., Yates J.R. III, Stearns T.;
"Proximity interactions among centrosome components identify
regulators of centriole duplication.";
Curr. Biol. 24:664-670(2014).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WDR62 AND PCM1.
PubMed=26297806; DOI=10.7554/eLife.07519;
Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L.,
Al-Gazali L., Sztriha L., Partlow J.N., Kim H., Krup A.L.,
Dammermann A., Krogan N., Walsh C.A., Reiter J.F.;
"Centriolar satellites assemble centrosomal microcephaly proteins to
recruit CDK2 and promote centriole duplication.";
Elife 4:0-0(2015).
[10]
INVOLVEMENT IN OFD15, INTERACTION WITH FOPNL; OFD1 AND PCM1, AND
SUBCELLULAR LOCATION.
PubMed=26643951; DOI=10.1093/hmg/ddv488;
Chevrier V., Bruel A.L., Van Dam T.J., Franco B., Lo Scalzo M.,
Lembo F., Audebert S., Baudelet E., Isnardon D., Bole A., Borg J.P.,
Kuentz P., Thevenon J., Burglen L., Faivre L., Riviere J.B.,
Huynen M.A., Birnbaum D., Rosnet O., Thauvin-Robinet C.;
"OFIP/KIAA0753 forms a complex with OFD1 and FOR20 at pericentriolar
satellites and centrosomes and is mutated in one individual with oral-
facial-digital syndrome.";
Hum. Mol. Genet. 25:497-513(2016).
[11]
VARIANT GLY-257.
PubMed=28220259; DOI=10.1007/s00439-017-1765-z;
NISC Comparative Sequencing Program;
Stephen J., Vilboux T., Mian L., Kuptanon C., Sinclair C.M.,
Yildirimli D., Maynard D.M., Bryant J., Fischer R., Vemulapalli M.,
Mullikin J.C., Huizing M., Gahl W.A., Malicdan M.C.V., Gunay-Aygun M.;
"Mutations in KIAA0753 cause Joubert syndrome associated with growth
hormone deficiency.";
Hum. Genet. 136:399-408(2017).
-!- FUNCTION: Involved in centriole duplication. Positively regulates
CEP63 centrosomal localization. Required for WDR62 centrosomal
localization and promotes the centrosomal localization of CDK2
(PubMed:24613305, PubMed:26297806). {ECO:0000269|PubMed:26297806}.
-!- SUBUNIT: Interacts with CEP63 (PubMed:24613305). Interacts with
WDR62 (PubMed:26297806). Forms a complex with OFD1 and FOPNL/FOR20
(PubMed:26643951). Interacts with PCM1 (PubMed:26297806,
PubMed:26643951). {ECO:0000269|PubMed:24613305,
ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:26643951}.
-!- INTERACTION:
Q8WUE5:CT55; NbExp=3; IntAct=EBI-2805604, EBI-6873363;
Q3B820:FAM161A; NbExp=3; IntAct=EBI-2805604, EBI-719941;
Q96CN9:GCC1; NbExp=3; IntAct=EBI-2805604, EBI-746252;
A0A0S2Z4Q4:HGS; NbExp=3; IntAct=EBI-2805604, EBI-16429135;
Q15154:PCM1; NbExp=7; IntAct=EBI-2805604, EBI-741421;
A0A0S2Z4G9:RNF6; NbExp=3; IntAct=EBI-2805604, EBI-16428950;
Q9BT92:TCHP; NbExp=3; IntAct=EBI-2805604, EBI-740781;
D3DUQ6:TEAD4; NbExp=3; IntAct=EBI-2805604, EBI-10176734;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-2805604, EBI-739895;
O43379:WDR62; NbExp=3; IntAct=EBI-2805604, EBI-714790;
Q8NC26:ZNF114; NbExp=3; IntAct=EBI-2805604, EBI-10265237;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole
{ECO:0000269|PubMed:26643951}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriolar satellite
{ECO:0000269|PubMed:24613305, ECO:0000269|PubMed:26297806,
ECO:0000269|PubMed:26643951}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:26643951}.
Note=Localization to centrioles and pericentriolar satellites may
be mediated by interaction with PCM1.
{ECO:0000269|PubMed:26643951}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q2KHM9-1; Sequence=Displayed;
Name=2;
IsoId=Q2KHM9-2; Sequence=VSP_023539;
-!- DISEASE: Orofaciodigital syndrome 15 (OFD15) [MIM:617127]: A form
of orofaciodigital syndrome, a group of heterogeneous disorders
characterized by malformations of the oral cavity, face and
digits, and associated phenotypic abnormalities that lead to the
delineation of various subtypes. OFD15 features include facial
dysmorphism, lobulated tongue, clefting of the alveolar ridges,
left hand postaxial polydactyly, broad right hallux and left
hallux duplication, and intermittent respiratory difficulty. Brain
anomalies include vermis hypoplasia with molar tooth sign,
agenesis of corpus callosum, and ventricular dilation. OFD15
inheritance is autosomal recessive. {ECO:0000269|PubMed:26643951}.
Note=The disease may be caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAA34473.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB018296; BAA34473.2; ALT_INIT; mRNA.
EMBL; AK292876; BAF85565.1; -; mRNA.
EMBL; AK296971; BAH12465.1; -; mRNA.
EMBL; AC004706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC015916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC113016; AAI13017.1; -; mRNA.
EMBL; BC113017; AAI13018.1; -; mRNA.
EMBL; AL080108; CAB45712.1; -; mRNA.
CCDS; CCDS42247.1; -. [Q2KHM9-1]
CCDS; CCDS86564.1; -. [Q2KHM9-2]
PIR; T12550; T12550.
RefSeq; NP_055619.2; NM_014804.2. [Q2KHM9-1]
RefSeq; XP_006721675.1; XM_006721612.2. [Q2KHM9-2]
RefSeq; XP_016880945.1; XM_017025456.1.
UniGene; Hs.28070; -.
ProteinModelPortal; Q2KHM9; -.
BioGrid; 115185; 125.
CORUM; Q2KHM9; -.
DIP; DIP-61716N; -.
IntAct; Q2KHM9; 118.
STRING; 9606.ENSP00000355250; -.
iPTMnet; Q2KHM9; -.
PhosphoSitePlus; Q2KHM9; -.
BioMuta; KIAA0753; -.
DMDM; 296439322; -.
OGP; O94853; -.
EPD; Q2KHM9; -.
MaxQB; Q2KHM9; -.
PaxDb; Q2KHM9; -.
PeptideAtlas; Q2KHM9; -.
PRIDE; Q2KHM9; -.
ProteomicsDB; 61302; -.
ProteomicsDB; 61303; -. [Q2KHM9-2]
Ensembl; ENST00000361413; ENSP00000355250; ENSG00000198920. [Q2KHM9-1]
Ensembl; ENST00000572370; ENSP00000460050; ENSG00000198920. [Q2KHM9-2]
GeneID; 9851; -.
KEGG; hsa:9851; -.
UCSC; uc002gde.5; human. [Q2KHM9-1]
CTD; 9851; -.
DisGeNET; 9851; -.
EuPathDB; HostDB:ENSG00000198920.9; -.
GeneCards; KIAA0753; -.
HGNC; HGNC:29110; KIAA0753.
HPA; HPA023057; -.
HPA; HPA023494; -.
MalaCards; KIAA0753; -.
MIM; 617112; gene.
MIM; 617127; phenotype.
neXtProt; NX_Q2KHM9; -.
OpenTargets; ENSG00000198920; -.
PharmGKB; PA142671615; -.
eggNOG; ENOG410IKS4; Eukaryota.
eggNOG; ENOG410Z2QY; LUCA.
GeneTree; ENSGT00390000009714; -.
HOVERGEN; HBG081825; -.
InParanoid; Q2KHM9; -.
KO; K21765; -.
OMA; PASPKCA; -.
OrthoDB; EOG091G01P0; -.
PhylomeDB; Q2KHM9; -.
TreeFam; TF331402; -.
ChiTaRS; KIAA0753; human.
GenomeRNAi; 9851; -.
PRO; PR:Q2KHM9; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000198920; Expressed in 198 organ(s), highest expression level in lower esophagus.
CleanEx; HS_KIAA0753; -.
ExpressionAtlas; Q2KHM9; baseline and differential.
Genevisible; Q2KHM9; HS.
GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0007099; P:centriole replication; IEA:InterPro.
GO; GO:0071539; P:protein localization to centrosome; IMP:UniProtKB.
InterPro; IPR031447; MNR.
PANTHER; PTHR15732; PTHR15732; 1.
Pfam; PF15718; MNR; 1.
1: Evidence at protein level;
Alternative splicing; Ciliopathy; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 967 Protein moonraker.
/FTId=PRO_0000280109.
REGION 885 967 Necessary and sufficient for FOPNL-
binding. {ECO:0000269|PubMed:26643951}.
COILED 616 642 {ECO:0000255}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 700 700 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 826 826 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 299 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_023539.
VARIANT 201 201 H -> Q (in dbSNP:rs16955985).
/FTId=VAR_031065.
VARIANT 257 257 R -> G (found in two patients with
Joubert syndrome associated with GH
deficency; unknown pathological
significance).
{ECO:0000269|PubMed:28220259}.
/FTId=VAR_079381.
VARIANT 375 375 E -> D (in dbSNP:rs9889363).
/FTId=VAR_031066.
VARIANT 375 375 E -> G (in dbSNP:rs17794522).
/FTId=VAR_031067.
VARIANT 444 444 D -> N (in dbSNP:rs2289643).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_031068.
VARIANT 466 466 L -> P (in dbSNP:rs2289642).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_031069.
VARIANT 501 501 V -> M (in dbSNP:rs11868877).
/FTId=VAR_031070.
VARIANT 566 566 P -> L (in dbSNP:rs2304977).
/FTId=VAR_031071.
VARIANT 896 896 Q -> R (in dbSNP:rs1443417).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_031072.
CONFLICT 250 250 E -> K (in Ref. 3; BAF85565).
{ECO:0000305}.
CONFLICT 821 821 S -> G (in Ref. 1; BAA34473).
{ECO:0000305}.
SEQUENCE 967 AA; 109407 MW; 2245C5246165B8AA CRC64;
MGPGQPASTC VHLAPRTQLD GRSDPKVLQT QNQLQFNRNV PTHSSNLAIR YSCPHAIRIE
KLKHSYNESY HCKDADCRVG PDLGSSVSFS VISQERLSYA VHLARRDVKR RQFEKHIKEH
HLRSQPQSSQ KCGHTKYKIP DHRVERKESK SQAACQCSHQ PSKVEISSSG AKVYLYSSHP
GQSDLTVPNS PPTHDPGLQP HPRIGDHKNI SEQKSLLEVQ RLQKELSSCI HKIEEVTKKD
RLEEALDPDE ERRIRIRRQE QAARSARMLY VLQQQVKEIQ EELDKLSPHK IKHTKKSWAM
SKLAAAHRGA IRALQMFVTQ FTDRGEHPLP ARCKELGSLI RQLSLCSVKL DADPSVPDVV
IDILQQIEAL ESLLEKKLSP KKVKKCFSEI RSRFPIGSQK ALERWPSTSP KGERRPLTAK
DTFPQETSRP SVAKQLLADK YQPDTELPET QRLQSELDVL DADIVLEEGP FILDQSASFK
DEVLAVAKTK AGKKKPVTEN VPFRKKDTLA PARQQGLRKA ERGRQSQPHS KSRVQQTTVS
SRLKMNRQPV KDRKAPWIPP NPTSPPASPK CAAWLKVKTS PRDATKEPLQ QEDPQEESHL
TGAVEHEAAR LAWLDAETSK RLKELEELKA KEIDSMQKQR LDWLDAETSR RTKELNELKA
EEMYRLQQLS VSATHLADKV EEAVLDRLKP LLVKAQRVNS TTEANIHLKD GSSVNTAKAQ
PAQEVAAVDF ESNNIRQLDD FLEDCASELW AVTHAKILGS ETLATVEDSK DSPDLEIMMR
RMEEMEKYQE SVRQRYNKIA YADPRLWMQE ENNDQKISAI SEKPLSPHPI RITKTVDRKD
PAVNIMLERP CNGNSLDESV GTEEGSEKRE APLLSLAEDS QQKEGRAPLF VPPGMQHSIG
DYCSRFEQYL RIISHEAVGS FNPWLIAESF SEELVDEALG AVAAELQDMC EDYAEAVFTS
EFLEAAT


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EIAAB30253 Aip1,ALG-2-interacting protein 1,ALG-2-interacting protein X,Alix,E2F1-inducible protein,Eig2,Mouse,Mus musculus,Pdcd6ip,Programmed cell death 6-interacting protein
EIAAB07421 Cdc42-interacting protein 4,Cip4,Rat,Rattus norvegicus,Salt tolerant protein,Stp,Thyroid receptor-interacting protein 10,TR-interacting protein 10,Trip10,TRIP-10
EIAAB44012 Homo sapiens,Human,OIP1,OIP-1,Opa-interacting protein 1,Thyroid receptor-interacting protein 6,TR-interacting protein 6,TRIP6,TRIP-6,ZRP-1,Zyxin-related protein 1
EIAAB31033 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Miz1,Mouse,Msx-interacting zinc finger protein,Mus musculus,Pias2,Piasx,Protein inhibitor of act
EIAAB31032 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Miz1,Msx-interacting-zinc finger protein,Pias2,Piasx,Protein inhibitor of activated STAT x,Prote
EIAAB29754 Homo sapiens,HSPC218,Human,PABP-interacting protein 2,PAIP2,PAIP-2,PAIP2A,Poly(A)-binding protein-interacting protein 2,Polyadenylate-binding protein-interacting protein 2
EIAAB29748 Homo sapiens,Human,KIAA1155,PABP-interacting protein 2B,PAIP2B,PAIP-2B,Poly(A)-binding protein-interacting protein 2B,Polyadenylate-binding protein-interacting protein 2B
10-288-21983F Calcium and integrin-binding protein 1 - Calmyrin; DNA-PKcs-interacting protein; Kinase-interacting protein; KIP; CIB; SNK-interacting protein 2-28; SIP2-28 0.05 mg
10-288-21983F Calcium and integrin-binding protein 1 - Calmyrin; DNA-PKcs-interacting protein; Kinase-interacting protein; KIP; CIB; SNK-interacting protein 2-28; SIP2-28 0.1 mg
EIAAB29747 Kiaa1155,Mouse,Mus musculus,PABP-interacting protein 2B,Paip2b,PAIP-2B,Poly(A)-binding protein-interacting protein 2B,Polyadenylate-binding protein-interacting protein 2B
EIAAB32248 ADP-ribosylation factor-like protein 6-interacting protein 5,Aip-5,ARL-6-interacting protein 5,Arl6ip5,Glutamate transporter EAAC1-interacting protein,GTRAP3-18,Gtrap3-18,Jwa,PRA1 family protein 3,Pra
EIAAB29749 Homo sapiens,Human,PABP-interacting protein 1,PAIP1,PAIP-1,Poly(A)-binding protein-interacting protein 1,Polyadenylate-binding protein-interacting protein 1


 

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