DLGP5_MOUSE
ID DLGP5_MOUSE Reviewed; 808 AA.
AC Q8K4R9; Q6ZQL3; Q80VS7; Q8BUC8; Q8BZ79;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Disks large-associated protein 5;
DE Short=DAP-5;
DE AltName: Full=Discs large homolog 7;
DE AltName: Full=Disks large-associated protein DLG7;
DE AltName: Full=Hepatoma up-regulated protein homolog;
DE Short=HURP;
GN Name=Dlgap5; Synonyms=Dlg7, Kiaa0008;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB97377.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=12527899; DOI=10.1038/sj.onc.1206129;
RA Tsou A.-P., Yang C.-W., Huang C.-Y.F., Yu R.C.-T., Lee Y.-C.G.,
RA Chang C.-W., Chen B.-R., Chung Y.-F., Fann M.-J., Chi C.-W., Chiu J.-H.,
RA Chou C.-K.;
RT "Identification of a novel cell cycle regulated gene, HURP, overexpressed
RT in human hepatocellular carcinoma.";
RL Oncogene 22:298-307(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Bone, and Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC97842.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail {ECO:0000312|EMBL:BAC97842.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH58087.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH58087.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH58087.1}, and
RC Mammary gland {ECO:0000312|EMBL:AAH43924.1};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-328, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Potential cell cycle regulator that may play a role in
CC carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the
CC ubiquitin-proteasome pathway. Key regulator of adherens junction
CC integrity and differentiation that may be involved in CDH1-mediated
CC adhesion and signaling in epithelial cells (By similarity).
CC {ECO:0000250|UniProtKB:Q15398}.
CC -!- SUBUNIT: Interacts with CDC2. Interacts with the C-terminal proline-
CC rich region of FBXO7. Recruited by FBXO7 to a SCF (SKP1-CUL1-F-box)
CC protein complex in a CDC2/Cyclin B-phosphorylation dependent manner.
CC Interacts with CDH1 (By similarity). {ECO:0000250|UniProtKB:Q15398}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to the
CC spindle in mitotic cells. Colocalizes with CDH1 at sites of cell-cell
CC contact in intestinal epithelial cells (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:12527899};
CC IsoId=Q8K4R9-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q8K4R9-2; Sequence=VSP_051827, VSP_051828;
CC Name=3 {ECO:0000305};
CC IsoId=Q8K4R9-3; Sequence=VSP_051825, VSP_051826;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in normal resting liver.
CC Up-regulated in regenerating liver after partial hepatectomy.
CC {ECO:0000269|PubMed:12527899}.
CC -!- PTM: Ubiquitinated, leading to its degradation. {ECO:0000250}.
CC -!- PTM: Decreased phosphorylation levels are associated with the
CC differentiation of intestinal epithelial cells.
CC {ECO:0000250|UniProtKB:Q15398}.
CC -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97842.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB076696; BAB97377.1; -; mRNA.
DR EMBL; AK036384; BAC29405.1; -; mRNA.
DR EMBL; AK085882; BAC39560.1; -; mRNA.
DR EMBL; AK129032; BAC97842.1; ALT_INIT; mRNA.
DR EMBL; BC043924; AAH43924.1; -; mRNA.
DR EMBL; BC058087; AAH58087.1; -; mRNA.
DR CCDS; CCDS26987.1; -. [Q8K4R9-1]
DR RefSeq; NP_653136.2; NM_144553.2.
DR AlphaFoldDB; Q8K4R9; -.
DR SMR; Q8K4R9; -.
DR BioGRID; 230090; 2.
DR IntAct; Q8K4R9; 2.
DR STRING; 10090.ENSMUSP00000040416; -.
DR iPTMnet; Q8K4R9; -.
DR PhosphoSitePlus; Q8K4R9; -.
DR EPD; Q8K4R9; -.
DR jPOST; Q8K4R9; -.
DR MaxQB; Q8K4R9; -.
DR PaxDb; Q8K4R9; -.
DR PeptideAtlas; Q8K4R9; -.
DR PRIDE; Q8K4R9; -.
DR ProteomicsDB; 277465; -. [Q8K4R9-1]
DR ProteomicsDB; 277466; -. [Q8K4R9-2]
DR ProteomicsDB; 277467; -. [Q8K4R9-3]
DR DNASU; 218977; -.
DR GeneID; 218977; -.
DR KEGG; mmu:218977; -.
DR CTD; 9787; -.
DR MGI; MGI:2183453; Dlgap5.
DR eggNOG; KOG3971; Eukaryota.
DR InParanoid; Q8K4R9; -.
DR OrthoDB; 566337at2759; -.
DR PhylomeDB; Q8K4R9; -.
DR TreeFam; TF321382; -.
DR BioGRID-ORCS; 218977; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Dlgap5; mouse.
DR PRO; PR:Q8K4R9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K4R9; protein.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031616; C:spindle pole centrosome; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051382; P:kinetochore assembly; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; IEA:InterPro.
DR InterPro; IPR005026; SAPAP.
DR PANTHER; PTHR12353; PTHR12353; 1.
DR Pfam; PF03359; GKAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..808
FT /note="Disks large-associated protein 5"
FT /id="PRO_0000174300"
FT REGION 134..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 88..119
FT /evidence="ECO:0000255"
FT COMPBIAS 136..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 386
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 607
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 617
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 728
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 743
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 797
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15398"
FT VAR_SEQ 606..627
FT /note="LSSERRSQRFGTPLSASKVVPE -> CSFAETEERCLGQLGAGVNGGE (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051825"
FT VAR_SEQ 628..808
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051826"
FT VAR_SEQ 758
FT /note="V -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_051827"
FT VAR_SEQ 759..808
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_051828"
FT CONFLICT 165
FT /note="I -> M (in Ref. 3; BAC97842)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="P -> L (in Ref. 1; BAB97377)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="N -> D (in Ref. 4; AAH43924)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="G -> A (in Ref. 2; BAC29405/BAC39560 and 4;
FT AAH58087)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="L -> Q (in Ref. 2; BAC29405/BAC39560 and 4;
FT AAH58087)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="L -> Q (in Ref. 2; BAC29405)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="S -> P (in Ref. 2; BAC29405/BAC39560 and 4;
FT AAH58087)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="D -> E (in Ref. 3; BAC97842 and 4; AAH43924)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="T -> N (in Ref. 2; BAC29405/BAC39560 and 4;
FT AAH58087)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="M -> N (in Ref. 3; BAC97842 and 4; AAH43924)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="T -> S (in Ref. 2; BAC39560 and 4; AAH58087)"
FT /evidence="ECO:0000305"
FT CONFLICT 808
FT /note="L -> LRP (in Ref. 4; AAH43924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 808 AA; 90196 MW; 9F9B0EBA3CCF705C CRC64;
MLVSRFASRF RKDSSTEMVR TNLAHRKSLS QKENRHRVYE RNRHFGLKDV NIPLEGRELG
NIHETSQDLS PEKASSKTRS VKMVLSDQRK QLLQKYKEEK QLQKLKEQRE KAKRGVFKVG
LYRPAAPGFL VTDQRGAKAE PEKAFPHTGR ITRSKTKEYM EQTKIGSRNV PKATQSDQRQ
TSEKQPLDRE RKVMQPVLFT SGKGTESAAT QRAKLMARTV SSTTRKPVTR ATNEKGSERM
RPSGGRPAKK PEGKPDKVIP SKVERDEKHL DSQTRETSEM GPLGVFREVE SLPATAPAQG
KERKSFAPKH CVFQPPCGLK SYQVAPLSPR SANAFLTPNC DWNQLRPEVF STTTQDKANE
ILVQQGLESL TDRSKEHVLN QKGASTSDSN HASVKGVPCS EGSEGQTSQP PHDVPYFRKI
LQSETDRLTS HCLEWEGKLD LDISDEAKGL IRTTVGQTRL LIKERFRQFE GLVDNCEYKR
GEKETTCTDL DGFWDMVSFQ VDDVNQKFNN LIKLEASGWK DSNNPSKKVL RKKIVPGRTS
KAKQDDDGRA AARSRLAAIK NAMKGRPQQE VQAHAAAPET TKEVDKIVFD AGFFRIESPV
KSFSVLSSER RSQRFGTPLS ASKVVPEGRA AGDLLRQKMP LKKPDPQSSK SEHVDRTFSD
GLESRCHVED TPCPGEQDSS DIEHDVNKIN VKMDCFSVET NLPLPAGDAN TNQKEAISAV
EGASTAVTSQ DLLMSNPETN TSSQSNTSQE EAEASQSVLL HKSLTSECHL LEPPGLSCTS
PCTREETRQP DRSRQFSFGG DLILFSPL
