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PAX-interacting protein 1 (PAX transactivation activation domain-interacting protein)

 PAXI1_HUMAN             Reviewed;        1069 AA.
Q6ZW49; O15404; Q6N099; Q6ZWH9; Q7Z315; Q86UN0; Q8N4P9; Q96HP2;
24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
30-AUG-2017, entry version 116.
RecName: Full=PAX-interacting protein 1;
AltName: Full=PAX transactivation activation domain-interacting protein;
Name=PAXIP1; Synonyms=PAXIP1L, PTIP; ORFNames=CAGF28;
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] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-680 (ISOFORM 1).
TISSUE=Adrenal gland, Prostate, and Tongue;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
VAL-1013.
TISSUE=Rectum tumor, and Uterus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 202-1069.
TISSUE=Fetal brain;
PubMed=9225980; DOI=10.1007/s004390050476;
Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S.,
Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.;
"cDNAs with long CAG trinucleotide repeats from human brain.";
Hum. Genet. 100:114-122(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 244-1069.
TISSUE=Brain, 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).
[6]
FUNCTION.
PubMed=14576432; DOI=10.1126/science.1088877;
Manke I.A., Lowery D.M., Nguyen A., Yaffe M.B.;
"BRCT repeats as phosphopeptide-binding modules involved in protein
targeting.";
Science 302:636-639(2003).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TP53BP1.
PubMed=15456759; DOI=10.1074/jbc.M411021200;
Jowsey P.A., Doherty A.J., Rouse J.;
"Human PTIP facilitates ATM-mediated activation of p53 and promotes
cellular resistance to ionizing radiation.";
J. Biol. Chem. 279:55562-55569(2004).
[8]
FUNCTION IN MLL2 COMPLEX ASSEMBLY, AND IDENTIFICATION IN THE MLL2/3
COMPLEX.
PubMed=17925232; DOI=10.1016/j.devcel.2007.09.004;
Patel S.R., Kim D., Levitan I., Dressler G.R.;
"The BRCT-domain containing protein PTIP links PAX2 to a histone H3,
lysine 4 methyltransferase complex.";
Dev. Cell 13:580-592(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MLL2/3
COMPLEX.
PubMed=17500065; DOI=10.1074/jbc.M701574200;
Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
"PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
methyltransferase complex.";
J. Biol. Chem. 282:20395-20406(2007).
[10]
IDENTIFICATION IN THE MLL2 COMPLEX, AND ASSOCIATION WITH
KMT2D-REGULATED GENE PROMOTERS.
PubMed=17178841; DOI=10.1128/MCB.01506-06;
Issaeva I., Zonis Y., Rozovskaia T., Orlovsky K., Croce C.M.,
Nakamura T., Mazo A., Eisenbach L., Canaani E.;
"Knockdown of ALR (MLL2) reveals ALR target genes and leads to
alterations in cell adhesion and growth.";
Mol. Cell. Biol. 27:1889-1903(2007).
[11]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TP53BP1, AND
MUTAGENESIS OF TRP-676; ARG-910 AND TRP-929.
PubMed=17690115; DOI=10.1093/nar/gkm493;
Munoz I.M., Jowsey P.A., Toth R., Rouse J.;
"Phospho-epitope binding by the BRCT domains of hPTIP controls
multiple aspects of the cellular response to DNA damage.";
Nucleic Acids Res. 35:5312-5322(2007).
[12]
IDENTIFICATION IN THE MLL2/3 COMPLEX.
PubMed=17761849; DOI=10.1126/science.1149042;
Lee M.G., Villa R., Trojer P., Norman J., Yan K.P., Reinberg D.,
Di Croce L., Shiekhattar R.;
"Demethylation of H3K27 regulates polycomb recruitment and H2A
ubiquitination.";
Science 318:447-450(2007).
[13]
FUNCTION.
PubMed=18353733; DOI=10.1016/j.dnarep.2008.02.001;
Gohler T., Munoz I.M., Rouse J., Blow J.J.;
"PTIP/Swift is required for efficient PCNA ubiquitination in response
to DNA damage.";
DNA Repair 7:775-787(2008).
[14]
INTERACTION WITH HLTF.
PubMed=19723507; DOI=10.1016/j.bbrc.2009.08.151;
MacKay C., Toth R., Rouse J.;
"Biochemical characterisation of the SWI/SNF family member HLTF.";
Biochem. Biophys. Res. Commun. 390:187-191(2009).
[15]
FUNCTION.
PubMed=20088963; DOI=10.1111/j.1365-2443.2009.01379.x;
Wang X., Takenaka K., Takeda S.;
"PTIP promotes DNA double-strand break repair through homologous
recombination.";
Genes Cells 15:243-254(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
FUNCTION, AND INTERACTION WITH TP53BP1.
PubMed=23727112; DOI=10.1016/j.cell.2013.05.023;
Callen E., Di Virgilio M., Kruhlak M.J., Nieto-Soler M., Wong N.,
Chen H.T., Faryabi R.B., Polato F., Santos M., Starnes L.M.,
Wesemann D.R., Lee J.E., Tubbs A., Sleckman B.P., Daniel J.A., Ge K.,
Alt F.W., Fernandez-Capetillo O., Nussenzweig M.C., Nussenzweig A.;
"53BP1 mediates productive and mutagenic DNA repair through distinct
phosphoprotein interactions.";
Cell 153:1266-1280(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
-!- FUNCTION: Involved in DNA damage response and in transcriptional
regulation through histone methyltransferase (HMT) complexes.
Plays a role in early development. In DNA damage response is
required for cell survival after ionizing radiation. In vitro
shown to be involved in the homologous recombination mechanism for
the repair of double-strand breaks (DSBs). Its localization to DNA
damage foci requires RNF8 and UBE2N. Recruits TP53BP1 to DNA
damage foci and, at least in particular repair processes,
effective DNA damage response appears to require the association
with TP53BP1 phosphorylated by ATM at 'Ser-25'. Together with
TP53BP1 regulates ATM association. Proposed to recruit PAGR1 to
sites of DNA damage and the PAGR1:PAXIP1 complex is required for
cell survival in response to DNA damage; the function is probably
independent of MLL-containing histone methyltransferase (HMT)
complexes. However, this function has been questioned (By
similarity). Promotes ubiquitination of PCNA following UV
irradiation and may regulate recruitment of polymerase eta and
RAD51 to chromatin after DNA damage. Proposed to be involved in
transcriptional regulation by linking MLL-containing histone
methyltransferase (HMT) complexes to gene promoters by interacting
with promoter-bound transcription factors such as PAX2. Associates
with gene promoters that are known to be regulated by KMT2D/MLL2.
During immunoglobulin class switching in activated B-cells is
involved in trimethylation of histone H3 at 'Lys-4' and in
transcription initiation of downstream switch regions at the
immunoglobulin heavy-chain (Igh) locus; this function appears to
involve the recruitment of MLL-containing HMT complexes.
Conflictingly, its function in transcriptional regulation during
immunoglobulin class switching is reported to be independent of
the MLL2/MLL3 complex (By similarity).
{ECO:0000250|UniProtKB:Q6NZQ4, ECO:0000269|PubMed:14576432,
ECO:0000269|PubMed:15456759, ECO:0000269|PubMed:17690115,
ECO:0000269|PubMed:17925232, ECO:0000269|PubMed:18353733,
ECO:0000269|PubMed:20088963, ECO:0000269|PubMed:23727112}.
-!- SUBUNIT: Interacts with the C-terminal transactivation domain of
PAX2 (By similarity). Forms a constitutive complex with PAGR1
independently of the MLL2/MLL3 complex. Interacts with TP53BP1
(when phosphorylated at the N-terminus by ATM) (PubMed:15456759,
PubMed:17690115, PubMed:23727112). Interacts with HLTF. Component
of the KMT2 family MLL2/MLL3 complex (also named ASCOM complex),
at least composed of the HMTs KMT2D and/or KMT2C, the common
subunits ASH2L, RBBP5, WDR5 and DPY30, and the complex type-
specific subunits PAXIP1/PTIP, PAGR1, NCOA6 and KDM6A; required
for the association of PAGR1 with the MLL2/MLL3 complex.
{ECO:0000250|UniProtKB:Q6NZQ4, ECO:0000269|PubMed:15456759,
ECO:0000269|PubMed:17178841, ECO:0000269|PubMed:17500065,
ECO:0000269|PubMed:17690115, ECO:0000269|PubMed:17761849,
ECO:0000269|PubMed:17925232, ECO:0000269|PubMed:19723507,
ECO:0000269|PubMed:23727112}.
-!- INTERACTION:
Q9UBL3:ASH2L; NbExp=11; IntAct=EBI-743225, EBI-540797;
P16104:H2AFX; NbExp=7; IntAct=EBI-7521368, EBI-494830;
Q15555:MAPRE2; NbExp=3; IntAct=EBI-10236271, EBI-739717;
Q9UKK6:NXT1; NbExp=3; IntAct=EBI-10236271, EBI-301889;
Q9BTK6:PAGR1; NbExp=8; IntAct=EBI-743225, EBI-2372223;
Q96HA1:POM121; NbExp=3; IntAct=EBI-10236271, EBI-739990;
Q15291:RBBP5; NbExp=11; IntAct=EBI-743225, EBI-592823;
Q12888:TP53BP1; NbExp=4; IntAct=EBI-743225, EBI-396540;
P61964:WDR5; NbExp=8; IntAct=EBI-743225, EBI-540834;
-!- SUBCELLULAR LOCATION: Nucleus matrix
{ECO:0000250|UniProtKB:Q6NZQ4}. Chromosome
{ECO:0000269|PubMed:15456759, ECO:0000269|PubMed:17690115}.
Note=Localizes to DNA damage foci upon ionizing radiation.
{ECO:0000269|PubMed:15456759, ECO:0000269|PubMed:17690115}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q6ZW49-6; Sequence=Displayed;
Name=2;
IsoId=Q6ZW49-1; Sequence=VSP_040300;
Name=3;
IsoId=Q6ZW49-2; Sequence=VSP_040303;
Note=No experimental confirmation available.;
-!- DOMAIN: The BRCT 1 and 2 domains mediate the interaction with
PAGR1A. {ECO:0000250|UniProtKB:Q6NZQ4}.
-!- DOMAIN: The BRCT 5 and 6 domains mediate the association with the
MLL2/MLL3 complex (By similarity). The BRCT 5 and 6 domains
function as a single module and are necessary and sufficient for
in vitro phospho-specific binding (substrates phosphorylated by
the kinases ataxia telangiectasia-mutated (ATM), ataxia
telangiectasia and RAD3-related (ATR) in response to gamma
irradiation). In contrast, in vivo two pairs of BRCT domains (3-6)
bind to phosphorylated TP53BP1 much more efficiently.
{ECO:0000250|UniProtKB:Q6NZQ4}.
-!- CAUTION: The terminology of MLL proteins in mammalia is not
consistent also concerning the terminology of MLL protein-
containing complexes. The decribed MLL2/MLL3 complex is commonly
described as MLL3/MLL4 complex in literature. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB91434.1; Type=Frameshift; Positions=643, 662; Evidence={ECO:0000305};
Sequence=AAH33781.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH33781.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
Sequence=AAP21865.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAC85523.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AK123044; BAC85523.1; ALT_SEQ; mRNA.
EMBL; AK123600; BAC85657.1; -; mRNA.
EMBL; AK307417; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BX538201; CAD98066.1; -; mRNA.
EMBL; BX640616; CAE45762.1; -; mRNA.
EMBL; AC093726; AAP21865.1; ALT_SEQ; Genomic_DNA.
EMBL; U80735; AAB91434.1; ALT_FRAME; mRNA.
EMBL; BC008328; AAH08328.1; -; mRNA.
EMBL; BC033781; AAH33781.1; ALT_SEQ; mRNA.
CCDS; CCDS47753.1; -. [Q6ZW49-6]
RefSeq; NP_031375.3; NM_007349.3. [Q6ZW49-6]
RefSeq; XP_005249596.1; XM_005249539.1. [Q6ZW49-1]
RefSeq; XP_016867370.1; XM_017011881.1. [Q6ZW49-1]
UniGene; Hs.443881; -.
PDB; 3SQD; X-ray; 2.15 A; A/B=860-1069.
PDBsum; 3SQD; -.
ProteinModelPortal; Q6ZW49; -.
SMR; Q6ZW49; -.
BioGrid; 116625; 262.
DIP; DIP-41786N; -.
IntAct; Q6ZW49; 30.
MINT; MINT-276076; -.
STRING; 9606.ENSP00000384048; -.
iPTMnet; Q6ZW49; -.
PhosphoSitePlus; Q6ZW49; -.
BioMuta; PAXIP1; -.
DMDM; 317373316; -.
EPD; Q6ZW49; -.
MaxQB; Q6ZW49; -.
PaxDb; Q6ZW49; -.
PeptideAtlas; Q6ZW49; -.
PRIDE; Q6ZW49; -.
Ensembl; ENST00000397192; ENSP00000380376; ENSG00000157212. [Q6ZW49-6]
Ensembl; ENST00000404141; ENSP00000384048; ENSG00000157212. [Q6ZW49-6]
GeneID; 22976; -.
KEGG; hsa:22976; -.
UCSC; uc033aqm.2; human. [Q6ZW49-6]
CTD; 22976; -.
DisGeNET; 22976; -.
GeneCards; PAXIP1; -.
H-InvDB; HIX0007243; -.
HGNC; HGNC:8624; PAXIP1.
HPA; HPA006694; -.
HPA; HPA016950; -.
MalaCards; PAXIP1; -.
MIM; 608254; gene.
neXtProt; NX_Q6ZW49; -.
OpenTargets; ENSG00000157212; -.
PharmGKB; PA32964; -.
eggNOG; KOG2043; Eukaryota.
eggNOG; ENOG410XSGS; LUCA.
GeneTree; ENSGT00600000084454; -.
HOVERGEN; HBG061191; -.
InParanoid; Q6ZW49; -.
KO; K14972; -.
OMA; TFYGGDC; -.
OrthoDB; EOG091G0YK0; -.
PhylomeDB; Q6ZW49; -.
TreeFam; TF329580; -.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
SignaLink; Q6ZW49; -.
SIGNOR; Q6ZW49; -.
ChiTaRS; PAXIP1; human.
GeneWiki; PAXIP1; -.
GenomeRNAi; 22976; -.
PRO; PR:Q6ZW49; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000157212; -.
CleanEx; HS_PAXIP1; -.
ExpressionAtlas; Q6ZW49; baseline and differential.
Genevisible; Q6ZW49; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
GO; GO:0044666; C:MLL3/4 complex; IDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
GO; GO:0060717; P:chorion development; IEA:Ensembl.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
GO; GO:0035066; P:positive regulation of histone acetylation; ISS:UniProtKB.
GO; GO:0000416; P:positive regulation of histone H3-K36 methylation; ISS:UniProtKB.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISS:UniProtKB.
GO; GO:0045830; P:positive regulation of isotype switching; ISS:UniProtKB.
GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IEA:Ensembl.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
CDD; cd00027; BRCT; 4.
Gene3D; 3.40.50.10190; -; 6.
InterPro; IPR001357; BRCT_dom.
Pfam; PF00533; BRCT; 1.
Pfam; PF12738; PTCB-BRCT; 2.
Pfam; PF16770; RTT107_BRCT_5; 1.
SMART; SM00292; BRCT; 5.
SUPFAM; SSF52113; SSF52113; 5.
PROSITE; PS50172; BRCT; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosome; Complete proteome;
DNA damage; DNA recombination; DNA repair; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transcription;
Transcription regulation.
CHAIN 1 1069 PAX-interacting protein 1.
/FTId=PRO_0000296262.
DOMAIN 8 93 BRCT 1. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 94 183 BRCT 2. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 601 694 BRCT 3. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 703 779 BRCT 4. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 866 947 BRCT 5. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 970 1059 BRCT 6. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
REGION 94 183 Interaction with PAGR1. {ECO:0000250}.
REGION 590 1069 Interaction with TP53BP1.
MOTIF 702 719 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 223 250 Glu-rich.
COMPBIAS 406 624 Gln-rich.
MOD_RES 227 227 Phosphoserine.
{ECO:0000250|UniProtKB:Q6NZQ4}.
MOD_RES 235 235 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 247 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_040303.
VAR_SEQ 1 108 MSDQAPKVPEEMFREVKYYAVGDIDPQVIQLLKAGKAKEVS
YNALASHIISEDGDNPEVGEAREVFDLPVVKPSWVILSVQC
GTLLPVNGFSPESCQIFFGITACLSQ -> MVFLQNHVRFF
LESLPAFLRVLIQAGALCWSLPELSQGEVGKGACPAEVGKH
RDHLPSSDPVLMQAEASVVMCW (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040300.
VARIANT 1013 1013 M -> V (in dbSNP:rs3501).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_034627.
MUTAGEN 676 676 W->A: Abolishes interaction with TP53BP1;
prevents recruitment to DNA damage foci.
{ECO:0000269|PubMed:17690115}.
MUTAGEN 910 910 R->Q: Abolishes interaction with TP53BP1;
impairs intact cellular response to DNA
damage. {ECO:0000269|PubMed:17690115}.
MUTAGEN 929 929 W->A: Abolishes interaction with TP53BP1;
prevents recruitment to DNA damage foci.
{ECO:0000269|PubMed:17690115}.
CONFLICT 121 121 V -> D (in Ref. 1; AK307417).
{ECO:0000305}.
CONFLICT 154 154 K -> R (in Ref. 2; CAE45762).
{ECO:0000305}.
CONFLICT 260 260 Q -> H (in Ref. 2; CAE45762).
{ECO:0000305}.
CONFLICT 406 406 Missing (in Ref. 1; AK307417).
{ECO:0000305}.
CONFLICT 458 581 Missing (in Ref. 4; AAB91434).
{ECO:0000305}.
CONFLICT 847 847 K -> Q (in Ref. 4; AAB91434).
{ECO:0000305}.
CONFLICT 912 912 V -> L (in Ref. 4; AAB91434).
{ECO:0000305}.
CONFLICT 916 916 T -> A (in Ref. 4; AAB91434).
{ECO:0000305}.
HELIX 863 865 {ECO:0000244|PDB:3SQD}.
STRAND 868 871 {ECO:0000244|PDB:3SQD}.
HELIX 876 888 {ECO:0000244|PDB:3SQD}.
HELIX 897 899 {ECO:0000244|PDB:3SQD}.
STRAND 901 904 {ECO:0000244|PDB:3SQD}.
HELIX 912 917 {ECO:0000244|PDB:3SQD}.
TURN 918 920 {ECO:0000244|PDB:3SQD}.
STRAND 922 925 {ECO:0000244|PDB:3SQD}.
HELIX 927 936 {ECO:0000244|PDB:3SQD}.
HELIX 943 945 {ECO:0000244|PDB:3SQD}.
HELIX 950 955 {ECO:0000244|PDB:3SQD}.
HELIX 960 969 {ECO:0000244|PDB:3SQD}.
TURN 972 975 {ECO:0000244|PDB:3SQD}.
STRAND 976 980 {ECO:0000244|PDB:3SQD}.
HELIX 988 997 {ECO:0000244|PDB:3SQD}.
STRAND 1001 1005 {ECO:0000244|PDB:3SQD}.
HELIX 1009 1017 {ECO:0000244|PDB:3SQD}.
STRAND 1023 1028 {ECO:0000244|PDB:3SQD}.
HELIX 1030 1036 {ECO:0000244|PDB:3SQD}.
HELIX 1037 1041 {ECO:0000244|PDB:3SQD}.
HELIX 1050 1058 {ECO:0000244|PDB:3SQD}.
TURN 1063 1065 {ECO:0000244|PDB:3SQD}.
SEQUENCE 1069 AA; 121341 MW; 78CD535A150E1FC1 CRC64;
MSDQAPKVPE EMFREVKYYA VGDIDPQVIQ LLKAGKAKEV SYNALASHII SEDGDNPEVG
EAREVFDLPV VKPSWVILSV QCGTLLPVNG FSPESCQIFF GITACLSQVS SEDRSALWAL
VTFYGGDCQL TLNKKCTHLI VPEPKGEKYE CALKRASIKI VTPDWVLDCV SEKTKKDEAF
YHPRLIIYEE EEEEEEEEEE VENEEQDSQN EGSTDEKSSP ASSQEGSPSG DQQFSPKSNT
EKSKGELMFD DSSDSSPEKQ ERNLNWTPAE VPQLAAAKRR LPQGKEPGLI NLCANVPPVP
GNILPPEVRG NLMAAGQNLQ SSERSEMIAT WSPAVRTLRN ITNNADIQQM NRPSNVAHIL
QTLSAPTKNL EQQVNHSQQG HTNANAVLFS QVKVTPETHM LQQQQQAQQQ QQQHPVLHLQ
PQQIMQLQQQ QQQQISQQPY PQQPPHPFSQ QQQQQQQAHP HQFSQQQLQF PQQQLHPPQQ
LHRPQQQLQP FQQQHALQQQ FHQLQQHQLQ QQQLAQLQQQ HSLLQQQQQQ QIQQQQLQRM
HQQQQQQQMQ SQTAPHLSQT SQALQHQVPP QQPPQQQQQQ QPPPSPQQHQ LFGHDPAVEI
PEEGFLLGCV FAIADYPEQM SDKQLLATWK RIIQAHGGTV DPTFTSRCTH LLCESQVSSA
YAQAIRERKR CVTAHWLNTV LKKKKMVPPH RALHFPVAFP PGGKPCSQHI ISVTGFVDSD
RDDLKLMAYL AGAKYTGYLC RSNTVLICKE PTGLKYEKAK EWRIPCVNAQ WLGDILLGNF
EALRQIQYSR YTAFSLQDPF APTQHLVLNL LDAWRVPLKV SAELLMSIRL PPKLKQNEVA
NVQPSSKRAR IEDVPPPTKK LTPELTPFVL FTGFEPVQVQ QYIKKLYILG GEVAESAQKC
THLIASKVTR TVKFLTAISV VKHIVTPEWL EECFRCQKFI DEQNYILRDA EAEVLFSFSL
EESLKRAHVS PLFKAKYFYI TPGICPSLST MKAIVECAGG KVLSKQPSFR KLMEHKQNSS
LSEIILISCE NDLHLCREYF ARGIDVHNAE FVLTGVLTQT LDYESYKFN


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