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Q9C0C2 (TB182_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
182 kDa tankyrase-1-binding protein
Gene names
Name:TNKS1BP1
Synonyms:KIAA1741, TAB182
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1729 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Binds to the ANK repeat domain of TNKS1 and TNKS2.

Subcellular location

Nucleus. Cytoplasmcytoskeleton. Chromosome. Note: Colocalizes with chromosomes during mitosis, and in the cytoplasm with cortical actin.

Tissue specificity

Detected in testis, ovary, lung, skeletal muscle, heart, prostate and pancreas, and at very low levels in brain and peripheral blood leukocytes.

Post-translational modification

ADP-ribosylated by TNKS1 (in vitro).

Sequence caution

The sequence BAB21832.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB84939.1 differs from that shown. Reason: Frameshift at positions 1070, 1098 and 1466.

The sequence BAB84939.1 differs from that shown. Reason: Frameshift at positions 1071, 1097 and 1467.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9C0C2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9C0C2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-549: Missing.
     1275-1327: GVGQADWTPD...RDLEVTCDPD → LGRHIYALCI...SSSSLPWVFF
     1328-1729: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17291729182 kDa tankyrase-1-binding protein
PRO_0000072437

Regions

Region210 – 15721363Acidic
Region1450 – 154293Tankyrase-binding
Motif1629 – 16357Nuclear localization signal Potential
Motif1723 – 17297Nuclear localization signal Potential
Compositional bias2 – 103102Arg/Glu/Lys/Pro-rich (charged)
Compositional bias127 – 767641Pro-rich
Compositional bias1010 – 1340331Gly-rich
Compositional bias1572 – 1729158Arg/Glu/Lys-rich (charged)

Amino acid modifications

Modified residue1781Phosphoserine Ref.15 Ref.20
Modified residue2211Phosphoserine Ref.20
Modified residue2391Phosphothreonine Ref.15
Modified residue4291Phosphoserine Ref.15 Ref.19 Ref.20 Ref.22
Modified residue4351Phosphoserine Ref.15 Ref.20
Modified residue4371Phosphoserine Ref.20
Modified residue4941Phosphoserine Ref.15 Ref.19
Modified residue4981Phosphoserine Ref.15
Modified residue6011Phosphoserine Ref.14 Ref.15 Ref.20 Ref.22
Modified residue6721Phosphoserine Ref.9 Ref.15 Ref.20 Ref.22
Modified residue6911Phosphoserine Ref.10 Ref.14 Ref.18 Ref.19 Ref.20 Ref.22
Modified residue6951Phosphoserine Ref.10
Modified residue7121Phosphoserine Ref.15
Modified residue7441Phosphoserine Ref.15
Modified residue7621Phosphoserine Ref.15 Ref.20
Modified residue8331Phosphothreonine Ref.9
Modified residue8361Phosphoserine Ref.9 Ref.10 Ref.12 Ref.14 Ref.19 Ref.20 Ref.22
Modified residue8511Phosphoserine Ref.22
Modified residue8721Phosphoserine Ref.15 Ref.20 Ref.22
Modified residue8771Phosphoserine Ref.15
Modified residue8821Phosphoserine Ref.20
Modified residue8931Phosphoserine Ref.15 Ref.20 Ref.22
Modified residue8991Phosphoserine Ref.22
Modified residue9201Phosphoserine Ref.15
Modified residue9361Phosphoserine Ref.15
Modified residue9791Phosphothreonine Ref.15
Modified residue9831Phosphoserine Ref.15
Modified residue9871Phosphoserine Ref.15 Ref.20
Modified residue10081Phosphoserine Ref.15 Ref.20
Modified residue10241Phosphoserine Ref.20
Modified residue10291Phosphoserine Ref.15
Modified residue10541Phosphoserine Ref.22
Modified residue11031Phosphoserine Ref.10 Ref.14 Ref.15 Ref.20
Modified residue11331Phosphoserine Ref.15 Ref.20
Modified residue11381Phosphoserine Ref.10 Ref.15 Ref.20 Ref.22
Modified residue11781Phosphoserine Ref.15
Modified residue12481Phosphoserine Ref.12 Ref.20
Modified residue12531Phosphoserine Ref.20
Modified residue12821Phosphothreonine Ref.20
Modified residue12971Phosphoserine Ref.15 Ref.20
Modified residue13281Phosphoserine Ref.15
Modified residue13311Phosphoserine Ref.12 Ref.15
Modified residue13831Phosphoserine Ref.9 Ref.20
Modified residue13851Phosphoserine Ref.9 Ref.20 Ref.22
Modified residue14391Phosphoserine Ref.15
Modified residue15331Phosphoserine Ref.15 Ref.20 Ref.22
Modified residue15451Phosphoserine Ref.15 Ref.22
Modified residue15581Phosphoserine Ref.15
Modified residue15631Phosphothreonine Ref.15
Modified residue16201Phosphoserine Ref.10 Ref.15 Ref.19 Ref.20 Ref.22
Modified residue16211Phosphoserine Ref.10 Ref.15 Ref.19 Ref.20 Ref.22
Modified residue16311Phosphoserine Ref.22
Modified residue16521Phosphoserine Ref.15 Ref.20
Modified residue16661Phosphoserine Ref.9 Ref.10 Ref.15 Ref.19 Ref.20 Ref.22
Modified residue17151Phosphoserine Ref.20

Natural variations

Alternative sequence1 – 549549Missing in isoform 2.
VSP_026000
Alternative sequence1275 – 132753GVGQA…TCDPD → LGRHIYALCITLRTPPTPSL PWISSLVVEGFVPSSPPSLS LSASSSSLPWVFF in isoform 2.
VSP_026001
Alternative sequence1328 – 1729402Missing in isoform 2.
VSP_026002
Natural variant3221T → S. Ref.1
Corresponds to variant rs4939134 [ dbSNP | Ensembl ].
VAR_028141
Natural variant7141S → N.
Corresponds to variant rs34203865 [ dbSNP | Ensembl ].
VAR_032615

Experimental info

Sequence conflict841L → P in AAM15531. Ref.1
Sequence conflict3881P → S in AAM15531. Ref.1
Sequence conflict5541Q → H in BAB84939. Ref.7
Sequence conflict6041P → S in AAM15531. Ref.1
Sequence conflict14501S → F in AAM15531. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: 561FA5C27C923036

FASTA1,729181,796
        10         20         30         40         50         60 
MKVSTLRESS AMASPLPREM EEELVPTGSE PGDTRAKPPV KPKPRALPAK PALPAKPSLL 

        70         80         90        100        110        120 
VPVGPRPPRG PLAELPSARK MNMLAGPQPY GGSKRPLPFA PRPAVEASTG GEATQETGKE 

       130        140        150        160        170        180 
EAGKEEPPPL TPPARCAAPG GVRKAPAPFR PASERFAATT VEEILAKMEQ PRKEVLASPD 

       190        200        210        220        230        240 
RLWGSRLTFN HDGSSRYGPR TYGTTTAPRD EDGSTLFRGW SQEGPVKSPA ECREEHSKTP 

       250        260        270        280        290        300 
EERSLPSDLA FNGDLAKAAS SELPADISKP WIPSSPAPSS ENGGPASPGL PAEASGSGPG 

       310        320        330        340        350        360 
SPHLHPPDKS SPCHSQLLEA QTPEASQASP CPAVTPSAPS AALPDEGSRH TPSPGLPAEG 

       370        380        390        400        410        420 
APEAPRPSSP PPEVLEPHSL DQPPATSPRP LIEVGELLDL TRTFPSGGEE EAKGDAHLRP 

       430        440        450        460        470        480 
TSLVQRRFSE GVLQSPSQDQ EKLGGSLAAL PQGQGSQLAL DRPFGAESNW SLSQSFEWTF 

       490        500        510        520        530        540 
PTRPSGLGVW RLDSPPPSPI TEASEAAEAA EAGNLAVSSR EEGVSQQGQG AGSAPSGSGS 

       550        560        570        580        590        600 
SWVQGDDPSM SLTQKGDGES QPQFPAVPLE PLPTTEGTPG LPLQQAEERY ESQEPLAGQE 

       610        620        630        640        650        660 
SPLPLATREA ALPILEPVLG QEQPAAPDQP CVLFADAPEP GQALPVEEEA VTLARAETTQ 

       670        680        690        700        710        720 
ARTEAQDLCR ASPEPPGPES SSRWLDDLLA SPPPSGGGAR RGAGAELKDT QSPSTCSEGL 

       730        740        750        760        770        780 
LGWSQKDLQS EFGITGDPQP SSFSPSSWCQ GASQDYGLGG ASPRGDPGLG ERDWTSKYGQ 

       790        800        810        820        830        840 
GAGEGSTREW ASRCGIGQEE MEASSSQDQS KVSAPGVLTA QDRVVGKPAQ LGTQRSQEAD 

       850        860        870        880        890        900 
VQDWEFRKRD SQGTYSSRDA ELQDQEFGKR DSLGTYSSRD VSLGDWEFGK RDSLGAYASQ 

       910        920        930        940        950        960 
DANEQGQDLG KRDHHGRYSS QDADEQDWEF QKRDVSLGTY GSRAAEPQEQ EFGKSAWIRD 

       970        980        990       1000       1010       1020 
YSSGGSSRTL DAQDRSFGTR PLSSGFSPEE AQQQDEEFEK KIPSVEDSLG EGSRDAGRPG 

      1030       1040       1050       1060       1070       1080 
ERGSGGLFSP STAHVPDGAL GQRDQSSWQN SDASQEVGGH QERQQAGAQG PGSADLEDGE 

      1090       1100       1110       1120       1130       1140 
MGKRGWVGEF SLSVGPQREA AFSPGQQDWS RDFCIEASER SYQFGIIGND RVSGAGFSPS 

      1150       1160       1170       1180       1190       1200 
SKMEGGHFVP PGKTTAGSVD WTDQLGLRNL EVSSCVGSGG SSEARESAVG QMGWSGGLSL 

      1210       1220       1230       1240       1250       1260 
RDMNLTGCLE SGGSEEPGGI GVGEKDWTSD VNVKSKDLAE VGEGGGHSQA RESGVGQTDW 

      1270       1280       1290       1300       1310       1320 
SGVEAGEFLK SRERGVGQAD WTPDLGLRNM APGAVCSPGE SKELGVGQMD WGNNLGLRDL 

      1330       1340       1350       1360       1370       1380 
EVTCDPDSGG SQGLRGCGVG QMDWTQDLAP QNVELFGAPS EAREHGVGGV SQCPEPGLRH 

      1390       1400       1410       1420       1430       1440 
NGSLSPGLEA RDPLEARELG VGETSGPETQ GEDYSSSSLE PHPADPGMET GEALSFGASP 

      1450       1460       1470       1480       1490       1500 
GRCPARPPPS GSQGLLEEML AASSSKAVAR RESAASGLGG LLEEEGAGAG AAQEEVLEPG 

      1510       1520       1530       1540       1550       1560 
RDSPPSWRPQ PDGEASQTED VDGTWGSSAA RWSDQGPAQT SRRPSQGPPA RSPSQDFSFI 

      1570       1580       1590       1600       1610       1620 
EDTEILDSAM YRSRANLGRK RGHRAPVIRP GGTLGLSEAA DSDAHLFQDS TEPRASRVPS 

      1630       1640       1650       1660       1670       1680 
SDEEVVEEPQ SRRTRMSLGT KGLKVNLFPG LSPSALKAKL RPRNRSAEEG ELAESKSSQK 

      1690       1700       1710       1720 
ESAVQRSKSC KVPGLGKPLT LPPKPEKSSG SEGSSPNWLQ ALKLKKKKV 

« Hide

Isoform 2 [UniParc].

Checksum: A08CC80D7372B25D
Show »

FASTA77882,677

References

« Hide 'large scale' references
[1]"The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)."
Seimiya H., Smith S.
J. Biol. Chem. 277:14116-14126(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-322.
Tissue: Placenta and Testis.
[2]"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Hippocampus.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Skin.
[8]"Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones."
Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O.
DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-1729 (ISOFORM 1).
Tissue: Spleen.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; THR-833; SER-836; SER-1383; SER-1385 AND SER-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691; SER-695; SER-836; SER-1103; SER-1138; SER-1620; SER-1621 AND SER-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[12]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-836; SER-1248 AND SER-1331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[13]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601; SER-691; SER-836 AND SER-1103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; THR-239; SER-429; SER-435; SER-494; SER-498; SER-601; SER-672; SER-712; SER-744; SER-762; SER-872; SER-877; SER-893; SER-920; SER-936; THR-979; SER-983; SER-987; SER-1008; SER-1029; SER-1103; SER-1133; SER-1138; SER-1178; SER-1297; SER-1328; SER-1331; SER-1439; SER-1533; SER-1545; SER-1558; THR-1563; SER-1620; SER-1621; SER-1652 AND SER-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-494; SER-691; SER-836; SER-1620; SER-1621 AND SER-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-221; SER-429; SER-435; SER-437; SER-601; SER-672; SER-691; SER-762; SER-836; SER-872; SER-882; SER-893; SER-987; SER-1008; SER-1024; SER-1103; SER-1133; SER-1138; SER-1248; SER-1253; THR-1282; SER-1297; SER-1383; SER-1385; SER-1533; SER-1620; SER-1621; SER-1652; SER-1666 AND SER-1715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-601; SER-672; SER-691; SER-836; SER-851; SER-872; SER-893; SER-899; SER-1054; SER-1138; SER-1385; SER-1533; SER-1545; SER-1620; SER-1621; SER-1631 AND SER-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF441771 mRNA. Translation: AAM15531.1.
AB051528 mRNA. Translation: BAB21832.2. Different initiation.
AK124903 mRNA. Translation: BAC85989.1.
AP000781 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73731.1.
BC023622 mRNA. Translation: AAH23622.1.
BC150333 mRNA. Translation: AAI50334.1.
AK074113 mRNA. Translation: BAB84939.1. Frameshift.
CCDSCCDS7951.1. [Q9C0C2-1]
RefSeqNP_203754.2. NM_033396.2. [Q9C0C2-1]
XP_006718788.1. XM_006718725.1. [Q9C0C2-1]
UniGeneHs.530730.

3D structure databases

ProteinModelPortalQ9C0C2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124540. 19 interactions.
IntActQ9C0C2. 12 interactions.
MINTMINT-4538987.
STRING9606.ENSP00000350990.

PTM databases

PhosphoSiteQ9C0C2.

Polymorphism databases

DMDM317373547.

Proteomic databases

MaxQBQ9C0C2.
PaxDbQ9C0C2.
PRIDEQ9C0C2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358252; ENSP00000350990; ENSG00000149115. [Q9C0C2-1]
ENST00000532437; ENSP00000437271; ENSG00000149115. [Q9C0C2-1]
GeneID85456.
KEGGhsa:85456.
UCSCuc001njr.3. human. [Q9C0C2-1]

Organism-specific databases

CTD85456.
GeneCardsGC11M057067.
HGNCHGNC:19081. TNKS1BP1.
HPAHPA037929.
HPA037930.
MIM607104. gene.
neXtProtNX_Q9C0C2.
PharmGKBPA38789.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46995.
HOGENOMHOG000001569.
HOVERGENHBG080593.
InParanoidQ9C0C2.
OMAQDQEKLG.
OrthoDBEOG7DC23N.
PhylomeDBQ9C0C2.
TreeFamTF336029.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9C0C2.
BgeeQ9C0C2.
CleanExHS_TNKS1BP1.
GenevestigatorQ9C0C2.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSTNKS1BP1. human.
GeneWikiTNKS1BP1.
GenomeRNAi85456.
NextBio76085.
PROQ9C0C2.
SOURCESearch...

Entry information

Entry nameTB182_HUMAN
AccessionPrimary (citable) accession number: Q9C0C2
Secondary accession number(s): A7E2F8, Q6PJ35, Q6ZV74
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 118 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM