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Centrosomal protein of 19 kDa (Cep19)

 CEP19_HUMAN             Reviewed;         163 AA.
Q96LK0; B2RA74; Q96I48;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 2.
25-OCT-2017, entry version 103.
RecName: Full=Centrosomal protein of 19 kDa;
Short=Cep19;
Name=CEP19; Synonyms=C3orf34; ORFNames=HSD5;
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].
TISSUE=Testis;
Wang L.F., Zhang X.D., Miao S.Y., Gou D., Wang Y.;
"A new spermatogenesis-related gene.";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Testis;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=21399614; DOI=10.1038/emboj.2011.63;
Jakobsen L., Vanselow K., Skogs M., Toyoda Y., Lundberg E., Poser I.,
Falkenby L.G., Bennetzen M., Westendorf J., Nigg E.A., Uhlen M.,
Hyman A.A., Andersen J.S.;
"Novel asymmetrically localizing components of human centrosomes
identified by complementary proteomics methods.";
EMBO J. 30:1520-1535(2011).
[6]
INVOLVEMENT IN MOSPGF, AND SUBCELLULAR LOCATION.
PubMed=24268657; DOI=10.1016/j.ajhg.2013.10.025;
Shalata A., Ramirez M.C., Desnick R.J., Priedigkeit N., Buettner C.,
Lindtner C., Mahroum M., Abdul-Ghani M., Dong F., Arar N.,
Camacho-Vanegas O., Zhang R., Camacho S.C., Chen Y., Ibdah M.,
DeFronzo R., Gillespie V., Kelley K., Dynlacht B.D., Kim S.,
Glucksman M.J., Borochowitz Z.U., Martignetti J.A.;
"Morbid obesity resulting from inactivation of the ciliary protein
CEP19 in humans and mice.";
Am. J. Hum. Genet. 93:1061-1071(2013).
[7]
FUNCTION, INTERACTION WITH FGFR1OP AND RABL2B, SUBCELLULAR LOCATION,
AND PHYLOGENETIC ANALYSIS.
PubMed=28625565; DOI=10.1016/j.devcel.2017.05.016;
Kanie T., Abbott K.L., Mooney N.A., Plowey E.D., Demeter J.,
Jackson P.K.;
"The CEP19-RABL2 GTPase complex binds IFT-B to initiate intraflagellar
transport at the ciliary base.";
Dev. Cell 42:1-15(2017).
[8]
FUNCTION, INTERACTION WITH FGFR1OP AND RABL2B, AND SUBCELLULAR
LOCATION.
PubMed=28428259; DOI=10.1091/mbc.E17-01-0017;
Nishijima Y., Hagiya Y., Kubo T., Takei R., Katoh Y., Nakayama K.;
"RABL2 interacts with the intraflagellar transport-B complex and CEP19
and participates in ciliary assembly.";
Mol. Biol. Cell 28:1652-1666(2017).
[9]
FUNCTION, INTERACTION WITH FGFR1OP AND CEP350, AND SUBCELLULAR
LOCATION.
PubMed=28659385; DOI=10.1098/rsob.170114;
Mojarad B.A., Gupta G.D., Hasegan M., Goudiam O., Basto R.,
Gingras A.C., Pelletier L.;
"CEP19 cooperates with FOP and CEP350 to drive early steps in the
ciliogenesis programme.";
Open Biol. 7:0-0(2017).
-!- FUNCTION: Required for ciliation (PubMed:28625565,
PubMed:28428259, PubMed:28659385). Recruits the RABL2B GTPase to
the ciliary base to initiate ciliation. After specifically
capturing the activated GTP-bound RABL2B, the CEP19-RABL2B complex
binds intraflagellar transport (IFT) complex B from the large pool
pre-docked at the base of the cilium and thus triggers its entry
into the cilia (PubMed:28625565, PubMed:28428259). Involved in the
early steps in cilia formation by recruiting the ciliary vesicles
(CVs) to the distal end of the mother centriole where they fuse to
initiate cilium assembly. Involved in microtubule (MT) anchoring
to the centrosomes (PubMed:28659385).
{ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565,
ECO:0000269|PubMed:28659385}.
-!- SUBUNIT: Interacts with FGFR1OP; this interaction is required for
its localization to the mother centriole (PubMed:28625565,
PubMed:28428259, PubMed:28659385). Interacts (via residues 121-
150) with RABL2B (PubMed:28625565, PubMed:28428259). Interacts
(via C-terminus) with CEP350; this interaction is required for its
localization to the mother centriole (PubMed:28659385).
{ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565,
ECO:0000269|PubMed:28659385}.
-!- INTERACTION:
Q9P1Z2:CALCOCO1; NbExp=5; IntAct=EBI-741885, EBI-749920;
Q68D86:CCDC102B; NbExp=5; IntAct=EBI-741885, EBI-10171570;
P51861:CDR1; NbExp=4; IntAct=EBI-741885, EBI-2836538;
O95684:FGFR1OP; NbExp=6; IntAct=EBI-741885, EBI-1266334;
O95684-2:FGFR1OP; NbExp=4; IntAct=EBI-741885, EBI-1266347;
Q6PIV2:FOXR1; NbExp=4; IntAct=EBI-741885, EBI-10253815;
V9HW80:HEL-S-70; NbExp=3; IntAct=EBI-741885, EBI-10175326;
Q8N8K9:KIAA1958; NbExp=3; IntAct=EBI-741885, EBI-10181113;
Q9BQD3:KXD1; NbExp=6; IntAct=EBI-741885, EBI-739657;
Q9NRD5:PICK1; NbExp=4; IntAct=EBI-741885, EBI-79165;
Q92569:PIK3R3; NbExp=3; IntAct=EBI-741885, EBI-79893;
Q9UBK7-2:RABL2A; NbExp=3; IntAct=EBI-741885, EBI-4402837;
Q04864:REL; NbExp=3; IntAct=EBI-741885, EBI-307352;
Q8N205:SYNE4; NbExp=3; IntAct=EBI-741885, EBI-7131783;
O43829:ZBTB14; NbExp=5; IntAct=EBI-741885, EBI-10176632;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole
{ECO:0000269|PubMed:21399614, ECO:0000269|PubMed:28428259,
ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:21399614}. Cytoplasm, cytoskeleton, cilium
basal body {ECO:0000269|PubMed:24268657,
ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565,
ECO:0000269|PubMed:28659385}. Note=Associates with the mother
centriole in early interphase. Localizes to spindle poles during
mitosis, and to distinct foci oriented towards the midbody at
telophase (PubMed:21399614). Localizes slightly apical to the
subdistal appendage on the mother centriole, but below the distal
appendage (PubMed:28625565, PubMed:28659385).
{ECO:0000269|PubMed:21399614, ECO:0000269|PubMed:28625565}.
-!- DISEASE: Morbid obesity and spermatogenic failure (MOSPGF)
[MIM:615703]: An autosomal recessive morbid obesity syndrome
characterized by hypertension, fatty liver disease, insulin
resistance, and decreased sperm counts. Variable clinical
manifestations are early coronary artery disease with myocardial
infarction before 45 years of age, type II diabetes mellitus, and
intellectual disability. Morbid obese individuals are defined as
having a BMI greater than 40. {ECO:0000269|PubMed:24268657}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the CEP19 family. {ECO:0000305}.
-!- CAUTION: The region that interacts with FGFR1OP is conflicting:
According to a report, interacts via N-terminus (PubMed:28428259).
According to another report, interacts via C-terminus
(PubMed:28659385). {ECO:0000269|PubMed:28428259,
ECO:0000269|PubMed:28659385}.
-!- SEQUENCE CAUTION:
Sequence=AAM47487.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB71691.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AY099509; AAM47487.1; ALT_INIT; mRNA.
EMBL; AK058155; BAB71691.1; ALT_INIT; mRNA.
EMBL; AK314070; BAG36771.1; -; mRNA.
EMBL; AC055725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007827; AAH07827.1; -; mRNA.
RefSeq; NP_116287.2; NM_032898.4.
RefSeq; XP_005269427.1; XM_005269370.4.
RefSeq; XP_011511548.1; XM_011513246.2.
UniGene; Hs.282800; -.
ProteinModelPortal; Q96LK0; -.
BioGrid; 124410; 107.
IntAct; Q96LK0; 128.
MINT; MINT-1481099; -.
STRING; 9606.ENSP00000387209; -.
PhosphoSitePlus; Q96LK0; -.
BioMuta; CEP19; -.
DMDM; 115503728; -.
PaxDb; Q96LK0; -.
PeptideAtlas; Q96LK0; -.
PRIDE; Q96LK0; -.
DNASU; 84984; -.
Ensembl; ENST00000409690; ENSP00000387209; ENSG00000174007.
GeneID; 84984; -.
KEGG; hsa:84984; -.
UCSC; uc011btw.3; human.
CTD; 84984; -.
DisGeNET; 84984; -.
EuPathDB; HostDB:ENSG00000174007.7; -.
GeneCards; CEP19; -.
H-InvDB; HIX0003974; -.
HGNC; HGNC:28209; CEP19.
HPA; HPA047614; -.
HPA; HPA071138; -.
MalaCards; CEP19; -.
MIM; 615586; gene.
MIM; 615703; phenotype.
neXtProt; NX_Q96LK0; -.
Orphanet; 397615; Obesity due to CEP19 deficiency.
PharmGKB; PA142672395; -.
eggNOG; ENOG410IWEE; Eukaryota.
eggNOG; ENOG4111MS1; LUCA.
HOVERGEN; HBG081009; -.
InParanoid; Q96LK0; -.
KO; K16801; -.
OrthoDB; EOG091G0WDG; -.
PhylomeDB; Q96LK0; -.
TreeFam; TF328425; -.
GenomeRNAi; 84984; -.
PRO; PR:Q96LK0; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000174007; -.
CleanEx; HS_C3orf34; -.
ExpressionAtlas; Q96LK0; baseline and differential.
Genevisible; Q96LK0; HS.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
GO; GO:0005929; C:cilium; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:UniProtKB.
GO; GO:0097712; P:vesicle targeting, trans-Golgi to periciliary membrane compartment; IMP:UniProtKB.
InterPro; IPR029412; CEP19.
PANTHER; PTHR31539; PTHR31539; 2.
Pfam; PF14933; CEP19; 1.
1: Evidence at protein level;
Cell projection; Cilium; Cilium biogenesis/degradation;
Complete proteome; Cytoplasm; Cytoskeleton; Obesity;
Reference proteome.
CHAIN 1 163 Centrosomal protein of 19 kDa.
/FTId=PRO_0000251960.
SEQUENCE 163 AA; 19166 MW; D5F65C3C0A1B1AD7 CRC64;
MMCTAKKCGI RFQPPAIILI YESEIKGKIR QRIMPVRNFS KFSDCTRAAE QLKNNPRHKS
YLEQVSLRQL EKLFSFLRGY LSGQSLAETM EQIQRETTID PEEDLNKLDD KELAKRKSIM
DELFEKNQKK KDDPNFVYDI EVEFPQDDQL QSCGWDTESA DEF


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