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Protein FAM111A

 F111A_HUMAN             Reviewed;         611 AA.
Q96PZ2; A8K5Y8; Q5RKS9; Q5XKM2; Q68DK9; Q6IPR7; Q9H5Y1;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
27-SEP-2017, entry version 111.
RecName: Full=Protein FAM111A;
Name=FAM111A; Synonyms=KIAA1895;
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=Brain;
PubMed=11572484; DOI=10.1093/dnares/8.4.179;
Nagase T., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XXI.
The complete sequences of 60 new cDNA clones from brain which code for
large proteins.";
DNA Res. 8:179-187(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Ileal mucosa;
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 MRNA].
TISSUE=Uterine endothelium;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Testis;
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]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH SV40
VIRUS LARGE T ANTIGEN.
PubMed=23093934; DOI=10.1371/journal.ppat.1002949;
Fine D.A., Rozenblatt-Rosen O., Padi M., Korkhin A., James R.L.,
Adelmant G., Yoon R., Guo L., Berrios C., Zhang Y., Calderwood M.A.,
Velmurgan S., Cheng J., Marto J.A., Hill D.E., Cusick M.E., Vidal M.,
Florens L., Washburn M.P., Litovchick L., DeCaprio J.A.;
"Identification of FAM111A as an SV40 host range restriction and
adenovirus helper factor.";
PLoS Pathog. 8:E1002949-E1002949(2012).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[7]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA, AND MUTAGENESIS
OF 24-TYR-PHE-25.
PubMed=24561620; DOI=10.1038/ncb2918;
Alabert C., Bukowski-Wills J.C., Lee S.B., Kustatscher G.,
Nakamura K., de Lima Alves F., Menard P., Mejlvang J., Rappsilber J.,
Groth A.;
"Nascent chromatin capture proteomics determines chromatin dynamics
during DNA replication and identifies unknown fork components.";
Nat. Cell Biol. 16:281-293(2014).
[8]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-30 AND LYS-65, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[9]
VARIANTS KCS2 HIS-511 AND HIS-569, AND VARIANTS GCLEB ALA-338; SER-342
DEL; THR-527 AND GLY-528.
PubMed=23684011; DOI=10.1016/j.ajhg.2013.04.020;
Unger S., Gorna M.W., Le Bechec A., Do Vale-Pereira S., Bedeschi M.F.,
Geiberger S., Grigelioniene G., Horemuzova E., Lalatta F., Lausch E.,
Magnani C., Nampoothiri S., Nishimura G., Petrella D.,
Rojas-Ringeling F., Utsunomiya A., Zabel B., Pradervand S.,
Harshman K., Campos-Xavier B., Bonafe L., Superti-Furga G.,
Stevenson B., Superti-Furga A.;
"FAM111A mutations result in hypoparathyroidism and impaired skeletal
development.";
Am. J. Hum. Genet. 92:990-995(2013).
[10]
VARIANT KCS2 HIS-569.
PubMed=24635597; DOI=10.1111/cge.12290;
Nikkel S., Ahmed A., Smith A., Marcadier J., Bulman D., Boycott K.;
"Mother-to-daughter transmission of Kenny-Caffey syndrome associated
with the recurrent, dominant FAM111A mutation p.Arg569His.";
Clin. Genet. 86:394-395(2014).
[11]
VARIANT KCS2 HIS-569.
PubMed=23996431; DOI=10.1002/jbmr.2091;
Isojima T., Doi K., Mitsui J., Oda Y., Tokuhiro E., Yasoda A.,
Yorifuji T., Horikawa R., Yoshimura J., Ishiura H., Morishita S.,
Tsuji S., Kitanaka S.;
"A recurrent de novo FAM111A mutation causes kenny-caffey syndrome
type 2.";
J. Bone Miner. Res. 29:992-998(2014).
-!- FUNCTION: Chromatin-associated protein required for PCNA loading
on replication sites. Promotes S-phase entry and DNA synthesis
(PubMed:24561620). May directly function at replication forks,
explaining why Simian virus 40 (SV40) interacts with FAM111A to
overcome host range restriction (PubMed:23093934).
{ECO:0000269|PubMed:23093934, ECO:0000269|PubMed:24561620}.
-!- SUBUNIT: Interacts with PCNA; then interaction is direct.
Interacts with SV40 virus large T antigen and this interaction is
required for efficient viral replication and sustained viral gene
expression in restrictive cell types.
{ECO:0000269|PubMed:23093934, ECO:0000269|PubMed:24561620}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly localizes to
nucleus: colocalizes with PCNA on replication sites.
{ECO:0000269|PubMed:24561620}.
-!- INDUCTION: Regulated in a cell cycle dependent manner with the
lowest expression during G0 or the quiescent phase and with peak
expression during G2/M phase (at protein level).
{ECO:0000269|PubMed:23093934}.
-!- DOMAIN: The PIP-box mediates the interaction with PCNA.
{ECO:0000269|PubMed:24561620}.
-!- DISEASE: Kenny-Caffey syndrome 2 (KCS2) [MIM:127000]: A disorder
characterized by impaired skeletal development with small and
dense bones, short stature, and primary hypoparathyroidism with
hypocalcemia. Clinical features include cortical thickening and
medullary stenosis of the tubular bones, delayed closure of
fontanels, defective dentition, small eyes with hypermetropia, and
frontal bossing with a triangular face.
{ECO:0000269|PubMed:23684011, ECO:0000269|PubMed:23996431,
ECO:0000269|PubMed:24635597}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Gracile bone dysplasia (GCLEB) [MIM:602361]: A
perinatally lethal condition characterized by narrowing of the
medullary cavity of the long bones and of the skull, gracile bones
with thin diaphyses, premature closure of basal cranial sutures,
and microphthalmia. Most affected individuals who survive beyond
the perinatal period develop hypocalcemia with low parathyroid
hormone levels. {ECO:0000269|PubMed:23684011}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the FAM111 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB15486.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB67788.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB067482; BAB67788.1; ALT_INIT; mRNA.
EMBL; AK026447; BAB15486.1; ALT_INIT; mRNA.
EMBL; AK291453; BAF84142.1; -; mRNA.
EMBL; CR749358; CAH18211.1; -; mRNA.
EMBL; BC013137; AAH13137.1; -; mRNA.
EMBL; BC054515; AAH54515.1; -; mRNA.
EMBL; BC071759; AAH71759.1; -; mRNA.
CCDS; CCDS7973.1; -.
RefSeq; NP_001135991.1; NM_001142519.2.
RefSeq; NP_001135992.1; NM_001142520.2.
RefSeq; NP_001135993.1; NM_001142521.2.
RefSeq; NP_001299838.1; NM_001312909.1.
RefSeq; NP_001299839.1; NM_001312910.1.
RefSeq; NP_001299840.1; NM_001312911.1.
RefSeq; NP_071357.2; NM_022074.3.
RefSeq; NP_942144.1; NM_198847.2.
UniGene; Hs.150651; -.
ProteinModelPortal; Q96PZ2; -.
BioGrid; 121979; 5.
IntAct; Q96PZ2; 4.
iPTMnet; Q96PZ2; -.
PhosphoSitePlus; Q96PZ2; -.
BioMuta; FAM111A; -.
DMDM; 125991848; -.
EPD; Q96PZ2; -.
MaxQB; Q96PZ2; -.
PaxDb; Q96PZ2; -.
PeptideAtlas; Q96PZ2; -.
PRIDE; Q96PZ2; -.
Ensembl; ENST00000361723; ENSP00000355264; ENSG00000166801.
Ensembl; ENST00000420244; ENSP00000406683; ENSG00000166801.
Ensembl; ENST00000528737; ENSP00000434435; ENSG00000166801.
Ensembl; ENST00000531147; ENSP00000431631; ENSG00000166801.
Ensembl; ENST00000533703; ENSP00000433154; ENSG00000166801.
GeneID; 63901; -.
KEGG; hsa:63901; -.
UCSC; uc001nno.4; human.
CTD; 63901; -.
DisGeNET; 63901; -.
EuPathDB; HostDB:ENSG00000166801.15; -.
GeneCards; FAM111A; -.
H-InvDB; HIX0021067; -.
HGNC; HGNC:24725; FAM111A.
HPA; HPA039529; -.
HPA; HPA040176; -.
MalaCards; FAM111A; -.
MIM; 127000; phenotype.
MIM; 602361; phenotype.
MIM; 615292; gene.
neXtProt; NX_Q96PZ2; -.
OpenTargets; ENSG00000166801; -.
Orphanet; 93325; Autosomal dominant Kenny-Caffey syndrome.
Orphanet; 2763; Osteocraniostenosis.
PharmGKB; PA143485468; -.
eggNOG; ENOG410IH7H; Eukaryota.
eggNOG; ENOG410YPWU; LUCA.
GeneTree; ENSGT00390000005182; -.
HOVERGEN; HBG081494; -.
InParanoid; Q96PZ2; -.
OMA; MPLSCFP; -.
OrthoDB; EOG091G03VT; -.
PhylomeDB; Q96PZ2; -.
TreeFam; TF332538; -.
ChiTaRS; FAM111A; human.
GenomeRNAi; 63901; -.
PRO; PR:Q96PZ2; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000166801; -.
CleanEx; HS_FAM111A; -.
ExpressionAtlas; Q96PZ2; baseline and differential.
Genevisible; Q96PZ2; HS.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR009003; Peptidase_S1_PA.
SUPFAM; SSF50494; SSF50494; 2.
1: Evidence at protein level;
Antiviral defense; Complete proteome; Cytoplasm; Disease mutation;
DNA replication; Dwarfism; Host-virus interaction; Isopeptide bond;
Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 611 Protein FAM111A.
/FTId=PRO_0000274407.
REGION 336 611 Interaction with SV40 large T antigen.
MOTIF 16 28 PIP-box.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 20 20 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 30 30 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 65 65 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 338 338 T -> A (in GCLEB; dbSNP:rs587777014).
{ECO:0000269|PubMed:23684011}.
/FTId=VAR_069513.
VARIANT 342 342 Missing (in GCLEB).
{ECO:0000269|PubMed:23684011}.
/FTId=VAR_069514.
VARIANT 511 511 Y -> H (in KCS2; dbSNP:rs587777012).
{ECO:0000269|PubMed:23684011}.
/FTId=VAR_069515.
VARIANT 527 527 P -> T (in GCLEB; dbSNP:rs587777015).
{ECO:0000269|PubMed:23684011}.
/FTId=VAR_069516.
VARIANT 528 528 D -> G (in GCLEB; dbSNP:rs587777013).
{ECO:0000269|PubMed:23684011}.
/FTId=VAR_069517.
VARIANT 569 569 R -> H (in KCS2; dbSNP:rs587777011).
{ECO:0000269|PubMed:23684011,
ECO:0000269|PubMed:23996431,
ECO:0000269|PubMed:24635597}.
/FTId=VAR_069518.
MUTAGEN 24 25 YF->AA: In PIPmt; affects subcellular
localization. Impaired PCNA stability and
chromatin binding.
{ECO:0000269|PubMed:24561620}.
CONFLICT 97 97 T -> S (in Ref. 4; AAH71759).
{ECO:0000305}.
SEQUENCE 611 AA; 70196 MW; 97425E4198B809EA CRC64;
MSCKKQRSRK HSVNEKCNMK IEHYFSPVSK EQQNNCSTSL MRMESRGDPR ATTNTQAQRF
HSPKKNPEDQ TMPQNRTIYV TLKVNHRRNQ DMKLKLTHSE NSSLYMALNT LQAVRKEIET
HQGQEMLVRG TEGIKEYINL GMPLSCFPEG GQVVITFSQS KSKQKEDNHI FGRQDKASTE
CVKFYIHAIG IGKCKRRIVK CGKLHKKGRK LCVYAFKGET IKDALCKDGR FLSFLENDDW
KLIENNDTIL ESTQPVDELE GRYFQVEVEK RMVPSAAASQ NPESEKRNTC VLREQIVAQY
PSLKRESEKI IENFKKKMKV KNGETLFELH RTTFGKVTKN SSSIKVVKLL VRLSDSVGYL
FWDSATTGYA TCFVFKGLFI LTCRHVIDSI VGDGIEPSKW ATIIGQCVRV TFGYEELKDK
ETNYFFVEPW FEIHNEELDY AVLKLKENGQ QVPMELYNGI TPVPLSGLIH IIGHPYGEKK
QIDACAVIPQ GQRAKKCQER VQSKKAESPE YVHMYTQRSF QKIVHNPDVI TYDTEFFFGA
SGSPVFDSKG SLVAMHAAGF AYTYQNETRS IIEFGSTMES ILLDIKQRHK PWYEEVFVNQ
QDVEMMSDED L


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