ID   LLPH_HUMAN              Reviewed;         129 AA.
AC   Q9BRT6; Q3B766;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   17-JUN-2020, entry version 129.
DE   RecName: Full=Protein LLP homolog;
DE   AltName: Full=Protein LAPS18-like;
GN   Name=LLPH; Synonyms=C12orf31, cPERP-G {ECO:0000303|PubMed:20813266};
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=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney, and Skeletal muscle;
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   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA   Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA   Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA   Earnshaw W.C., Rappsilber J.;
RT   "The protein composition of mitotic chromosomes determined using
RT   multiclassifier combinatorial proteomics.";
RL   Cell 142:810-821(2010).
RN   [4]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-74, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [5]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [6]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-74, AND IDENTIFICATION
RP   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).
CC   -!- FUNCTION: In hippocampal neurons, regulates dendritic and spine growth
CC       and synaptic transmission. {ECO:0000250|UniProtKB:Q9D945}.
CC   -!- SUBUNIT: Interacts with CTCF, MYO1C and with the transcriptional
CC       machinery, including RNA polymerase II and TBP.
CC       {ECO:0000250|UniProtKB:Q9D945}.
CC   -!- INTERACTION:
CC       Q9BRT6; A0A494C108: KRI1; NbExp=3; IntAct=EBI-741396, EBI-12342761;
CC       Q9BRT6; Q8N8Y5: ZFP41; NbExp=3; IntAct=EBI-741396, EBI-12224489;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9D945}. Chromosome
CC       {ECO:0000269|PubMed:20813266}. Note=Cell-permeable protein. 22 hours
CC       after injection in the hippocampal area CA1, internalized by most cells
CC       at the injection site (By similarity). Localizes at the chromosome
CC       periphery during mitosis (PubMed:20813266).
CC       {ECO:0000250|UniProtKB:Q9D945, ECO:0000269|PubMed:20813266}.
CC   -!- SIMILARITY: Belongs to the learning-associated protein family.
CC       {ECO:0000305}.
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DR   EMBL; AK091568; BAC03699.1; -; mRNA.
DR   EMBL; BC006002; AAH06002.1; -; mRNA.
DR   EMBL; BC070232; AAH70232.1; -; mRNA.
DR   EMBL; BC107780; AAI07781.1; -; mRNA.
DR   CCDS; CCDS8974.1; -.
DR   RefSeq; NP_115714.1; NM_032338.3.
DR   SMR; Q9BRT6; -.
DR   BioGRID; 124024; 28.
DR   IntAct; Q9BRT6; 16.
DR   STRING; 9606.ENSP00000266604; -.
DR   iPTMnet; Q9BRT6; -.
DR   MetOSite; Q9BRT6; -.
DR   PhosphoSitePlus; Q9BRT6; -.
DR   BioMuta; LLPH; -.
DR   DMDM; 74732927; -.
DR   EPD; Q9BRT6; -.
DR   jPOST; Q9BRT6; -.
DR   MassIVE; Q9BRT6; -.
DR   MaxQB; Q9BRT6; -.
DR   PaxDb; Q9BRT6; -.
DR   PeptideAtlas; Q9BRT6; -.
DR   PRIDE; Q9BRT6; -.
DR   ProteomicsDB; 78829; -.
DR   Antibodypedia; 53204; 100 antibodies.
DR   Ensembl; ENST00000266604; ENSP00000266604; ENSG00000139233.
DR   Ensembl; ENST00000446587; ENSP00000437372; ENSG00000139233.
DR   GeneID; 84298; -.
DR   KEGG; hsa:84298; -.
DR   UCSC; uc010ssw.3; human.
DR   CTD; 84298; -.
DR   EuPathDB; HostDB:ENSG00000139233.6; -.
DR   GeneCards; LLPH; -.
DR   HGNC; HGNC:28229; LLPH.
DR   HPA; ENSG00000139233; Low tissue specificity.
DR   MIM; 616998; gene.
DR   neXtProt; NX_Q9BRT6; -.
DR   OpenTargets; ENSG00000139233; -.
DR   PharmGKB; PA164722116; -.
DR   eggNOG; KOG4811; Eukaryota.
DR   eggNOG; ENOG4111VT9; LUCA.
DR   GeneTree; ENSGT00390000012979; -.
DR   HOGENOM; CLU_134502_0_0_1; -.
DR   InParanoid; Q9BRT6; -.
DR   OMA; HCQEKTQ; -.
DR   OrthoDB; 1594400at2759; -.
DR   PhylomeDB; Q9BRT6; -.
DR   TreeFam; TF314654; -.
DR   BioGRID-ORCS; 84298; 165 hits in 778 CRISPR screens.
DR   ChiTaRS; LLPH; human.
DR   GenomeRNAi; 84298; -.
DR   Pharos; Q9BRT6; Tdark.
DR   PRO; PR:Q9BRT6; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9BRT6; protein.
DR   Bgee; ENSG00000139233; Expressed in adrenal tissue and 176 other tissues.
DR   ExpressionAtlas; Q9BRT6; baseline and differential.
DR   Genevisible; Q9BRT6; HS.
DR   GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0001099; F:basal RNA polymerase II transcription machinery binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0097484; P:dendrite extension; ISS:UniProtKB.
DR   GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:UniProtKB.
DR   InterPro; IPR018784; LAPS18-like.
DR   PANTHER; PTHR34253; PTHR34253; 1.
DR   Pfam; PF10169; Laps; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation.
FT   CHAIN           1..129
FT                   /note="Protein LLP homolog"
FT                   /id="PRO_0000274346"
FT   COMPBIAS        3..125
FT                   /note="Lys-rich"
FT   CROSSLNK        67
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447,
FT                   ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:28112733"
FT   CROSSLNK        74
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447,
FT                   ECO:0000244|PubMed:28112733"
FT   CONFLICT        76
FT                   /note="E -> G (in Ref. 2; AAI07781)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   129 AA;  15225 MW;  71C2CE6F79B63E4D CRC64;
     MAKSLRSKWK RKMRAEKRKK NAPKEASRLK SILKLDGDVL MKDVQEIATV VVPKPKHCQE
     KMQCEVKDEK DDMKMETDIK RNKKTLLDQH GQYPIWMNQR QRKRLKAKRE KRKGKSKAKA
     VKVAKGLAW
//