F111A_HUMAN
ID F111A_HUMAN Reviewed; 611 AA.
AC Q96PZ2; A8K5Y8; Q5RKS9; Q5XKM2; Q68DK9; Q6IPR7; Q9H5Y1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Serine protease FAM111A {ECO:0000305};
DE EC=3.4.21.- {ECO:0000269|PubMed:32165630};
GN Name=FAM111A {ECO:0000303|PubMed:23093934, ECO:0000312|HGNC:HGNC:24725};
GN Synonyms=KIAA1895 {ECO:0000303|PubMed:11572484};
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].
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Ileal mucosa;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, 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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH SV40 VIRUS
RP LARGE T ANTIGEN (MICROBIAL INFECTION).
RX PubMed=23093934; DOI=10.1371/journal.ppat.1002949;
RA Fine D.A., Rozenblatt-Rosen O., Padi M., Korkhin A., James R.L.,
RA Adelmant G., Yoon R., Guo L., Berrios C., Zhang Y., Calderwood M.A.,
RA Velmurgan S., Cheng J., Marto J.A., Hill D.E., Cusick M.E., Vidal M.,
RA Florens L., Washburn M.P., Litovchick L., DeCaprio J.A.;
RT "Identification of FAM111A as an SV40 host range restriction and adenovirus
RT helper factor.";
RL PLoS Pathog. 8:E1002949-E1002949(2012).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA, AND MUTAGENESIS OF
RP 24-TYR-PHE-25.
RX PubMed=24561620; DOI=10.1038/ncb2918;
RA Alabert C., Bukowski-Wills J.C., Lee S.B., Kustatscher G., Nakamura K.,
RA de Lima Alves F., Menard P., Mejlvang J., Rappsilber J., Groth A.;
RT "Nascent chromatin capture proteomics determines chromatin dynamics during
RT DNA replication and identifies unknown fork components.";
RL Nat. Cell Biol. 16:281-293(2014).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-30 AND LYS-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF
RP 24-TYR-PHE-25; PHE-231; PHE-334 AND SER-541, CHARACTERIZATION OF VARIANTS
RP GCLEB SER-342 DEL AND GLY-528, AND CHARACTERIZATION OF VARIANTS KCS2
RP HIS-511 AND HIS-569.
RX PubMed=32165630; DOI=10.1038/s41467-020-15170-7;
RA Kojima Y., Machida Y., Palani S., Caulfield T.R., Radisky E.S.,
RA Kaufmann S.H., Machida Y.J.;
RT "FAM111A protects replication forks from protein obstacles via its trypsin-
RT like domain.";
RL Nat. Commun. 11:1318-1318(2020).
RN [10]
RP VARIANTS KCS2 HIS-511 AND HIS-569, AND VARIANTS GCLEB ALA-338; SER-342 DEL;
RP THR-527 AND GLY-528.
RX PubMed=23684011; DOI=10.1016/j.ajhg.2013.04.020;
RA Unger S., Gorna M.W., Le Bechec A., Do Vale-Pereira S., Bedeschi M.F.,
RA Geiberger S., Grigelioniene G., Horemuzova E., Lalatta F., Lausch E.,
RA Magnani C., Nampoothiri S., Nishimura G., Petrella D., Rojas-Ringeling F.,
RA Utsunomiya A., Zabel B., Pradervand S., Harshman K., Campos-Xavier B.,
RA Bonafe L., Superti-Furga G., Stevenson B., Superti-Furga A.;
RT "FAM111A mutations result in hypoparathyroidism and impaired skeletal
RT development.";
RL Am. J. Hum. Genet. 92:990-995(2013).
RN [11]
RP VARIANT KCS2 HIS-569.
RX PubMed=24635597; DOI=10.1111/cge.12290;
RA Nikkel S., Ahmed A., Smith A., Marcadier J., Bulman D., Boycott K.;
RT "Mother-to-daughter transmission of Kenny-Caffey syndrome associated with
RT the recurrent, dominant FAM111A mutation p.Arg569His.";
RL Clin. Genet. 86:394-395(2014).
RN [12]
RP VARIANT KCS2 HIS-569.
RX PubMed=23996431; DOI=10.1002/jbmr.2091;
RA Isojima T., Doi K., Mitsui J., Oda Y., Tokuhiro E., Yasoda A., Yorifuji T.,
RA Horikawa R., Yoshimura J., Ishiura H., Morishita S., Tsuji S., Kitanaka S.;
RT "A recurrent de novo FAM111A mutation causes kenny-caffey syndrome type
RT 2.";
RL J. Bone Miner. Res. 29:992-998(2014).
CC -!- FUNCTION: Single-stranded DNA-binding serine protease that mediates the
CC proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during
CC DNA synthesis, thereby playing a key role in maintaining genomic
CC integrity (PubMed:32165630). DPCs are highly toxic DNA lesions that
CC interfere with essential chromatin transactions, such as replication
CC and transcription, and which are induced by reactive agents, such as UV
CC light or formaldehyde (PubMed:32165630). Protects replication fork from
CC stalling by removing DPCs, such as covalently trapped topoisomerase 1
CC (TOP1) adducts on DNA lesion, or poly(ADP-ribose) polymerase 1 (PARP1)-
CC DNA complexes trapped by PARP inhibitors (PubMed:32165630). Required
CC for PCNA loading on replication sites (PubMed:24561620). Promotes S-
CC phase entry and DNA synthesis (PubMed:24561620).
CC {ECO:0000269|PubMed:24561620, ECO:0000269|PubMed:32165630}.
CC -!- FUNCTION: (Microbial infection) May directly function at replication
CC forks, explaining why Simian virus 40 (SV40) interacts with FAM111A to
CC overcome host range restriction. {ECO:0000269|PubMed:23093934}.
CC -!- SUBUNIT: Interacts (via PIP-box) with PCNA; then interaction is direct.
CC {ECO:0000269|PubMed:24561620}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 virus large T
CC antigen and this interaction is required for efficient viral
CC replication and sustained viral gene expression in restrictive cell
CC types. {ECO:0000269|PubMed:23093934}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23093934,
CC ECO:0000269|PubMed:24561620}. Chromosome {ECO:0000269|PubMed:24561620}.
CC Cytoplasm {ECO:0000269|PubMed:23093934}. Note=Mainly localizes to
CC nucleus: colocalizes with PCNA on replication sites.
CC {ECO:0000269|PubMed:24561620}.
CC -!- INDUCTION: Regulated in a cell cycle dependent manner with the lowest
CC expression during G0 or the quiescent phase and with peak expression
CC during G2/M phase (at protein level). {ECO:0000269|PubMed:23093934}.
CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA.
CC {ECO:0000269|PubMed:24561620}.
CC -!- PTM: Autocatalytically cleaved; activating the protein
CC (PubMed:32165630). Autocatalytic cleavage takes place in trans
CC (PubMed:32165630). {ECO:0000269|PubMed:32165630}.
CC -!- DISEASE: Kenny-Caffey syndrome 2 (KCS2) [MIM:127000]: A disorder
CC characterized by impaired skeletal development with small and dense
CC bones, short stature, and primary hypoparathyroidism with hypocalcemia.
CC Clinical features include cortical thickening and medullary stenosis of
CC the tubular bones, delayed closure of fontanels, defective dentition,
CC small eyes with hypermetropia, and frontal bossing with a triangular
CC face. {ECO:0000269|PubMed:23684011, ECO:0000269|PubMed:23996431,
CC ECO:0000269|PubMed:24635597, ECO:0000269|PubMed:32165630}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Gracile bone dysplasia (GCLEB) [MIM:602361]: A perinatally
CC lethal condition characterized by narrowing of the medullary cavity of
CC the long bones and of the skull, gracile bones with thin diaphyses,
CC premature closure of basal cranial sutures, and microphthalmia. Most
CC affected individuals who survive beyond the perinatal period develop
CC hypocalcemia with low parathyroid hormone levels.
CC {ECO:0000269|PubMed:23684011, ECO:0000269|PubMed:32165630}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the FAM111 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15486.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB67788.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB067482; BAB67788.1; ALT_INIT; mRNA.
DR EMBL; AK026447; BAB15486.1; ALT_INIT; mRNA.
DR EMBL; AK291453; BAF84142.1; -; mRNA.
DR EMBL; CR749358; CAH18211.1; -; mRNA.
DR EMBL; BC013137; AAH13137.1; -; mRNA.
DR EMBL; BC054515; AAH54515.1; -; mRNA.
DR EMBL; BC071759; AAH71759.1; -; mRNA.
DR CCDS; CCDS7973.1; -.
DR RefSeq; NP_001135991.1; NM_001142519.2.
DR RefSeq; NP_001135992.1; NM_001142520.2.
DR RefSeq; NP_001135993.1; NM_001142521.2.
DR RefSeq; NP_001299838.1; NM_001312909.1.
DR RefSeq; NP_001299839.1; NM_001312910.1.
DR RefSeq; NP_001299840.1; NM_001312911.1.
DR RefSeq; NP_071357.2; NM_022074.3.
DR RefSeq; NP_942144.1; NM_198847.2.
DR AlphaFoldDB; Q96PZ2; -.
DR BioGRID; 121979; 93.
DR IntAct; Q96PZ2; 8.
DR STRING; 9606.ENSP00000434435; -.
DR MEROPS; S01.530; -.
DR iPTMnet; Q96PZ2; -.
DR MetOSite; Q96PZ2; -.
DR PhosphoSitePlus; Q96PZ2; -.
DR BioMuta; FAM111A; -.
DR DMDM; 125991848; -.
DR EPD; Q96PZ2; -.
DR jPOST; Q96PZ2; -.
DR MassIVE; Q96PZ2; -.
DR MaxQB; Q96PZ2; -.
DR PaxDb; Q96PZ2; -.
DR PeptideAtlas; Q96PZ2; -.
DR PRIDE; Q96PZ2; -.
DR ProteomicsDB; 77794; -.
DR Antibodypedia; 27720; 48 antibodies from 12 providers.
DR DNASU; 63901; -.
DR Ensembl; ENST00000361723.7; ENSP00000355264.3; ENSG00000166801.17.
DR Ensembl; ENST00000420244.6; ENSP00000406683.1; ENSG00000166801.17.
DR Ensembl; ENST00000527629.6; ENSP00000436128.2; ENSG00000166801.17.
DR Ensembl; ENST00000528737.5; ENSP00000434435.1; ENSG00000166801.17.
DR Ensembl; ENST00000529985.3; ENSP00000502754.2; ENSG00000166801.17.
DR Ensembl; ENST00000531147.1; ENSP00000431631.1; ENSG00000166801.17.
DR Ensembl; ENST00000531408.6; ENSP00000432821.2; ENSG00000166801.17.
DR Ensembl; ENST00000533703.1; ENSP00000433154.1; ENSG00000166801.17.
DR Ensembl; ENST00000674617.1; ENSP00000501786.1; ENSG00000166801.17.
DR Ensembl; ENST00000675163.1; ENSP00000501952.1; ENSG00000166801.17.
DR Ensembl; ENST00000675806.2; ENSP00000501617.2; ENSG00000166801.17.
DR Ensembl; ENST00000676340.1; ENSP00000501909.1; ENSG00000166801.17.
DR Ensembl; ENST00000676459.1; ENSP00000501771.1; ENSG00000166801.17.
DR Ensembl; ENST00000682018.1; ENSP00000507215.1; ENSG00000166801.17.
DR GeneID; 63901; -.
DR KEGG; hsa:63901; -.
DR MANE-Select; ENST00000675163.1; ENSP00000501952.1; NM_001312909.2; NP_001299838.1.
DR UCSC; uc001nno.4; human.
DR CTD; 63901; -.
DR DisGeNET; 63901; -.
DR GeneCards; FAM111A; -.
DR HGNC; HGNC:24725; FAM111A.
DR HPA; ENSG00000166801; Low tissue specificity.
DR MalaCards; FAM111A; -.
DR MIM; 127000; phenotype.
DR MIM; 602361; phenotype.
DR MIM; 615292; gene.
DR neXtProt; NX_Q96PZ2; -.
DR OpenTargets; ENSG00000166801; -.
DR Orphanet; 93325; Autosomal dominant Kenny-Caffey syndrome.
DR Orphanet; 2763; Osteocraniostenosis.
DR PharmGKB; PA143485468; -.
DR VEuPathDB; HostDB:ENSG00000166801; -.
DR eggNOG; KOG0866; Eukaryota.
DR GeneTree; ENSGT00390000005182; -.
DR HOGENOM; CLU_022719_0_0_1; -.
DR InParanoid; Q96PZ2; -.
DR OMA; YIHAIGK; -.
DR OrthoDB; 470902at2759; -.
DR PhylomeDB; Q96PZ2; -.
DR TreeFam; TF332538; -.
DR PathwayCommons; Q96PZ2; -.
DR SignaLink; Q96PZ2; -.
DR BioGRID-ORCS; 63901; 10 hits in 1085 CRISPR screens.
DR ChiTaRS; FAM111A; human.
DR GenomeRNAi; 63901; -.
DR Pharos; Q96PZ2; Tbio.
DR PRO; PR:Q96PZ2; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96PZ2; protein.
DR Bgee; ENSG00000166801; Expressed in monocyte and 188 other tissues.
DR ExpressionAtlas; Q96PZ2; baseline and differential.
DR Genevisible; Q96PZ2; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IDA:UniProtKB.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Chromosome; Cytoplasm; Disease variant; DNA damage;
KW DNA repair; DNA replication; DNA-binding; Dwarfism; Host-virus interaction;
KW Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..611
FT /note="Serine protease FAM111A"
FT /id="PRO_0000274407"
FT REGION 44..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..611
FT /note="Interaction with SV40 large T antigen"
FT /evidence="ECO:0000269|PubMed:23093934"
FT MOTIF 16..28
FT /note="PIP-box"
FT /evidence="ECO:0000269|PubMed:24561620"
FT ACT_SITE 385
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P06681"
FT ACT_SITE 439
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P06681"
FT ACT_SITE 541
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:32165630"
FT SITE 334..335
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000305|PubMed:32165630"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 30
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 338
FT /note="T -> A (in GCLEB; dbSNP:rs587777014)"
FT /evidence="ECO:0000269|PubMed:23684011"
FT /id="VAR_069513"
FT VARIANT 342
FT /note="Missing (in GCLEB; enhanced autocatalytic cleavage)"
FT /evidence="ECO:0000269|PubMed:23684011,
FT ECO:0000269|PubMed:32165630"
FT /id="VAR_069514"
FT VARIANT 511
FT /note="Y -> H (in KCS2; enhanced autocatalytic cleavage;
FT dbSNP:rs587777012)"
FT /evidence="ECO:0000269|PubMed:23684011,
FT ECO:0000269|PubMed:32165630"
FT /id="VAR_069515"
FT VARIANT 527
FT /note="P -> T (in GCLEB; dbSNP:rs587777015)"
FT /evidence="ECO:0000269|PubMed:23684011"
FT /id="VAR_069516"
FT VARIANT 528
FT /note="D -> G (in GCLEB; enhanced autocatalytic cleavage;
FT dbSNP:rs587777013)"
FT /evidence="ECO:0000269|PubMed:23684011,
FT ECO:0000269|PubMed:32165630"
FT /id="VAR_069517"
FT VARIANT 569
FT /note="R -> H (in KCS2; enhanced autocatalytic cleavage;
FT dbSNP:rs587777011)"
FT /evidence="ECO:0000269|PubMed:23684011,
FT ECO:0000269|PubMed:23996431, ECO:0000269|PubMed:24635597,
FT ECO:0000269|PubMed:32165630"
FT /id="VAR_069518"
FT MUTAGEN 24..25
FT /note="YF->AA: In PIPmt; affects subcellular localization.
FT Impaired PCNA stability and chromatin binding. Does not
FT affect protease activity."
FT /evidence="ECO:0000269|PubMed:24561620,
FT ECO:0000269|PubMed:32165630"
FT MUTAGEN 231
FT /note="F->A: Strongly decreased single-stranded DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:32165630"
FT MUTAGEN 334
FT /note="F->R,G: Abolished autocatalytic cleavage."
FT /evidence="ECO:0000269|PubMed:32165630"
FT MUTAGEN 541
FT /note="S->A: Abolished protease activity."
FT /evidence="ECO:0000269|PubMed:32165630"
FT CONFLICT 97
FT /note="T -> S (in Ref. 4; AAH71759)"
FT /evidence="ECO:0000305"
SQ 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
