Details for: CAD
Associated with
Other Information
Genular Protein ID: 3824672137
Symbol: PYR1_HUMAN
Name: Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 8619816
Title: Molecular cloning of a human cDNA encoding a trifunctional enzyme of carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase in de Novo pyrimidine synthesis.
PubMed ID: 8619816
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 1979741
Title: Organization and nucleotide sequence of the 3' end of the human CAD gene.
PubMed ID: 1979741
PubMed ID: 7766613
Title: Function of conserved histidine residues in mammalian dihydroorotase.
PubMed ID: 7766613
DOI: 10.1021/bi00021a015
PubMed ID: 11872754
Title: Growth-dependent regulation of mammalian pyrimidine biosynthesis by the protein kinase A and MAPK signaling cascades.
PubMed ID: 11872754
PubMed ID: 15890648
Title: Nuclear localization and mitogen-activated protein kinase phosphorylation of the multifunctional protein CAD.
PubMed ID: 15890648
PubMed ID: 16155188
Title: Transcriptional repression of human cad gene by hypoxia inducible factor-1alpha.
PubMed ID: 16155188
DOI: 10.1093/nar/gki839
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16964243
Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
PubMed ID: 16964243
DOI: 10.1038/nbt1240
PubMed ID: 17485345
Title: Protein kinase C modulates the up-regulation of the pyrimidine biosynthetic complex, CAD, by MAP kinase.
PubMed ID: 17485345
DOI: 10.2741/2358
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22223895
Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
PubMed ID: 22223895
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 23429704
Title: Quantitative phosphoproteomics reveal mTORC1 activates de novo pyrimidine synthesis.
PubMed ID: 23429704
PubMed ID: 23429703
Title: Stimulation of de novo pyrimidine synthesis by growth signaling through mTOR and S6K1.
PubMed ID: 23429703
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 26657846
Title: Versatile function of the circadian protein CIPC as a regulator of Erk activation.
PubMed ID: 26657846
PubMed ID: 24332717
Title: Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD.
PubMed ID: 24332717
PubMed ID: 27265852
Title: Structure and functional characterization of human aspartate transcarbamoylase, the target of the anti-tumoral drug PALA.
PubMed ID: 27265852
PubMed ID: 30268498
Title: Crystal structures of monometallic dihydropyrimidinase and the human dihydroorotase domain K1556A mutant reveal no lysine carbamylation within the active site.
PubMed ID: 30268498
PubMed ID: 30315107
Title: Characterization of the catalytic flexible loop in the dihydroorotase domain of the human multi-enzymatic protein CAD.
PubMed ID: 30315107
PubMed ID: 16959974
Title: The consensus coding sequences of human breast and colorectal cancers.
PubMed ID: 16959974
PubMed ID: 25678555
Title: Biallelic mutations in CAD, impair de novo pyrimidine biosynthesis and decrease glycosylation precursors.
PubMed ID: 25678555
DOI: 10.1093/hmg/ddv057
PubMed ID: 28087732
Title: Novel GNB1 mutations disrupt assembly and function of G protein heterotrimers and cause global developmental delay in humans.
PubMed ID: 28087732
DOI: 10.1093/hmg/ddx018
Sequence Information:
- Length: 2225
- Mass: 242984
- Checksum: 2AB8E8413E825A8F
- Sequence:
MAALVLEDGS VLRGQPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY GIPPDEMDEF GLCKWFESSG IHVAALVVGE CCPTPSHWSA TRTLHEWLQQ HGIPGLQGVD TRELTKKLRE QGSLLGKLVQ NGTEPSSLPF LDPNARPLVP EVSIKTPRVF NTGGAPRILA LDCGLKYNQI RCLCQRGAEV TVVPWDHALD SQEYEGLFLS NGPGDPASYP SVVSTLSRVL SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGSGRCFL TSQNHGFAVE TDSLPADWAP LFTNANDGSN EGIVHNSLPF FSVQFHPEHQ AGPSDMELLF DIFLETVKEA TAGNPGGQTV RERLTERLCP PGIPTPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITPHYV TQVIRNERPD GVLLTFGGQT ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ AQAAAERLGY PVLVRAAFAL GGLGSGFASN REELSALVAP AFAHTSQVLV DKSLKGWKEI EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRQ TAIKVTQHLG IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA LGIPLPELRN SVTGGTAAFE PSVDYCVVKI PRWDLSKFLR VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL RMVDENCVGF DHTVKPVSDM ELETPTDKRI FVVAAALWAG YSVDRLYELT RIDRWFLHRM KRIIAHAQLL EQHRGQPLPP DLLQQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV KQIDTVAAEW PAQTNYLYLT YWGTTHDLTF RTPHVLVLGS GVYRIGSSVE FDWCAVGCIQ QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPEG VILSMGGQLP NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCQT VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV ASDGVVAAIA ISEHVENAGV HSGDATLVTP PQDITAKTLE RIKAIVHAVG QELQVTGPFN LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR VIMGEEVEPV GLMTGSGVVG VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PKKNILLTIG SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI LEQLAEKNFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGITMV CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGTVAG SAAGLKLYLN ETFSELRLDS VVQWMEHFET WPSHLPIVAH AEQQTVAAVL MVAQLTQRSV HICHVARKEE ILLIKAAKAR GLPVTCEVAP HHLFLSHDDL ERLGPGKGEV RPELGSRQDV EALWENMAVI DCFASDHAPH TLEEKCGSRP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF HLPPQEDTYV EVDLEHEWTI PSHMPFSKAH WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL VPPGYGQDVR KWPQGAVPQL PPSAPATSEM TTTPERPRRG IPGLPDGRFH LPPRIHRASD PGLPAEEPKE KSSRKVAEPE LMGTPDGTCY PPPPVPRQAS PQNLGTPGLL HPQTSPLLHS LVGQHILSVQ QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS LRYVAPPSLR MPPTVRAFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSTQEYEA CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT VLGRF
Genular Protein ID: 208735420
Symbol: F8VPD4_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 15815621
Title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.
PubMed ID: 15815621
DOI: 10.1038/nature03466
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16964243
Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
PubMed ID: 16964243
DOI: 10.1038/nbt1240
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22223895
Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
PubMed ID: 22223895
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
Sequence Information:
- Length: 2162
- Mass: 236023
- Checksum: 3B325D9DA569C08C
- Sequence:
MAALVLEDGS VLRGQPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY GIPPDEMDEF GLCKWFESSG IHVAALVVGE CCPTPSHWSA TRTLHEWLQQ HGIPGLQGVD TRELTKKLRE QGSLLGKLVQ NGTEPSSLPF LDPNARPLVP EVSIKTPRVF NTGGAPRILA LDCGLKYNQI RCLCQRGAEV TVVPWDHALD SQEYEGLFLS NGPGDPASYP SVVSTLSRVL SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGSGRCFL TSQNHGFAVE TDSLPADWAP LFTNANDGSN EGIVHNSLPF FSVQFHPEHQ AGPSDMELLF DIFLETVKEA TAGNPGGQTV RERLTERLCP PGIPTPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITPHYV TQVIRNERPD GVLLTFGGQT ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ AQAAAERLGY PVLVRAAFAL GGLGSGFASN REELSALVAP AFAHTSQVLV DKSLKGWKEI EYEVVRDAYG NCVTYYIIEV NARLSRSSAL ASKATGYPLA YVAAKLALGI PLPELRNSVT GGTAAFEPSV DYCVVKIPRW DLSKFLRVST KIGSCMKSVG EVMGIGRSFE EAFQKALRMV DENCVGFDHT VKPVSDMELE TPTDKRIFVV AAALWAGYSV DRLYELTRID RWFLHRMKRI IAHAQLLEQH RGQPLPPDLL QQAKCLGFSD KQIALAVLST ELAVRKLRQE LGICPAVKQI DTVAAEWPAQ TNYLYLTYWG TTHDLTFRTP HVLVLGSGVY RIGSSVEFDW CAVGCIQQLR KMGYKTIMVN YNPETVSTDY DMCDRLYFDE ISFEVVMDIY ELENPEGVIL SMGGQLPNNM AMALHRQQCR VLGTSPEAID SAENRFKFSR LLDTIGISQP QWRELSDLES ARQFCQTVGY PCVVRPSYVL SGAAMNVAYT DGDLERFLSS AAAVSKEHPV VISKFIQEAK EIDVDAVASD GVVAAIAISE HVENAGVHSG DATLVTPPQD ITAKTLERIK AIVHAVGQEL QVTGPFNLQL IAKDDQLKVI ECNVRVSRSF PFVSKTLGVD LVALATRVIM GEEVEPVGLM TGSGVVGVKV PQFSFSRLAG ADVVLGVEMT STGEVAGFGE SRCEAYLKAM LSTGFKIPKK NILLTIGSYK NKSELLPTVR LLESLGYSLY ASLGTADFYT EHGVKVTAVD WHFEEAVDGE CPPQRSILEQ LAEKNFELVI NLSMRGAGGR RLSSFVTKGY RTRRLAADFS VPLIIDIKCT KLFVEALGQI GPAPPLKVHV DCMTSQKLVR LPGLIDVHVH LREPGGTHKE DFASGTAAAL AGGITMVCAM PNTRPPIIDA PALALAQKLA EAGARCDFAL FLGASSENAG TLGTVAGSAA GLKLYLNETF SELRLDSVVQ WMEHFETWPS HLPIVAHAEQ QTVAAVLMVA QLTQRSVHIC HVARKEEILL IKAAKARGLP VTCEVAPHHL FLSHDDLERL GPGKGEVRPE LGSRQDVEAL WENMAVIDCF ASDHAPHTLE EKCGSRPPPG FPGLETMLPL LLTAVSEGRL SLDDLLQRLH HNPRRIFHLP PQEDTYVEVD LEHEWTIPSH MPFSKAHWTP FEGQKVKGTV RRVVLRGEVA YIDGQVLVPP GYGQDVRKWP QGAVPQLPPS APATSEMTTT PERPRRGIPG LPDGRFHLPP RIHRASDPGL PAEEPKEKSS RKVAEPELMG TPDGTCYPPP PVPRQASPQN LGTPGLLHPQ TSPLLHSLVG QHILSVQQFT KDQMSHLFNV AHTLRMMVQK ERSLDILKGK VMASMFYEVS TRTSSSFAAA MARLGGAVLS FSEATSSVQK GESLADSVQT MSCYADVVVL RHPQPGAVEL AAKHCRRPVI NAGDGVGEHP TQALLDIFTI REELGTVNGM TITMVGDLKH GRTVHSLACL LTQYRVSLRY VAPPSLRMPP TVRAFVASRG TKQEEFESIE EALPDTDVLY MTRIQKERFG STQEYEACFG QFILTPHIMT RAKKKMVVMH PMPRVNEISV EVDSDPRAAY FRQAENGMYI RMALLATVLG RF
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.