wanglab/gogpt-training-data huggingface dataset:
Protein: Dihydroxy-acid dehydratase (DAD) (EC 4.2.1.9) (P9WKJ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. Is specific for the (R) isomer of 2,3-dihydroxy-3-methylbutanoate, with no catalytic activity against the (S) isomer.
Interaction partners:
- Ketol-acid reductoisomerase
- Branched-chain-amino-acid aminotransferase
- 2-isopropylmalate synthase
- Acetolactate synthase large subunit IlvB1
- 3-isopropylmalate dehydratase large subunit
- 3-isopropylmalate dehydrogenase
- Putative acetolactate synthase small subunit
- L-threonine dehydratase biosynthetic IlvA
- 3-isopropylmalate dehydratase small subunit
- Glutamate synthase large chain
Sequence:
MPQTTDEAASVSTVADIKPRSRDVTDGLEKAAARGMLRAVGMDDEDFAKPQIGVASSWNEITPCNLSLDRLANAVKEGVFSAGGYPLEFGTISVSDGISMGHEGMHFSLVSREVIADSVEVVMQAERLDGSVLLAGCDKSLPGMLMAAARLDLAAVFLYAGSILPGRAKLSDGSERDVTIIDAFEAVGACSRGLMSRADVDAIERAICPGEGACGGMYTANTMASAAEALGMSLPGSAAPPATDRRRDGFARRSGQAVVELLRRGITARDILTKEAFENAIAVVMAFGGSTNAVLHLLAIAHEANVALSLQDFSRIGSGVPHLADVKPFGRHVMSDVDHIGGVPVVMKALLDAGLLHGDCLTVTGHTMAENLAAITPPDPDGKVLRALANPIHPSGGITILHGSLAPEGAVVKTAGFDSDVFEGTARVFDGERAALDALEDGTITVGDAVVIRYEGPKGGPGMREMLAITGAIKGAGLGKDVLLLTDGRFSGGTTGLCVGHIAPEAVDGGPIALLRNGDRIRLDVAGRVLDVLADPAEFASRQQDFSPPPPRYTTGVLSKYVKLVSSAAVGAVCG
Protein: BRCA1-associated RING domain protein 1 (BARD-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BARD1) (Q9QZH2)
Organism: Rattus norvegicus (Rat)
Function: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O70445}. Cytoplasm {ECO:0000250|UniProtKB:O70445}. Note=Can translocate to the cytoplasm. Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex. {ECO:0000250|UniProtKB:Q99728}.
Interaction partners:
- Breast cancer type 1 susceptibility protein homolog
- BRCA1-A complex subunit Abraxas 1
- DNA endonuclease RBBP8
- BRCA1-A complex subunit RAP80
- DNA 5'-3' helicase
- Double-strand break repair protein MRE11
- Nibrin
- DNA topoisomerase 2-binding protein 1
- Breast cancer type 2 susceptibility protein homolog
- BRISC and BRCA1-A complex member 1
Sequence:
MPRRPPRVCSGNKPPPVPAMEPATDGLWAHSRAALARLEKLLRCSRCANILREPVCLGGCEHIFCSGCISDCVGSGCPVCHTPAWILDLKINRQLDSMIQLYSKLQNLLHDNKGSDSKDDTSRASLFGDAERKKNSVKMWFSPRSKKIRCVVNKVSVQTQPQKAKDDKAQEASVFEFVSATPPVVVSTRAKTASRTSAKKHPKKSVAKINREGNFRPETRDSRFDSKEKLKEEKVVSFSQTLVMENSRVNGEIDLLASGSVVESVFSGSFAEVSLPLAEHIVSPDTVSKSEEAPEKKVCVEDRCPVGSDGNPKGCHRPPTSTSKKCGSNVPSASGEIREPTLLAENVVLVDCSSLPSGRLQVDVTLRRQSNASDDSLSLSPGTPPSLLNNSTHRQMMSKPSTVKLSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDYTDAENIRSLLLLPEKTDSFSTSQCSVQVNTGQRKSGPLVLIGSGLSSQQQKLLSKLETVLKAKKCAEFDNTVTHVIVPDEEAQSTLKCMLGILNGCWVLKFDWVKACLDSQEREQEEKYEVPGGPQRSRLNREQLLPKLFDGCYFFLGGNFKHHPKEDLLKLIAAAGGRILSRKPKPDSDVTQTINTVAYHAKPDSDQRFCTQYIVYEDLFNCHPERVRQGKVWMAPSTWLISCVMAFELLPLDS
Protein: U5 small nuclear ribonucleoprotein 200 kDa helicase (EC 3.6.4.13) (Protein lethal (3) 72Ab) (Q9VUV9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome (By similarity). Plays a role in pre-mRNA splicing (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O75643}.
Interaction partners:
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-processing factor 6
- Splicing factor 3B subunit 3
- Thioredoxin-like protein
- Pre-mRNA-processing factor 17
- Splicing factor 3B subunit 1
- U5 small nuclear ribonucleoprotein 40 kDa protein
- Puff-specific protein Bx42
- Precursor RNA processing 3, isoform A
Sequence:
MADAAARQLQYEYKANSNLVLQADVRLIERPRRDEATGEVCSLVGKLDGTRMGDRYQRTKPEKTEERKVKRQKRDEAQYDFERMKGATLLSEGIDEMVGIVYRPKTQETRQTYEVLLSFIQEALGDQPRDILCGAADEILAVLKNDRLKDRERKKDIDSLLGAVTDERFALLVNLGKKITDFGSDAVNALTAAPNNEEQIDETYGINVQFEESEEESDNDMYGEIRDDDAQDEGEEARIDHTLHAENLANEEAANNVKKERSLHPLDIDAYWLQRCLSKFYKDAMVSQSKAADVLKILKDAADDRDCENQLVLLLGYDCFDFIKQLKLNRQMVLYCTMLASAQTDSERQRIREKMRGNSALAKILRQLDTGKSEDQEEGEARGSKRGKGDAEDGGAAAAGQVAGVRQLLELEEMAFTQGSHFMANKRCQLPDGSYRKQRKGYEEVHVPALKPVPFDANEELQPVDKLPKYVQPVFEGFKTLNRIQSRLYKAALDSDENMLLCAPTGAGKTNVALLTMMREIGKHINEDGTINAQDFKIIYVAPMKSLVQEMVGNFGRRLACYNLTVSELTGDHQLTREQIAATQVIVCTPEKWDIITRKGGERTFVSLVRLVIIDEIHLLHDERGPVLEALVARTIRNIETTQEEVRLVGLSATLPNYQDVATFLRVKPDKGLFYFDNSYRPVSLEQQYIGVTEKKALKRFQVMNEIVYEKTMEHAGRNQVLVFVHSRKETGKTARAVRDMCLEQDTLGSFLKEGSASMEVLRTEAEQVKNTELKELLPYGFAIHHAGMTRVDRTLVEDLFADRHIQVLVSTATLAWGVNLPAHTVIIKGTQVYNPEKGRWVELSALDVLQMLGRAGRPQYDTKGEGILITNHSELQFYLSLLNQQLPIESQFISKLPDMLNAEIVLGTVQHLQDAVNWLGYTYLYIRMLRNPTLYGVSHDAIKADPLLEQHRADLLHTAACCLERSGLIKYDRKTGHFQVTDLGRIASHYYLTHETMLTYNQLLKQTLSEIELFRVFSLSSEFRHISVREEEKLELQKLMERVPIPIKESIEEHSAKVNVLLQAYISQLKLEGFALMSDMVFITQSAARLMRAIFEIVLTRGWAQLADKTLTLCKMIDRRMWQSMTPLRQFKKMPDEIAKKLEKKHFPWGRLYDLEPHELGELIRVPKLGKTIHKFVHQFPKLELSTHIQPITRGTLRVELTITPDFQWDEKVHGQSEGFWVLIEDVDSELILHHEFFLLKQKYSQDEHQLKFFVPVFEPLPPQYFLRIVSDRWIGAETQLPVSFRHLILPEKNMPPTELLDLQPLPISALRQPKFESFYSQRFPQFNPIQTQVFNAVYNSDENVFVGAPTGSGKMTIAEFAIMRLFTTQSDARCVYLVSEEALADLVFADWHSKFGSLDIKVVKLTGETGTDLKLIAKGQLVITTADKWDVLSRRWKQRKNVQLVNLFIVDELQLVGGEEGPVLEIVCSRMRYISSQIEKQIRIVALSASLTDARDVAQWLGCNPNATFNFHPSVRPIPLELHIQGYNVTHNATRIATMSKPVYNAILKYSAHKPVIVFVSSRKQARLTAIDVLTYAASDLQPNRFFHAEEEDIKPFLERMTDKTLKETLAQGVAYLHEGLSASDHRLVEQLFDSGAVQVAVISRDLCWGMSISAHLVIIMDTQFYNGKNHSYEDYPITDVLQMIGRANRPNEDADAKCVLMCQSSKKDFFKKFINEPLPIESHLDHRMHDHFNAEVVTKTIENKQDAVDYLTWTFLYRRLTQNPNYYNLQGVTHRHLSDHLSELVENTLSDLEQSKCISVEDDMDTLPLNLGMIAAYYYINYTTIELFSLSLNSKTKVRGLLEIISSAAEYEDVVVRHHEEQVLRTLSQRLPNKLTGPNETAPKFNDPHIKTNLLLQAHLSRLQLGPELQGDTEQILSKAIRLIQACVDVLSSNGWLSPAVAAMELAQMVTQAMWSKDSYLKQLPHFSPEIVKRCTEKKIETVFDIMELEDEDRTRLLQLSDLQMADVARFCNRYPNIELNYEVVDKDRINSGSTVNVVVQLEREDEVTGPVIAPFFPQKREEGWWVVIGDPKTNSLLSIKRLTLQQKAKVKLDFVAPSPGKHDYTLYYMSDSYLGCDQEYKFSIEVGDFQSESESESD
Protein: Plexin A (Q8STG6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
TLQHYNVPDGAGLSLVPKQSSIYNFSILSDKNEKSHKYETLNISKYTSSSPTFSRAGSPLNNDMHENGLRYWHLVKHHDSDMQKEGERVNKLVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDDQAQLHGITDPEVVHTWKSNSLPLRFWVNLIKNPNFVFDIHKSNIVDSCLSVVAQTFMDSCSTSDHRLGKDSPSSKLLYAKDIPEYRKWVDRYYRDIRDMSPISDQDMNAMLAEESRLHTTEFNTNCALHELYTYAV
Protein: Disintegrin and metalloproteinase domain-containing protein 23 (ADAM 23) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 3) (MDC-3) (O75077)
Organism: Homo sapiens (Human)
Function: May play a role in cell-cell and cell-matrix interactions. This is a non-catalytic metalloprotease-like protein.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Secreted.
Interaction partners:
- Leucine-rich glioma-inactivated protein 1
- Disintegrin and metalloproteinase domain-containing protein 22
- Leucine-rich repeat LGI family member 3
- Leucine-rich repeat LGI family member 2
- Disks large homolog 4
- Leucine-rich repeat LGI family member 4
- Voltage-dependent calcium channel gamma-2 subunit
- Potassium voltage-gated channel subfamily A member 1
Sequence:
MKPPGSSSRQPPLAGCSLAGASCGPQRGPAGSVPASAPARTPPCRLLLVLLLLPPLAASSRPRAWGAAAPSAPHWNETAEKNLGVLADEDNTLQQNSSSNISYSNAMQKEITLPSRLIYYINQDSESPYHVLDTKARHQQKHNKAVHLAQASFQIEAFGSKFILDLILNNGLLSSDYVEIHYENGKPQYSKGGEHCYYHGSIRGVKDSKVALSTCNGLHGMFEDDTFVYMIEPLELVHDEKSTGRPHIIQKTLAGQYSKQMKNLTMERGDQWPFLSELQWLKRRKRAVNPSRGIFEEMKYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEQLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQRIKQHADAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGLPMAVAQVLSQSLAQNLGIQWEPSSRKPKCDCTESWGGCIMEETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRPTKLFEPTECGNGYVEAGEECDCGFHVECYGLCCKKCSLSNGAHCSDGPCCNNTSCLFQPRGYECRDAVNECDITEYCTGDSGQCPPNLHKQDGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLTRAPRIGQLQGEIIPTSFYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCLQIQALNMSSCPLDSKGKVCSGHGVCSNEATCICDFTWAGTDCSIRDPVRNLHPPKDEGPKGPSATNLIIGSIAGAILVAAIVLGGTGWGFKNVKKRRFDPTQQGPI
Protein: Cancer-related nucleoside-triphosphatase (NTPase) (EC 3.6.1.15) (Nucleoside triphosphate phosphohydrolase) (Q9BSD7)
Organism: Homo sapiens (Human)
Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency.
Interaction partners:
- Ribonucleoside-diphosphate reductase large subunit
- Ectonucleoside triphosphate diphosphohydrolase 2
- Nucleoside diphosphate kinase homolog 7
- Nucleoside diphosphate kinase 6
- Nucleoside diphosphate kinase, mitochondrial
- Nucleoside diphosphate kinase A
- Nucleoside diphosphate kinase B
- Nucleoside diphosphate kinase 3
- Nucleoside diphosphate kinase
- Adenylate kinase 2, mitochondrial
Sequence:
MARHVFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTLSGTRGPLSRVGLEPPPGKRECRVGQYVVDLTSFEQLALPVLRNADCSSGPGQRVCVIDEIGKMELFSQLFIQAVRQTLSTPGTIILGTIPVPKGKPLALVEEIRNRKDVKVFNVTKENRNHLLPDIVTCVQSSRK
Protein: Omega, isoform H (EC 3.4.14.1, EC 3.4.14.2, EC 3.4.14.4, EC 3.4.14.5) (M9PCH6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHTKEKKRRVRIILTVVTTVIAVALLATALVFILRTDEKDADDSDSNSNNAIDLEDVLSGQLYAKRFNGSWSNGNSLIYKENTSIMEFDAKTGERSILLEDAQHYVLYEKSADGEFLLLAKNYKKNFRYSFLAEYDLYNLNTKEFIQLTIQNEQHYLSMVQWSPVGNALVINYDRNLYYKESALAQEIALTSDEQAGILNGIPDWVYEEEVFSSNVATWFNPSGTQLAFIKFDDSSTHLINFPYYGDAGDLRYQYPLHQVIAYPKAGSSNPRVELVMVDLKRAVAGGDFVTVMPVPSALNTETDYIVTVVSWVDDDNVLSIWMNRIQNAAYVVTFDGLNRKVIYSAESKTGWVDLYTAPFRNRNGSRLAFVLPHNNYKHVQLLSSTVASSEPQALEPLTEGKYVVDSILHWDGKNDIIFYTANTEDHPEQLHLYAIRALAKQSPKCLTCNLIKSGDVQQTYFSATFNDNNHIVITSLGPGIPTTHIYEWKYENSQVVISKVLDWETNESLRAKLKGVALPSHKILTVDIDGGFQAKVLLQLPPNLDTSGATKYPMLVDVYGGPDSYSVTNKWMVDWGTYLSSNQSVIYAKIDGRGSGLRGESLLHAIYLKLGTVEISDQINVTQKLSTLFNYIDPDHVGIWGWSYGGYAAAMALANDEAKVFKCAASIAPVTDWAYYDSIYTERYMGLPNTNELGYANSRLSTMAVKLRGKKYLLVHGTLDDNVHYQQAMILAKNLERQDILFKQISYADEDHGLSNVRPHLYHSLDRFFGECFASSRLMKSAK
Protein: TRAF-interacting protein with FHA domain-containing protein B (TIFA-like protein) (Q8JZM6)
Organism: Mus musculus (Mouse)
Function: Inhibits TIFA-mediated TRAF6 activation possibly by inducing a conformational change in TIFA.
Interaction partners:
Sequence:
MERPLTVLQVSLYHPTQGPVAFAHVPQQLQHDASRLLVGRGQNTHLQLQLPQLSRYHLSLEPYLEKGSSLLAFCLKVLTRKSCVWVNGLPLRYLEQVPLGTINRISFSGIQMLVRKEGGASLETFVCYFHLSPSPLIYRPKAQETDE
Protein: Valine--tRNA ligase (EC 6.1.1.9) (Valyl-tRNA synthetase) (ValRS) (Q04462)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Elongation factor 1-gamma
- Methionine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Tyrosine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Elongation factor 1-delta
- Aspartate--tRNA ligase, mitochondrial
- Valine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, cytoplasmic
Sequence:
MSILYVSPHPDAFPSLRALIAARYGEAGDGPGWGGPHPRICLQPPPSSRTPFPPPRLPALEQGPGGLWVWGAPAVAQLLWPAGLGGPGGSRAAVLVQQWVSYADTELTPAACGATLPALGLRGPGQDPQAALGALGKALNPLEEWLRLHTYLAGDAPTLADLAAVTALLLPFRYVLDPSARRIWGNVTRWFNTCVRQPEFRAVLGEVVLYSGARSVTQQPGSEITAPQKTAAQLKKEAKKREKLEKFQQKQKTQQQQPAHGEKKPKPEKKEKRDPGVITYDLPTPPGEKKDVSGTMPDSYSPQYVEAAWYPWWERQGFFKPEYGRPSVSAPNPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLQEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKELTGRTLLSVPGYKEKVEFGVLVSFAYKVQGSDSDEEVVVATTRIETMLGDVAVAVHPKDPRYQHLKGKSVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIMDSKGALVNVPPPFLGLPRFEARKAVLAALKEQGLFRGIKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFITVHDPAVPPGEDPDGRYWVSGRTEAEAREKAAREFGVSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTEKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIHGVSLQGLHDQLLNSNLDPSEVEKAKEGQRADFPAGIPECGTDALRFGLCAYTSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSPTSKPEGHESLVDRWIRSRLAEAVRLSNEGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVLNGVDQVAADCARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPNAPASLCVTPYPEPSECSWKDPEAEAALELALSITRAVRSLRADYNLTRTRPDCFLEVADEATGALASAVSAYVQTLASAGVVAVLALGAPAPQGCAVAVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASGYSAKVPLEVQEADEVKLQQTEAELRKVDEAIALFQKML
Protein: Palmitoyltransferase ZDHHC11 (EC 2.3.1.225) (DHHC-containing protein 10) (DHHC10(z11)) (Zinc finger DHHC domain-containing protein 11) (DHHC-11) (Q14AK4)
Organism: Mus musculus (Mouse)
Function: Endoplasmic reticulum-localized palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes. Has a palmitoyltransferase activity toward NCDN and regulates NCDN association with endosome membranes through this palmitoylation. May play a role in cell proliferation (By similarity).
Subcellular location: Endosome membrane {ECO:0000269|PubMed:23687301}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Palmitoyltransferase ZDHHC22
- Palmitoyltransferase ZDHHC13
Sequence:
MKEMNICGINKNWVLPEAQENNVKKFLPRPLSRVNGWSPPLHSFQAISWITYLAMSIVTFGIFIPFLPYSWKYAANIVMGGVFIFHLIVHLIAITIDPADTNVRLKKDYTQPVPAFDRSKHTHVIQNQYCHLCEVTASKKAKHCSACNKCVSGFDHHCKWLNNCVGRRNYWFFFWSVASAAVGILGVMIILCYICIQYFVNPDELRTDPLYKEIISENTWLLFLSLWPVPVKTPIVLSIAVMALLLAIASFVMLGHLLIFHLYLITKNMSTFDYLMKTRFKKNLHPAEEKELPLQKKGDLPQEKSDNWAWPKSPPRVGSQKFPVSTLSPKSSVCFVASPPKICHSED
Protein: Cyclin-dependent kinase 15 (EC 2.7.11.22) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 7 protein) (Cell division protein kinase 15) (Serine/threonine-protein kinase ALS2CR7) (Serine/threonine-protein kinase PFTAIRE-2) (Q96Q40)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase that acts like an antiapoptotic protein that counters TRAIL/TNFSF10-induced apoptosis by inducing phosphorylation of BIRC5 at 'Thr-34'.
Interaction partners:
- Cyclin-Y
Sequence:
MGQELCAKTVQPGCSCYHCSEGGEAHSCRRSQPETTEAAFKLTDLKEASCSMTSFHPRGLQAARAQKFKSKRPRSNSDCFQEEDLRQGFQWRKSLPFGAASSYLNLEKLGEGSYATVYKGISRINGQLVALKVISMNAEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTDLAQYMSQHPGGLHPHNVRLFMFQLLRGLAYIHHQHVLHRDLKPQNLLISHLGELKLADFGLARAKSIPSQTYSSEVVTLWYRPPDALLGATEYSSELDIWGAGCIFIEMFQGQPLFPGVSNILEQLEKIWEVLGVPTEDTWPGVSKLPNYNPEWFPLPTPRSLHVVWNRLGRVPEAEDLASQMLKGFPRDRVSAQEALVHDYFSALPSQLYQLPDEESLFTVSGVRLKPEMCDLLASYQKGHHPAQFSKCW
Protein: Small ribosomal subunit protein eS7 (40S ribosomal protein S7) (P62082)
Organism: Mus musculus (Mouse)
Function: Required for rRNA maturation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P62081}. Cytoplasm {ECO:0000250|UniProtKB:P62081}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62081}. Note=Although RPS7 is functional within the cytoplasm, the assembly of ribosomal subunits occurs in the nucleus. RPS7 nuclear import is mediated by IPO5/RanBP5, IPO7/RanBP7, KPNB1/importin-beta or TPNO1/Trn. Colocalizes with NEK6 in the centrosome. {ECO:0000250|UniProtKB:P62081}.
Interaction partners:
- Large ribosomal subunit protein eL21
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein eS4
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS26
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS8
Sequence:
MFSSSAKIVKPNGEKPDEFESGISQALLELEMNSDLKAQLRELNITAAKEIEVGGGRKAIIIFVPVPQLKSFQKIQVRLVRELEKKFSGKHVVFIAQRRILPKPTRKSRTKNKQKRPRSRTLTAVHDAILEDLVFPSEIVGKRIRVKLDGSRLIKVHLDKAQQNNVEHKVETFSGVYKKLTGKDVNFEFPEFQL
Protein: Elongator complex protein 1 (AtELP1) (Elongator component 1) (Protein ABA-OVERLY SENSITIVE 1) (Protein ELONGATA 2) (Q9FNA4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). Promotes organ development by modulating cell division rate. Required for auxin distribution or signaling. Prevents abscisic acid (ABA) signaling leading to stomatal closure and seedling growth inhibition. Involved in oxidative stress signaling. Prevents anthocyanin accumulation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Elongator complex protein 3
- Elongator complex protein 2
- Protein KTI12 homolog
- Elongator complex protein 4
- Radical S-adenosyl methionine domain-containing protein 1, mitochondrial
- Elongator complex protein 5
- Elongator complex protein 6
- Pre-rRNA-processing ESF1-like protein
- tRNA
- tRNA
Sequence:
MKNLKLFSEVPQNIQLHSTEEVVQFAAYDIDQSRLFFASSANFVYALQLSSFQNESAGAKSAMPVEVCSIDIEPGDFITAFDYLAEKESLLIGTSHGLLLVHNVESDVTELVGNIEGGVKCISPNPTGDLLGLITGLGQLLVMTYDWALMYEKALGEVPEGGYVRETNDLSVNCGGISISWRGDGKYFATMGEVYESGCMSKKIKIWESDSGALQSSSETKEFTQGILEWMPSGAKIAAVYKRKSDDSSPSIAFFERNGLERSSFRIGEPEDATESCENLKWNSASDLLAGVVSCKTYDAIRVWFFSNNHWYLKQEIRYPREAGVTVMWDPTKPLQLICWTLSGQVSVRHFMWVTAVMEDSTAFVIDNSKILVTPLSLSLMPPPMYLFSLSFSSAVRDIAYYSRNSKNCLAVFLSDGNLSFVEFPAPNTWEDLEGKDFSVEISDCKTALGSFVHLLWLDVHSLLCVSAYGSSHNKCLSSGGYDTELHGSYLQEVEVVCHEDHVPDQVTCSGFKASITFQTLLESPVLALAWNPSKRDSAFVEFEGGKVLGYASRSEIMETRSSDDSVCFPSTCPWVRVAQVDASGVHKPLICGLDDMGRLSINGKNLCNNCSSFSFYSELANEVVTHLIILTKQDFLFIVDTKDVLNGDVALGNVFFVIDGRRRDEENMSYVNIWERGAKVIGVLNGDEAAVILQTMRGNLECIYPRKLVLSSITNALAQQRFKDAFNLVRRHRIDFNVIVDLYGWQAFLQSAVAFVEQVNNLNHVTEFVCAMKNEDVTETLYKKFSFSKKGDEVFRVKDSCSNKVSSVLQAIRKALEEHIPESPSRELCILTTLARSDPPAIEESLLRIKSVREMELLNSSDDIRKKSCPSAEEALKHLLWLLDSEAVFEAALGLYDLNLAAIVALNSQRDPKEFLPYLQELEKMPESLMHFKIDIKLQRFDSALRNIVSAGVGYFPDCMNLIKKNPQLFPLGLLLITDPEKKLVVLEAWADHLIDEKRFEDAATTYLCCCKLEKASKAYRECGDWSGVLRVGALMKLGKDEILKLAYELCEEVNALGKPAEAAKIALEYCSDISGGISLLINAREWEEALRVAFLHTADDRISVVKSSALECASGLVSEFKESIEKVGKYLTRYLAVRQRRLLLAAKLKSEERSVVDLDDDTASEASSNLSGMSAYTLGTRRGSAASVSSSNATSRARDLRRQRKSGKIRAGSAGEEMALVDHLKGMRMTDGGKRELKSLLICLVTLGEMESAQKLQQTAENFQVSQVAAVELAHDTVSSESVDEEVYCFERYAQKTRSTARDSDAFSWMLKVFISP
Protein: C-C motif chemokine 8 (Monocyte chemoattractant protein 2) (Monocyte chemotactic protein 2) (MCP-2) (Small-inducible cytokine A8) (Q9Z121)
Organism: Mus musculus (Mouse)
Function: Chemotactic factor that attracts monocytes. This protein can bind heparin (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- C-C chemokine receptor type 2
- C-C chemokine receptor type 5
- C-C chemokine receptor type 1
- Probable C-C chemokine receptor type 3
- C-C motif chemokine 6
- C-C motif chemokine 12
- C-C motif chemokine 27
- C-C motif chemokine 2
- Atypical chemokine receptor 4
- C-C motif chemokine 7
Sequence:
MKIYAVLLCLLLIAVPVSPEKLTGPDKAPVTCCFHVLKLKIPLRVLKSYERINNIQCPMEAVVFQTKQGMSLCVDPTQKWVSEYMEILDQKSQILQP
Protein: Transcription factor gaf1 (Gaf-1) (Q10280)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transcriptional activator.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Sexual differentiation process protein isp7
- Transcription factor ste11
Sequence:
MDLKFSNFFKEAEHPALVKKFDKSTTDESSSKEDYSTMSDLWKMFSKAKSELSNGRRVENLTWRLMSINLQKNLTPNGDSNTLTPDTFSDPTAPSSAQSVPPTSSAETTADNSDTEMKLNPIPAYSVPADTTGSSLMEFNYIQRRVRKTSFDESTAKSKKRSIADSHFPDPNAMQRPHDLESQPFSYPKIHASNSFNFVKRDIDSSNFSNLDASALPISPPSDFFSVHSHNLPNAPPSIPANSNNSASPNQRIKASPKHADTDVLGLDFDMTPSEPSSFPENGGFPSFVDANTHEQTLFPSSATNSFSFEHGSAGFPIPGSVPSTSYHANTASEDGFSSSYNSQGLFGISSPLSSGVTPNQSFFPDVSGNNIFDVSRNNHEVSSPLIQSPGSYVSMPSINMVSSLPISAPVPNSNSQFPRRPNTFRTNSSKSVGQGSSGVDSNQENAESFNPSISSHNSAEWASGETTGHSSNSPLPGSDMFSPQFMRVGTAMGVAPVRSNSSNNFGQNFFHQTSPQFSAVPHRKVSAQDTNLMGSSPGMYNHMPYLNRATSANSITSPGVLPEGMAASLKKRTTNTAATPQAALPTTLDTKKDRSVSFNINKNAEKPTVSNAAEDKKGDANTRRANATNPTPTCTNCQTRTTPLWRRSPDGQPLCNACGLFMKINGVVRPLSLKTDVIKKRNRGVGTSATPKQSGGRKGSTRKSSSKSSSAKSTAADMKPKADSKSISPGFVGGNQSLSSERIPLDPSMRSPLQQQSSENESKSQSMLSANNLNAGVNDFGLGFSEGLGSAHLDSNDSSMVQGKNDFAPVVDSPLFDAFDTDLGMSSVAESHTMNMDPSDLSRVSKSWDWYSVM
Protein: Transmembrane protein 41B (Protein stasimon) (A1A5V7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes. Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine. Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted by atg2 (atg2a or atg2b) to mediate autophagosome assembly. In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required (By similarity). Required for normal motor neuron development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5BJD5}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5BJD5}. Note=Localized to specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria. {ECO:0000250|UniProtKB:Q5BJD5}.
Interaction partners:
- Chondrolectin
- WD repeat domain 46.
- Vacuole membrane protein 1
- Heterogeneous nuclear ribonucleoprotein R.
- Plastin-3
Sequence:
MAKKRAGNRETESSPLVEQEPRPSKETPVPKGAQSPGGASARMSILLLVVIFACSACVMYLVFRNFPQLSEDEREKIKIPKDMEDAKALGTVLSKYKDTYYTQVLLAYFATYIFLQTFAIPGSIFLSILSGYLYPFPLALFLVCLCSGLGASFCYMLSYLVGRPMVYKYLTERAQKWSQQVDKHREHLINYIIFLRITPFLPNWFINITSPVINVPLGVFFLGTFLGVAPPSFVAINAGTTLYKLTTAGEAVSWNSLLVLGVLAVVSILPVCFQKKLQQKLE
Protein: CD44 antigen (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (Phagocytic glycoprotein I) (K7GN90)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cell projection, microvillus {ECO:0000256|ARBA:ARBA00004105}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDTFWWRAAWGLCLVQLSLAQIDLNITCRYAGVFHVEKNGRYSISKTEAADLCKAFNSTLPTMAQMEAALNIGFETCRYGFIDGHVVIPRIHPNAICAANNTGVYILASNTSQYDTYCFNASAPPEEDCTSVTDLPNTFEGPITITIVNRDGTRYTKKGEYRTNPEDINPNMAPEDDMSSGSSSERSTSGGYSIFHTHLPTTTHPDQEGPWVSSNPEDTPATNEDASHSTTLQPSADPHTGLVEDLDRTGLSVTAQQSDTQSSSTSHGGLEEDKDHPVAATPTSSNRNDGRSGRRGGSLPEDSATSVEGYTLHSPDTNEYRTLILVTPTKTGSPGVTEVTIVGDSTSNVDLSSSEDQDPYFDPSGRSFTTHGSESAGHSSGSQEGEANTTSGPIRKSQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINNGNGPVEERKPSGLNGEASKSQEMVHLVNKESTETPDQFMTADETRNLQNVDMKIGV