wanglab/gogpt-training-data huggingface dataset:
Protein: Metal transporter CNNM1 (Ancient conserved domain-containing protein 1) (Cyclin-M1) (Q9NRU3)
Organism: Homo sapiens (Human)
Function: Probable metal transporter.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Cystathionine beta-synthase
- Cystathionine beta-synthase-like protein
- Protein tyrosine phosphatase type IVA 2
- Protein tyrosine phosphatase type IVA 1
- Cytochrome c oxidase assembly protein COX11
- Transient receptor potential cation channel subfamily M member 6
- GMP synthase
Sequence:
MAAAAAAAAAVGVRLRDCCSRGAVLLLFFSLSPRPPAAAAWLLGLRPEDTAGGRVSLEGGTLRAAEGTSFLLRVYFQPGPPATAAPVPSPTLNSGENGTGDWAPRLVFIEEPPGGGGVAPSAVPTRPPGPQRCREQSDWASDVEVLGPLRPGGVAGSALVQVRVRELRKGEAERGGAGGGGKLFSLCAWDGRAWHHHGAAGGFLLRVRPRLYGPGGDLLPPAWLRALGALLLLALSALFSGLRLSLLSLDPVELRVLRNSGSAAEQEQARRVQAVRGRGTHLLCTLLLGQAGANAALAGWLYTSLPPGFGGTGEDYSEEGIHFPWLPALVCTGAVFLGAEICPYSVCSRHGLAIASHSVCLTRLLMAAAFPVCYPLGRLLDWALRQEISTFYTREKLLETLRAADPYSDLVKEELNIIQGALELRTKVVEEVLTPLGDCFMLRSDAVLDFATVSEILRSGYTRIPVYEGDQRHNIVDILFVKDLAFVDPDDCTPLLTVTRFYNRPLHCVFNDTRLDTVLEEFKKGKSHLAIVQRVNNEGEGDPFYEVMGIVTLEDIIEEIIKSEILDETDLYTDNRKKQRVPQRERKRHDFSLFKLSDTEMRVKISPQLLLATHRFMATEVEPFKSLYLSEKILLRLLKHPNVIQELKFDEKNKKAPEHYLYQRNRPVDYFVLLLQGKVEVEVGKEGLRFENGAFTYYGVPAIMTTACSDNDVRKVGSLAGSSVFLNRSPSRCSGLNRSESPNRERSDFGGSNTQLYSSSNNLYMPDYSVHILSDVQFVKITRQQYQNALTACHMDSSPQSPDMEAFTDGDSTKAPTTRGTPQTPKDDPAITLLNNRNSLPCSRSDGLRSPSEVVYLRMEELAFTQEEMTDFEEHSTQQLTLSPAAVPTRAASDSECCNINLDTETSPCSSDFEENVGKKLLRTLSGQKRKRSPEGERTSEDNSNLTPLIT
Protein: Beta-tubulin 1 (A6MUS5)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
TLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTNPSFGDLNHLISTTMSGVTCCLRFPGQFNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTIPELTQQMWDSKNMMCAADPRHGRYLTASA
Protein: Tectonin beta-propeller repeat-containing protein 1 (Q7Z6L1)
Organism: Homo sapiens (Human)
Function: Tethering factor involved in autophagy. Involved in autophagosome maturation by promoting the autophagosome fusion with lysosomes: acts by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns(3)P) present at the surface of autophagosomes. Also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation.
Subcellular location: Cytoplasmic vesicle, autophagosome membrane. Lysosome membrane. Note=Localizes to Lysosome membranes, and binds PtdIns(3)P at the surface of autophagosome. Localizes to autolysosomes, a vesicle formed by the fusion between autophagosomes and lysosomes.
Interaction partners:
- Autophagy protein 5
- WD repeat domain phosphoinositide-interacting protein 2
- Ubiquitin-like protein ATG12
- WD repeat domain phosphoinositide-interacting protein 1
- Autophagy-related protein 16-1
- Ubiquitin-like-conjugating enzyme ATG3
Sequence:
MPNSVLWAVDLFGRVYTLSTAGQYWEMCKDSQLEFKRVSATTQCCWGIACDNQVYVYVCASDVPIRRREEAYENQRWNPMGGFCEKLLLSDRWGWSDVSGLQHRPLDRVALPSPHWEWESDWYVDENFGGEPTEKGGWTYAIDFPATYTKDKKWNSCVRRRKWIRYRRYKSRDIWAKIPSKDDPKELPDPFNDLSVGGWEITEEPVGRLSVWAVSLQGKVWYREDVSHSNPEGSSWSLLDTPGEVVQISCGPHDLLWATLWEGQALVREGINRSNPKGSSWSIVEPPGSENGVMHISVGVSVVWAVTKDWKVWFRRGVNSHNPCGTSWIEMVGEMTMVNVGMNDQVWGIGCEDRAVYFRQGVTPSELSGKTWKAIIAARECDRSHSGSSSSLLSAGCFFGDEVRGSGESAPSDTDASSEVERPGPGQILPAEPLDDSKNATGNSASGLGAGRTAEDTVEDACPAEGSREARPNTHPGPAPTPAELPWTNIDLKEAKKVPSHSAAGFPETTSLSSLGLLPLGLEEPYGVDDHPLWAWVSGGGCVVEACAMPRWFTVQAGLSSSVHMLSLSITPAQTAAWRKQIFQQLTERTKRELENFRHYEQAVEQSVWVKTGALQWWCDWKPHKWVDVRLALEQFTGHDGVRDSILFIYYVVHEEKKYIHIFLNEVVALVPVLNETKHSFALYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVQGRPSPQAIWSITCKGDIFVSEPSPDLEAHEHPLPCDQMFWRQMGGHLRMVEANSRGVVWGIGYDHTAWVYTGGYGGGCFQGLASSTSNIYTQSDVKCVHIYENQRWNPVTGYTSRGLPTDRYMWSDASGLQECTKAGTKPPSLQWAWVSDWFVDFSVPGGTDQEGWQYASDFPASYHGSKTMKDFVRRRCWARKCKLVTSGPWLEVPPIALRDVSIIPESPGAEGSGHSIALWAVSDKGDVLCRLGVSELNPAGSSWLHVGTDQPFASISIGACYQVWAVARDGSAFYRGSVYPSQPAGDCWYHIPSPPRQRLKQVSAGQTSVYALDENGNLWYRQGITPSYPQGSSWEHVSNNVCRVSVGPLDQVWVIANKVQGSHSLSRGTVCHRTGVQPHEPKGHGWDYGIGGGWDHISVRANATRAPRSSSQEQEPSAPPEAHGPVCC
Protein: Complement factor H-related protein 1 (FHR-1) (H factor-like protein 1) (FHL-1) (H-factor-like 1) (H36) (Q03591)
Organism: Homo sapiens (Human)
Function: Involved in complement regulation. The dimerized forms have avidity for tissue-bound complement fragments and efficiently compete with the physiological complement inhibitor CFH. Can associate with lipoproteins and may play a role in lipid metabolism.
Subcellular location: Secreted.
Interaction partners:
- Complement C3
- Complement factor B
- Complement factor H
- Complement factor H-related protein 3
- Complement factor H-related protein 2
- Complement factor I
- A disintegrin and metalloproteinase with thrombospondin motifs 13
- Diacylglycerol kinase epsilon
- Gamma-tubulin complex component 5
- Complement C4-B
Sequence:
MWLLVSVILISRISSVGGEATFCDFPKINHGILYDEEKYKPFSQVPTGEVFYYSCEYNFVSPSKSFWTRITCTEEGWSPTPKCLRLCFFPFVENGHSESSGQTHLEGDTVQIICNTGYRLQNNENNISCVERGWSTPPKCRSTDTSCVNPPTVQNAHILSRQMSKYPSGERVRYECRSPYEMFGDEEVMCLNGNWTEPPQCKDSTGKCGPPPPIDNGDITSFPLSVYAPASSVEYQCQNLYQLEGNKRITCRNGQWSEPPKCLHPCVISREIMENYNIALRWTAKQKLYLRTGESAEFVCKRGYRLSSRSHTLRTTCWDGKLEYPTCAKR
Protein: Protein big1 (Q9Y7R6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Accessory subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Protein rot1
- Uncharacterized protein C11C11.05
Sequence:
MFSWSILFIVCFSLVSAFKDTSPIFLFSTNSKLPKSSDDSSISTCPMMFFDAAIEALSTCNTATLIIHQPGLEVNDFQLGAFKHLKRVSLQSPYSLLLPYSKESLDSQELVHSAKQNCDVEVVYLGGSFNAFPPLQNDRITVVYMNELSNESYHRSAQLMELDEMFYNLQSTLEQDAQWNVIIASSPLNNSDFEGFKVDANEEEANAEFVIQTLGGLNSGKSALQHGQLASLPDQNEGSQTTLAMHQTRKHPVTDNGATGLFTEYQFFTPGLYMGYLALAVLVPTLFISCRLLSSIQISYHAFDSPRRKQL
Protein: Exostosin-1 (EC 2.4.1.225) (Exostosin glycosyltransferase 1) (Heparan sulfate co-polymerase subunit EXT1) (Multiple exostoses protein 1) (N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase) (Q16394)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor. Required for the exosomal release of SDCBP, CD63 and syndecan.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10639137, ECO:0000269|PubMed:10679296}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:35137078}; Single-pass type II membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10679296, ECO:0000269|PubMed:9620772}; Single-pass type II membrane protein {ECO:0000255}. Note=The active heparan sulfate polymerase complex composed of EXT1 and EXT2 is localized to the Golgi apparatus. If both proteins are individually detected in the endoplasmic reticulum, the formation of the complex promotes their transport to the Golgi. {ECO:0000269|PubMed:10639137, ECO:0000269|PubMed:10679296, ECO:0000269|PubMed:9620772}.
Interaction partners:
- Exostosin-2
- Zinc finger transcription factor Trps1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Heparan sulfate 2-O-sulfotransferase 1
- Heat shock protein 75 kDa, mitochondrial
- Glypican-1
- Indian hedgehog protein
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Annexin A13
Sequence:
MQAKKRYFILLSAGSCLALLFYFGGLQFRASRSHSRREEHSGRNGLHHPSPDHFWPRFPDALRPFVPWDQLENEDSSVHISPRQKRDANSSIYKGKKCRMESCFDFTLCKKNGFKVYVYPQQKGEKIAESYQNILAAIEGSRFYTSDPSQACLFVLSLDTLDRDQLSPQYVHNLRSKVQSLHLWNNGRNHLIFNLYSGTWPDYTEDVGFDIGQAMLAKASISTENFRPNFDVSIPLFSKDHPRTGGERGFLKFNTIPPLRKYMLVFKGKRYLTGIGSDTRNALYHVHNGEDVVLLTTCKHGKDWQKHKDSRCDRDNTEYEKYDYREMLHNATFCLVPRGRRLGSFRFLEALQAACVPVMLSNGWELPFSEVINWNQAAVIGDERLLLQIPSTIRSIHQDKILALRQQTQFLWEAYFSSVEKIVLTTLEIIQDRIFKHISRNSLIWNKHPGGLFVLPQYSSYLGDFPYYYANLGLKPPSKFTAVIHAVTPLVSQSQPVLKLLVAAAKSQYCAQIIVLWNCDKPLPAKHRWPATAVPVVVIEGESKVMSSRFLPYDNIITDAVLSLDEDTVLSTTEVDFAFTVWQSFPERIVGYPARSHFWDNSKERWGYTSKWTNDYSMVLTGAAIYHKYYHYLYSHYLPASLKNMVDQLANCEDILMNFLVSAVTKLPPIKVTQKKQYKETMMGQTSRASRWADPDHFAQRQSCMNTFASWFGYMPLIHSQMRLDPVLFKDQVSILRKKYRDIERL
Protein: Carbon monoxide-induced hydrogenase CooH, putative (Q729Q8)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Hydrogenase, CooL subunit, putative
- Hydrogenase, CooX subunit, putative
- Ech hydrogenase, subunit EchC, putative
- Hydrogenase, CooU subunit, putative
- Hydrogenase, CooM subunit, putative
- Hydrogenase, CooK subunit, selenocysteine-containing, putative
- Iron-sulfur protein CooF
- Ech hydrogenase, subunit EchB, putative
- Hydrogenase maturation factor HypA 2
- Ech hydrogenase, subunit EchF, putative
Sequence:
MSTPDSTTQTWTLPVGPLHVALEEPMYFKLDVDGEIVRNVEITAGHVHRGMEALAMRRNLFQNIVLTERVCSLCSNSHPFTYCMAVEHLAGIEVPARADHLRVVAEEIKRTASHLFNVAILAHIIGFKSLFMHVMEVREIMQDIKETVYGNRMDLAANCIGGVKYDVDAELLAMLLAGLDKVERNAREIYRIYASDPMVTGRTTGIGVLPPDEARRFGVVGPVARGSGLAVDVRRDVPYAAYPQLSFDVITEEGCDVRARALVRLREVFESISIIRQCVATLPEGAMTVIMPEIPAGQSVARSEAPRGELMYYLRTDGTDIPNRLKWRVPSYMNWDALGVMMRDANVADIPLIVNSIDPCISCTER
Protein: Brevinin-1SN1 (E7EKH1)
Organism: Sylvirana spinulosa (Fine-spined frog) (Hylarana spinulosa)
Function: Antimicrobial peptide. Active against some Gram-negative and a variety of Gram-positive bacterial strains. Active against fungus C.glabrata 090902 but not against C.albicans ATCC 10231. Shows hemolytic activity against human erythrocytes.
Subcellular location: Secreted {ECO:0000305|PubMed:24055160}.
Interaction partners:
Sequence:
MFTMKKPLLLLFFLGTINLSLCEEERNADEEEKRDGDDEMDAEVEKRFLPAVLKVAAHILPTAICAISRRC
Protein: Uncharacterized protein (Q386I2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRVHQIPCKKLFRQLGRRGILSTPPSPVESAEPTTIRSRGYGPSKHLLRGVDATRGVVVEAALSPADVEMQRRVLSMANPNVAIHAKLEGEPSPVHSGTNSLHGDDQRLADRAGVASSEQLASVATVILDEVKEQLQLNLSAADASQDSRAATVVNAVAECLRNEVDRLIHANHTQESSITRVLRENTDLICKRVADVICSEQLKTLSFKDVGQLPQVIKEVGTSLVRLESALKSALDSSFGKDKNLEEVLGDLREHIVSAIEQASHFQQERLLASVSDLLADCADAQDSKSRLAQAASLKVIEKNVRDAMSQMVEDTQHKVQSVLRDLRGSASTSDAAGSTTNVSSGNEVAFERILASYGERLEELRESTAAAVDLKELMMEIHSMHQTSAGDVSEVKNLVKKLKRELISALQPSNTENTEGSTVERKSSDTIDYNGIFADKLDALADDVISRIDGRLKEQHADVRELSARLLQLEDVIKKTPRAALQVGSVPELNDDRLLALAQSISESILSSLPPHSAPAVEEKEQQEPPRPSVSTAVATTAHTFTATELAEAVSAALTPRLDELAAAIQKKVAPTSTASGNEYDNRHMGETQLVTVAQTICEGVREAVRESMALYKPPVASPPTPAPGAVVAPAVDTSALEQAMVTKVEDLKRCVMDAVQEMDRPQEIDLSPFRTYLDDVLRSMQTTLSKQQQATQDKVDGVVEALAKKLQDYQHQLESKLQRQHRDQVEQIQVVRRAQEQDMKADEETWKQRMSRNQEDAEQRTNEQKSAVTGAMQEVFLQVRQRLTEDVRTLLKGEVAAALIPLDDLYKELRESGQKSRTALEAKLRSVEDTLQSVLDSERHRSDRLQATLDDVIACIKNNSGEVSGSETEALKSLKRLLEDLAERNTATGMEICSDVKASLERTEELHVQTAEKMLRGFDTLKYEIHEGRQQLDQLLSSNQQNKDVALAVEAMRTKLDEVRYSLDCIMASVREMQEHPMRQLQEPQQQQQSLLSETEVKSPIDDKVLEQYEQRQREASDLIASRLETLSATTREVLSQLQRQQPRRSEEEMGSQPAVTTNLSVESLQAMEGRLGERMQALQAALDELTKVSASVPPTTEVFRKDEVDGVEGSKSFIKEVDELMTLVKSSRSVQAKQMWERLSILRTSLVDVSTKKTGDTNIKQLLGALEENRLKLREEMGEAERELVIKIDAATQKAVEHFAARIERAVKASADAGLGQLRNDLKESSEILKAHQHQFSSQLQDRMTNIERTNRECAAELKEKLRDTSKEYHNALGQFVKNDMIAALRSTVNEATTQQMRTFTQQFTWQKEREETNKEAVMRSVQQVSQGVGKLQSMSSEVRTAVTSSSAGVVQEVRNAQKDLAVLFEKRLAAVLEQQKKQQVVQVLSPVRVGEADSSNGIPSETTDTPSLVTMVNPQGASHLSWFLLSQSVVTIITIMLCAYFLFAAFLVAFVPIPLTDEFASHMEQAADNDVSEIALKRPLVSRVADRVIL
Protein: P2X purinoceptor (B7Z6W8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004155}. Membrane {ECO:0000256|RuleBase:RU000681}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU000681}.
Interaction partners:
Sequence:
MNRAVQLLILAYVIGWVFVWEKGYQETDSVVSSVTTKVKGVAVTNTSKLGFRIWDVADYVIPAQEENSLFVMTNVILTMNQTQGLCPEIPDATTVCKSDASCTAGSAGTHSNGVSTGRCVAFNGSVKTCEVAAWCPVEDDTHVPQPAFLKAAENFTLLVKNNIWYPKFNFSKRNILPNITTTYLKSCIYDAKTDPFCPIFRLGKIVENAGHSFQDMAVEGGIMGIQVNWDCNLDRAASLCLPRYSFRRLDTRDVEHNVSPGYNFRFAKYYRDLAGNEQRTLIKAYGIRFDIIVFGKAGKFDIIPTMINIGSGLALLGMATVLCDIIVLYCMKKRLYYREKKYKYVEDYEQGLASELDQ
Protein: Cyclin-dependent kinase 4 (EC 2.7.11.22) (CRK3) (Cell division protein kinase 4) (PSK-J3) (P30285)
Organism: Mus musculus (Mouse)
Function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11802}. Nucleus {ECO:0000250|UniProtKB:P11802}. Nucleus membrane {ECO:0000250|UniProtKB:P11802}. Note=Cytoplasmic when non-complexed. Forms a cyclin D-CDK4 complex in the cytoplasm as cells progress through G(1) phase. The complex accumulates on the nuclear membrane and enters the nucleus on transition from G(1) to S phase. Also present in nucleoli and heterochromatin lumps. Colocalizes with RB1 after release into the nucleus (By similarity). {ECO:0000250|UniProtKB:P11802}.
Interaction partners:
- G1/S-specific cyclin-E1
- Cyclin-A2
- Cyclin-dependent kinase 4 inhibitor D
- G1/S-specific cyclin-D2
- Cyclin-dependent kinase inhibitor 1B
- G1/S-specific cyclin-D1
- G1/S-specific cyclin-D3
- Cyclin-dependent kinase 4 inhibitor C
- Cyclin-dependent kinase inhibitor 1
- Retinoblastoma-associated protein
Sequence:
MAATRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGAAGGGLPVSTVREVALLRRLEAFEHPNVVRLMDVCATSRTDRDIKVTLVFEHIDQDLRTYLDKAPPPGLPVETIKDLMRQFLSGLDFLHANCIVHRDLKPENILVTSNGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPREVSLPRGAFAPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKEESDAE
Protein: Integrator complex subunit 7 (Int7) (Q9NVH2)
Organism: Homo sapiens (Human)
Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). Plays a role in DNA damage response (DDR) signaling during the S phase. May be not involved in the recruitment of cytoplasmic dynein to the nuclear envelope by different components of the INT complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:21659603, ECO:0000269|PubMed:29471365}. Chromosome {ECO:0000269|PubMed:21659603, ECO:0000269|PubMed:29471365, ECO:0000269|PubMed:39032490}. Cytoplasm {ECO:0000269|PubMed:23904267}. Note=Localizes to sites of DNA damage in a H2AX-independent manner. {ECO:0000269|PubMed:21659603}.
Interaction partners:
- Integrator complex subunit 8
- Integrator complex subunit 5
- Integrator complex subunit 1
- Integrator complex subunit 6
- Integrator complex subunit 3
- Integrator complex subunit 2
- Integrator complex subunit 11
- Integrator complex subunit 4
- Integrator complex subunit 9
- Integrator complex subunit 10
Sequence:
MASNSTKSFLADAGYGEQELDANSALMELDKGLRSGKLGEQCEAVVRFPRLFQKYPFPILINSAFLKLADVFRVGNNFLRLCVLKVTQQSEKHLEKILNVDEFVKRIFSVIHSNDPVARAITLRMLGSLASIIPERKNAHHSIRQSLDSHDNVEVEAAVFAAANFSAQSKDFAVGICNKISEMIQGLATPVDLKLKLIPILQHMHHDAILASSARQLLQQLVTSYPSTKMVIVSLHTFTLLAASSLVDTPKQIQLLLQYLKNDPRKAVKRLAIQDLKLLANKTPHTWSRENIQALCECALQTPYDSLKLGMLSVLSTLSGTIAIKHYFSIVPGNVSSSPRSSDLVKLAQECCYHNNRGIAAHGVRVLTNITVSCQEKDLLALEQDAVFGLESLLVLCSQDDSPGAQATLKIALNCMVKLAKGRPHLSQSVVETLLTQLHSAQDAARILMCHCLAAIAMQLPVLGDGMLGDLMELYKVIGRSATDKQQELLVSLATVIFVASQKALSVESKAVIKQQLESVSNGWTVYRIARQASRMGNHDMAKELYQSLLTQVASEHFYFWLNSLKEFSHAEQCLTGLQEENYSSALSCIAESLKFYHKGIASLTAASTPLNPLSFQCEFVKLRIDLLQAFSQLICTCNSLKTSPPPAIATTIAMTLGNDLQRCGRISNQMKQSMEEFRSLASRYGDLYQASFDADSATLRNVELQQQSCLLISHAIEALILDPESASFQEYGSTGTAHADSEYERRMMSVYNHVLEEVESLNRKYTPVSYMHTACLCNAIIALLKVPLSFQRYFFQKLQSTSIKLALSPSPRNPAEPIAVQNNQQLALKVEGVVQHGSKPGLFRKIQSVCLNVSSTLQSKSGQDYKIPIDNMTNEMEQRVEPHNDYFSTQFLLNFAILGTHNITVESSVKDANGIVWKTGPRTTIFVKSLEDPYSQQIRLQQQQAQQPLQQQQQRNAYTRF
Protein: Arf-GAP with dual PH domain-containing protein 2 (Centaurin-alpha-2) (Cnt-a2) (Q9JK15)
Organism: Rattus norvegicus (Rat)
Function: GTPase-activating protein for the ADP ribosylation factor family (Potential). Binds phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). Binding of phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4-bisphosphate occurs at a much lower affinity. Possesses a stoichiometry of two binding sites for InsP4 with identical affinity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Constitutively associated with the plasma membrane. Excluded from the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MGDRERNKKRLLELLQAAGTGNGHCADCGAADPDWASYKLGVFICLHCSGVHRNFPDISKVKSVRLDFWDDSMVEFMTHNGNLSVKAKFEARVPTFYYVPQASDCLVLKEQWIRAKYERQEFMAEKAVSPPGDREGFLWKRGRDNSQFLRRRFVLLSREGLLKYYTKEEGKTPKAIINIKDLNATFQTEKIGHPHGLQITYRKEGQTRNLFVYHDSGKEIVDWFNALRAARLQYLKLAFPDLPESELVPLITRNYLKQGFMEKTGPKHREPFKKRWFALDPQERRLLYYKNPLDAFEQGQVFLGSNEQGYEVWEGLPQGIRGNRWKVGLTVITPERKFVFTCPTEKEQREWLESLRGVLSSPLSPLHLLTTSAKSG
Protein: Beta carbonic anhydrase 3 (AtbCA3) (AtbetaCA3) (EC 4.2.1.1) (Beta carbonate dehydratase 3) (Q9ZUC2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reversible hydration of carbon dioxide.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17407539}.
Interaction partners:
- Cyanate hydratase
- Sodium/proton antiporter 2
- Adenylate kinase 2, chloroplastic
- Alpha carbonic anhydrase 3
- Probable sodium/metabolite cotransporter BASS4, chloroplastic
- Putative serine carboxypeptidase-like 30
- Tubulin-folding cofactor D
- Mediator of RNA polymerase II transcription subunit 15a
- Adenine phosphoribosyltransferase 3
Sequence:
MSTESYEDAIKRLGELLSKKSDLGNVAAAKIKKLTDELEELDSNKLDAVERIKSGFLHFKTNNYEKNPTLYNSLAKSQTPKFLVFACADSRVSPSHILNFQLGEAFIVRNIANMVPPYDKTKHSNVGAALEYPITVLNVENILVIGHSCCGGIKGLMAIEDNTAPTKTEFIENWIQICAPAKNRIKQDCKDLSFEDQCTNCEKEAVNVSLGNLLSYPFVRERVVKNKLAIRGAHYDFVKGTFDLWELDFKTTPAFALS
Protein: Palmitoyltransferase akr1 (EC 2.3.1.225) (Ankyrin repeat-containing protein akr1) (Q09701)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Palmitoyltransferase specific for casein kinase 1.
Subcellular location: Early endosome membrane; Multi-pass membrane protein. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Vacuolar protein 8
- Palmitoyltransferase swf1
Sequence:
MGSLFLAASQGELDTVKNLISSEKIDVNATDEGGATALHWAALNQQIPICKFLLEHGADVNAIGGDLQAAPIHWAAKRGSVKTVHYLVQHGADPLLKDKQGFNCLHLAVHAASPLLVVYLLHLDISVDLRDDQQHTPLMWASYHGNEPITNCLLRWGADVLATDEDKMTPLHWSIVGGNLKCMKLILKEGGIPCTAVTANLSGQLKTPWALASELRVSHLFKQALISNGLKVKETSEEPEKWVVVPSKFQFSQKTFIIFCFLSSFIITGVFFFIMSICPMVISLIIAPLWIYFTFKYITTCIHANIDIVHFYLETPFLAGIFSSIFFWVWCHSLLYIVPKTLPIKPLSSLLFVLISFTCIGLYVRTAFQNPGYVDKIGAVVQRREEISKLLDKDLFNQSHYCLKCFQVKPPRSYHCGACKRCINRYDHHCPWTGNCVGARNHRTFLLFVFTLSTLIPIYFYVAFYYLQNIPIQKKYESYRCLFISGTICQWSLKDMFVLVASLTLFVNWCWVVVLAFTQICQVAHNVTTAEFRLFKRYGTLVPPTKQNSSPKNGHGIHGSFLRTVCGILGLDQCILLIRESNCFVRCFPSRAELGSQNSTSLSRNLSTVNPYDEGSIIKNCKTFWKQNFLNDGRQDEATRHV
Protein: DNA helicase (EC 3.6.4.12) (F5GWX5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEEDPEEDLSETETPKLKKKKKPKKPRDPKIPKSKRQKKELGDSSGEGPEFVEEEEEVALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLEDWGMEDIDHVFSEEDYRTLTNYKAFSQFVRPLIAAKNPKIAVSKMMMVLGAKWREFSTNNPFKGSSGASVAAAAAAAVAVVESMVTATEVAPPPPPVEVPIRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPKKVAPLKIKLGGFGSKRKRSSSEDDDLDVESDFDDASINSYSVSDGSTSRSSRSRKKLRTTKKKKKGEEEVTAVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHMVCLDPDMEKAPEGKWSCPHCEKEGIQWEAKEDNSEGEEILEEVGGDLEEEDDHHMEFCRVCKDGGELLCCDTCPSSYHIHCLNPPLPEIPNGEWLCPRCTCPALKGKVQKILIWKWGQPPSPTPVPRPPDADPNTPSPKPLEGRPERQFFVKWQGMSYWHCSWVSELQLELHCQVMFRNYQRKNDMDEPPSGDFGGDEEKSRKRKNKDPKFAEMEERFYRYGIKPEWMMIHRILNHSVDKKGHVHYLIKWRDLPYDQASWESEDVEIQDYDLFKQSYWNHRELMRGEEGRPGKKLKKVKLRKLERPPETPTVDPTVKYERQPEYLDATGGTLHPYQMEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRRLKADVFKNMPSKTELIVRVELSPMQKKYYKYILTRNFEALNARGGGNQVSLLNVVMDLKKCCNHPYLFPVAAMEAPKMPNGMYDGSALIRASGKLLLLQKMLKNLKEGGHRVLIFSQMTKMLDLLEDFLEHEGYKYERIDGGITGNMRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKKKMMLTHLVVRPGLGSKTGSMSKQELDDILKFGTEELFKDEATDGGGDNKEGEDSSVIHYDDKAIERLLDRNQDETEDTELQGMNEYLSSFKVAQYVVREEEMGEEEEVEREIIKQEESVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDGSQEDRDWQDDQSDNQSDYSVASEEGDEDFDERSEAPRRPSRKGLRNDKDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRYGMPPQDAFTTQWLVRDLRGKSEKEFKAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLIRKKVQEFEHVNGRWSMPELAEVEENKKMSQPGSPSPKTPTPSTPGDTQPNTPAPVPPAEDGIKIEENSLKEEESIEGEKEVKSTAPETAIECTQAPAPASEDEKVVVEPPEGEEKVEKAEVKERTEEPMETEPKGAADVEKVEEKSAIDLTPIVVEDKEEKKEEEEKKEVMLQNGETPKDLNDEKQKKNIKQRFMFNIADGGFTELHSLWQNEERAATVTKKTYEIWHRRHDYWLLAGIINHGYARWQDIQNDPRYAILNEPFKGEMNRGNFLEIKNKFLARRFKLLEQALVIEEQLRRAAYLNMSEDPSHPSMALNTRFAEVECLAESHQHLSKESMAGNKPANAVLHKVLKQLEELLSDMKADVTRLPATIARIPPVAVRLQMSERNILSRLANRAPEPTPQQVAQQQ
Protein: GH06117p (Pastrel, isoform F) (Q8IQ80)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RH08992p
- Delta-1-pyrroline-5-carboxylate synthase
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS5m
Sequence:
MANRLGNHEVTRTAREVQQNFAESLGYAEEIIWDLLSHEQHDVLRGKLCQLIRDSPEPKTATETEKDRKIRLKVNADNERARQIIFDSVWQQRELDLQIVYSIVHFFAALTAYNCFPGKYTNRQSLTAIIYVMVVTDETDVNRAEDARVFSVHPVFRARRCVVGSSGTSSVSSNCCNLFIDELGRVYQNWEMYVTTNELPAGVMVAPEKGIYRLVRDQVRLDKYTTPAGTTNRKVLGYLDTGSAVGGFFAACVPIAALLTLPVSAPLMGAAGVVGLASAGYAASRSGSKLFDRSQHEQSINVTDREARGHWLGVAGGTVGLAAAGATTVLTTATNAGREVGAITQLTVNSMNISSIVVSGTGVANGVLDLILKAKDGDEIVAMDVLQLSASLVLLTHSVYNFKLASTIINETSNANIADYRKNLSNRQRRTFDKAAKETVRMQGNTRGKLDIIRNVNEISPQEFNDLFKINKNLNQEGVRYSFAPDGKGFLLNGDVQTTGAELRASVQHNQGGNVLGKVSQPIPGSHAGSGRLQLGGVNQVSRLIGPLPTSHPRQEPSTYAAGVFALELSSVLVGGVVFVLEKYGKIIFEHVINAESFESLINIMANKLDPKVFDHIMLLTRAFMDTMLEDLTSVLKFFISTESVLYRILLYILRNFEDVQLSVIADHTCEIVEAVRVYFMSLNPNAFPGLLQKCPKCIGHFSVCPL