ID   ARIP4_HUMAN             Reviewed;        1467 AA.
AC   Q9Y4B4; Q8TB57; Q9BV54;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 4.
DT   05-OCT-2010, entry version 71.
DE   RecName: Full=Helicase ARIP4;
DE            EC=3.6.4.12;
DE   AltName: Full=Androgen receptor-interacting protein 4;
DE   AltName: Full=RAD54-like protein 2;
GN   Name=RAD54L2; Synonyms=ARIP4, KIAA0809;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 83-1467.
RC   TISSUE=Brain;
RX   MEDLINE=99087487; PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XI.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 5:277-286(1998).
RN   [3]
RP   SEQUENCE REVISION.
RX   MEDLINE=22158633; PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-1467.
RC   TISSUE=Eye, and Placenta;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-188; SER-189;
RP   SER-191; SER-1169 AND SER-1172, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1138, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1169 AND SER-1172, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1260, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1169 AND SER-1172, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
CC   -!- FUNCTION: DNA helicase that modulates androgen receptor (AR)-
CC       dependent transactivation in a promoter-dependent manner. Not able
CC       to remodel mononucleosomes in vitro (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- ENZYME REGULATION: Enzyme activity is enhanced by dsDNA (double-
CC       stranded DNA) and ssDNA (single-stranded DNA) (By similarity).
CC   -!- SUBUNIT: Interacts with AR via its N-terminus. Interacts with
CC       DYRK1A. Binds DNA and mononucleosomes, but does not seem to form
CC       large multiprotein complexes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Localizes in
CC       speckle-like nuclear compartments (By similarity).
CC   -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to be
CC       important for the association with nuclear receptors (By
CC       similarity).
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH24298.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AC099050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB018352; BAA34529.2; -; mRNA.
DR   EMBL; BC001474; AAH01474.2; -; mRNA.
DR   EMBL; BC024298; AAH24298.1; ALT_INIT; mRNA.
DR   IPI; IPI00294787; -.
DR   RefSeq; NP_055921.2; -.
DR   UniGene; Hs.105399; -.
DR   HSSP; Q97XQ5; 1Z63.
DR   ProteinModelPortal; Q9Y4B4; -.
DR   SMR; Q9Y4B4; 261-913.
DR   IntAct; Q9Y4B4; 4.
DR   MINT; MINT-3086380; -.
DR   STRING; Q9Y4B4; -.
DR   PhosphoSite; Q9Y4B4; -.
DR   PRIDE; Q9Y4B4; -.
DR   Ensembl; ENST00000409535; ENSP00000386520; ENSG00000164080.
DR   GeneID; 23132; -.
DR   KEGG; hsa:23132; -.
DR   UCSC; uc003dbi.2; human.
DR   CTD; 23132; -.
DR   GeneCards; GC03P051637; -.
DR   HGNC; HGNC:29123; RAD54L2.
DR   HOGENOM; HBG506597; -.
DR   HOVERGEN; HBG104283; -.
DR   InParanoid; Q9Y4B4; -.
DR   NextBio; 44383; -.
DR   ArrayExpress; Q9Y4B4; -.
DR   Bgee; Q9Y4B4; -.
DR   CleanEx; HS_RAD54L2; -.
DR   Genevestigator; Q9Y4B4; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR001650; helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Repeat;
KW   Ubl conjugation.
FT   CHAIN         1   1467       Helicase ARIP4.
FT                                /FTId=PRO_0000315781.
FT   DOMAIN      292    512       Helicase ATP-binding.
FT   DOMAIN      728    896       Helicase C-terminal.
FT   NP_BIND     305    312       ATP (By similarity).
FT   MOTIF       463    466       DEAH box.
FT   MOTIF       551    555       LXXLL motif 1.
FT   MOTIF      1329   1333       LXXLL motif 2.
FT   MOD_RES     187    187       Phosphoserine.
FT   MOD_RES     188    188       Phosphoserine.
FT   MOD_RES     189    189       Phosphoserine.
FT   MOD_RES     191    191       Phosphoserine.
FT   MOD_RES    1138   1138       Phosphoserine.
FT   MOD_RES    1169   1169       Phosphoserine.
FT   MOD_RES    1172   1172       Phosphoserine.
FT   MOD_RES    1260   1260       Phosphothreonine.
FT   VARIANT    1369   1369       F -> L (in dbSNP:rs35712917).
FT                                /FTId=VAR_038302.
FT   CONFLICT    123    123       E -> Q (in Ref. 2; BAA34529).
FT   CONFLICT    249    249       L -> F (in Ref. 4; AAH24298).
FT   CONFLICT    328    328       A -> V (in Ref. 2; BAA34529).
FT   CONFLICT    860    860       Y -> F (in Ref. 4; AAH01474).
SQ   SEQUENCE   1467 AA;  162769 MW;  9B4144B6BBC4C3B1 CRC64;
     MSDESASGSD PDLDPDVELE DAEEEEEEEE VAVEECDRDD EEDLLDDPSL EGMCGTEHAQ
     LGEDGQQPPR CTSTTSSQSE PSEQLRRHQG KNLASEDPKK KRAQKPSHMR RNIRKLLRED
     QLEPVTKAAQ QEELERRKRL EQQRKDYAAP IPTVPLEFLP EEIALRASDG PQLPPRVLAQ
     EVICLDSSSG SEDEKSSRDE VIELSSGEED TLHIVDSSES VSEDDEEEEK GGTHVNDVLN
     QRDALGRVLV NLNHPPEEEN VFLAPQLARA VKPHQIGGIR FLYDNLVESL ERFKTSSGFG
     CILAHSMGLG KTLQVISFID VLFRHTPAKT VLAIVPVNTL QNWLAEFNMW LPPPEALPAD
     NKPEEVQPRF FKVHILNDEH KTMASRAKVM ADWVSEGGVL LMGYEMYRLL TLKKSFATGR
     PKKTKKRSHP VIIDLDEEDR QQEFRREFEK ALCRPGPDVV ICDEGHRIKN CQASTSQALK
     NIRSRRRVVL TGYPLQNNLI EYWCMVDFVR PDFLGTRQEF SNMFERPILN GQCIDSTPQD
     VRLMRYRSHV LHSLLEGFVQ RRGHTVLKIH LPAKEENVIL VRLSKIQRDL YTQFMDRFRD
     CGSSGWLGLN PLKAFCVCCK IWNHPDVLYE ALQKESLANE QDLDVEELGS AGTSARCPPQ
     GTKGKGEDST LASSMGEATN SKFLQGVGFN PFQERGNNIV TYEWAKDLLT NYQTGVLENS
     PKMVLLFHLI EESVKLGDKI LVFSQSLSTL ALIEEFLGKR EVPCPPGTEG QGAQKWVRNI
     SYFRLDGSTP AFERERLINQ FNDPSNLTTW LFLLSTRAGC LGVNLIGANR VVVFDASWNP
     CHDAQAVCRV YRYGQKKPCY IYRLVADYTL EKKIYDRQIS KQGMSDRVVD DLNPMLNFTR
     KEVENLLHFV EKEPAPQVSL NVKGIKESVL QLACLKYPHL ITKEPFEHES LLLNRKDHKL
     TKAEKKAAKK SYEEDKRTSV PYTRPSYAQY YPASDQSLTS IPAFSQRNWQ PTLKGDEKPV
     ASVRPVQSTP IPMMPRHVPL GGSVSSASST NPSMNFPINY LQRAGVLVQK VVTTTDIVIP
     GLNSSTDVQA RINAGESIHI IRGTKGTYIR TSDGRIFAVR ATGKPKVPED GRMAASGSQG
     PSCESTSNGR HSASSPKAPD PEGLARPVSP DSPEIISELQ QYADVAAARE SRQSSPSTNA
     ALPGPPAQLM DSSAVPGTAL GTEPRLGGHC LNSSLLVTGQ PCGDRHPVLD LRGHKRKLAT
     PPAAQESSRR RSRKGHLPAP VQPYEHGYPV SGGFAMPPVS LNHNLTTPFT SQAGENSLFM
     GSTPSYYQLS NLLADARLVF PVTTDPLVPA GPVSSSSTAT SVTASNPSFM LNPSVPGILP
     SYSLPFSQPL LSEPRMFAPF PSPVLPSNLS RGMSIYPGYM SPHAGYPAGG LLRSQVPPFD
     SHEVAEVGFS SNDDEDKDDD VIEVTGK
//