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Protein data for XAB2_HUMAN:

Description:
XPA-binding protein 2 (HCNP protein).

Molecular weight: 10001

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 ) transcription-coupled nucleotide-excision repair( GO:0006283 )


Important dates:
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 2.
07-MAR-2006, entry version 41.

Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein XAB2_HUMAN:

DatabasePointerAdd. info#1Add. info#2
EMBLAB026111BAB15807.1-
EMBLAF226051AAF86951.1ALT_FRAME
EMBLAF258567AAG23770.1-
EMBLAF547265AAN17847.1-
EMBLBC007208AAH07208.1-
EMBLBC008778AAH08778.1ALT_INIT
EMBLAK074035BAB84861.1ALT_FRAME
EMBLAB033003BAA86491.1-
IntActQ9HCS7-.1
EnsemblENSG00000076924Homo sapiens.1
HGNCHGNC:14089XAB2.1
ReactomeQ9HCS7-.1
GOGO:0005634C:nucleusIC.
GOGO:0005515F:protein bindingIPI.
GOGO:0006350P:transcriptionIDA.
GOGO:0006283P:transcription-coupled nucleotide-excision r...IDA.
InterProIPR003107HAT.
InterProIPR002885PPR.
InterProIPR011990TPR-like_helical.
InterProIPR013105TPR_2.
PfamPF07719TPR_21.
SMARTSM00386HAT1.
TIGRFAMsTIGR00756PPR1.

General information about the databases mentioned above

Keywords:
DNA damage; DNA repair; Nuclear protein; Polymorphism; Repeat; Transcription.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE, FUNCTION, AND SUBUNIT.
RX MEDLINE=20519578; PubMed=10944529; DOI=10.1074/jbc.M004936200;
RA Nakatsu Y., Asahina H., Citterio E., Rademakers S., Vermeulen W.,
RA Kamiuchi S., Yeo J.-P., Khaw M.-C., Saijo M., Kodo N., Matsuda T.,
RA Hoeijmakers J.H.J., Tanaka K.;
RT "XAB2, a novel tetratricopeptide repeat protein, involved in
RT transcription-coupled DNA repair and transcription.";
RL J. Biol. Chem. 275:34931-34937(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human adrenal gland.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-126; GLN-454 AND
RP THR-702.
RA Rieder M.J., Livingston R.J., Daniels M.R., Montoya M.A., Chung M.-W.,
RA Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D.,
RA Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-855.
RC TISSUE=Spleen;
RA Ohara O., Nagase T., Kikuno R., Okumura K.;
RT "The nucleotide sequence of a long cDNA clone isolated from human
RT spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-855.
RC TISSUE=Brain;
RX MEDLINE=20039618; PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis
RT from size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).

Feature:
CHAIN 1 855 XPA-binding protein 2.
/FTId=PRO_0000106414.
REPEAT 15 47 HAT 1.
REPEAT 48 80 HAT 2.
REPEAT 90 122 HAT 3.
REPEAT 124 158 HAT 4.
REPEAT 160 192 HAT 5.
REPEAT 198 230 HAT 6.
REPEAT 235 268 HAT 7.
REPEAT 270 305 HAT 8.
REPEAT 369 407 HAT 9.
REPEAT 498 530 HAT 10.
REPEAT 532 566 HAT 11.
REPEAT 571 605 HAT 12.
REPEAT 643 677 HAT 13.
REPEAT 679 713 HAT 14.
VARIANT 126 126 V -> I.
/FTId=VAR_016248.
VARIANT 454 454 R -> Q.
/FTId=VAR_016249.
VARIANT 702 702 A -> T.
/FTId=VAR_016250.
CONFLICT 68 68 Y -> T (in Ref. 2).
CONFLICT 140 140 L -> M (in Ref. 1).
CONFLICT 447 447 E -> K (in Ref. 5; AAH08778).
CONFLICT 680 680 E -> K (in Ref. 2).
CONFLICT 751 753 SAT -> IP (in Ref. 2).

Comments:
-!- FUNCTION: Involved in transcription-coupled repair (TCR) and
transcription.
-!- SUBUNIT: Associates with RNA polymerase II, the TCR-specific
proteins CKN1/CSA and ERCC6/CSB, and XPA.
-!- INTERACTION:
Q13216:ERCC8; NbExp=2; IntAct=EBI-295232, EBI-295260;
P24928:POLR2A; NbExp=1; IntAct=EBI-295232, EBI-295301;
P23025:XPA; NbExp=1; IntAct=EBI-295232, EBI-295222;
-!- SUBCELLULAR LOCATION: Nuclear; detected in the splicing complex
carrying pre-mRNA (By similarity).
-!- SIMILARITY: Contains 14 HAT repeats.
-!- CAUTION: Ref.2 sequence differs from that shown due to
frameshifts.
-!- CAUTION: Ref.6 sequence differs from that shown due to
frameshifts.
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Sequence length: 855

     MVVMARLSRP ERPDLVFEEE DLPYEEEIMR NQFSVKCWLR YIEFKQGAPK PRLNQLYERA
     LKLLPCSYKL WYRYLKARRA QVKHRCVTDP AYEDVNNCHE RAFVFMHKMP RLWLDYCQFL
     MDQGRVTHTR RTFDRALRAL PITQHSRIWP LYLRFLRSHP LPETAVRGYR RFLKLSPESA
     EEYIEYLKSS DRLDEAAQRL ATVVNDERFV SKAGKSNYQL WHELCDLISQ NPDKVQSLNV
     DAIIRGGLTR FTDQLGKLWC SLADYYIRSG HFEKARDVYE EAIRTVMTVR DFTQVFDSYA
     QFEESMIAAK METASELGRE EEDDVDLELR LARFEQLISR RPLLLNSVLL RQNPHHVHEW
     HKRVALHQGR PREIINTYTE AVQTVDPFKA TGKPHTLWVA FAKFYEDNGQ LDDARVILEK
     ATKVNFKQVD DLASVWCQCG ELELRHENYD EALRLLRKAT ALPARRAEYF DGSEPVQNRV
     YKSLKVWSML ADLEESLGTF QSTKAVYDRI LDLRIATPQI VINYAMFLEE HKYFEESFKA
     YERGISLFKW PNVSDIWSTY LTKFIARYGG RKLERARDLF EQALDGCPPK YAKTLYLLYA
     QLEEEWGLAR HAMAVYERAT RAVEPAQQYD MFNIYIKRAA EIYGVTHTRG IYQKAIEVLS
     DEHAREMCLR FADMECKLGE IDRARAIYSF CSQICDPRTT GAFWQTWKDF EVRHGNEDTI
     KEMLRIRRSV QATYNTQVNF MASQMLKVSG SATGTVSDLA PGQSGMDDMK LLEQRAEQLA
     AEAERDQPLR AQSKILFVRS DASREELAEL AQQVNPEEIQ LGEDEDEDEM DLEPNEVRLE
     QQSVPAAVFG SLKED

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