wanglab/gogpt-training-data huggingface dataset:
Protein: Oxidant-induced cell-cycle arrest protein 5 (P38738)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for replication of brome mosaic virus (BMV), a positive-strand RNA virus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Tyrosine-protein phosphatase-like protein OCA2
- Protein OCA4
- Putative tyrosine-protein phosphatase OCA1
- Inositol diphosphatase SIW14
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Fumarate hydratase, mitochondrial
- Citrate synthase, mitochondrial
- Citrate synthase 3, mitochondrial
- Citrate synthase, peroxisomal
Sequence:
MHDKKSPMANSHYLKNLKQQFRNKNLIETTIHLVKCNDHDSLAFLARTYGVPPQLRHVVWPILLKYHPMCISPNITSNTISWDPITNDFILNDPFLKSKAPTDKQDKSDDENILPYDIESIILHDLKKYFHSRSNPAGSSSNANTTNIATPTPVSSSDASTISSMEVLSPSLDYEFQIIETLKNAIVKFLLKWSKIFKYESGLAWIALGLAEWYPIYPYETMSPFNETHSFYEVEDYVVLSGRKHALLSTNNGNNGNSNSSSNNTNNNNTNITSGMHNLSINTNTSLHNSPYISHTLSYLYKEYPLPFELRSKLPTKPIFSFSALFERLALVILHCPDTILAHKQLKNDSNASSSSKANSNFNTNYFPIISGGDLSFQTQVFFKVFSSILPELYQPLTEESSLQPSSSRNSWIYWWLKCSGAKALQRQDRGRVWDLLLGWRPKPNMDTINFFLNYNDKKMDHLYHDTPQCDNEQYWMKDWIALYNNDPFWFPDLDSMALGSKKFPYDYSVFKELILRNRYGGTQSKAQKDNTVPSPGSDSNDKSELKLPFSSIDPHMQLIFIFIAILQFNEFKLLEFEEAEISEFLNNVPLLTKFDDSSYRKLYENTESSITSLPSSPTTSTMASLQSSSNSSAHISNYHMLIEVGNDAKASHCFDDLLNMAGDIWRKWLWRELEESSL
Protein: ATP-citrate synthase (EC 2.3.3.8) (ATP-citrate (pro-S-)-lyase) (ACL) (Citrate cleavage enzyme) (P53396)
Organism: Homo sapiens (Human)
Function: Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate for de novo cholesterol and fatty acid synthesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:9116495}.
Interaction partners:
- Citrate synthase, mitochondrial
- Fatty acid synthase
- Succinate--CoA ligase subunit alpha, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Acetyl-CoA carboxylase 1
- Aconitate hydratase, mitochondrial
- Cytoplasmic aconitate hydratase
- Malate dehydrogenase, mitochondrial
- Pyruvate carboxylase, mitochondrial
- Acetyl-CoA carboxylase 2
Sequence:
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALGHRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVPSPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMSM
Protein: Basic-leucine zipper (BZIP) transcription factor family protein (Putative bZIP transcription factor) (Q9SL54)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- At5g04840
Sequence:
MNGSDNSTPSRPRSITQPSLAFSSLPPLSPSPSSSRRNSIPLMNPSASVESRDSSIRVKKKSLLPPLCVKRRAPKDDIEPFKRHYRSLSVDSCLSDLLKLPPSPNNVSSSRSVDGEQNASELEFDTSVYTDDELNKIAKSTKLKEVASDPKEVRRILKNQESAARSKQKKLQYMINLELKINFLENKNASIFEKIKLLENDKTMRMNEKKEIMIRIESLEQHAELRDALTEHLHVEIERLKAVLISNEKGNEKSPKSRDDNM
Protein: Hca operon transcriptional activator HcaR (Q47141)
Organism: Escherichia coli (strain K12)
Function: Transcriptional activator of the hca operon for 3-phenylpropionic acid catabolism.
Interaction partners:
- 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin subunit
- 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha
- Glc operon transcriptional activator
- HTH-type transcriptional regulator DmlR
- HTH-type transcriptional activator AaeR
- HTH-type transcriptional regulator PgrR
- Transcriptional activator FeaR
- DNA-binding transcriptional activator MhpR
- Probable HTH-type transcriptional regulator LrhA
- Uncharacterized HTH-type transcriptional regulator YhjC
Sequence:
MELRHLRYFVAVAQALNFTRAAEKLHTSQPSLSSQIRDLENCVGVPLLVRDKRKVALTAAGECFLQDALAILEQAENAKLRARKIVQEDRQLTIGFVPSAEVNLLPKVLPMFRLRQPDTLIELVSLITTQQEEKIRRGELDVGLMRHPVYSPEIDYLELFDEPLVVVLPVDHPLAHEKEITAAQLDGVNFVSTDPVYSGSLAPIVKAWFAQENSQPNIVQVATNILVTMNLVGMGLGVTLIPGYMNNFNTGQVVFRPIAGNVPSIALLMAWKKGEMKPALRDFIAIVQERLASVTA
Protein: Galactoside alpha-(1,2)-fucosyltransferase 1 (Alpha(1,2)FT 1) (Blood group H alpha 2-fucosyltransferase) (Fucosyltransferase 1) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1) (Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT1) (EC 2.4.1.69) (Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT1) (EC 2.4.1.344) (P19526)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose residue of glycoconjugates through an alpha(1,2) linkage leading to H antigen synthesis that is an intermediate substrate in the synthesis of ABO blood group antigens. H antigen is essential for maturation of the glomerular layer of the main olfactory bulb, in cell migration and early cell-cell contacts during tumor associated angiogenesis. Preferentially fucosylates soluble lactose and to a lesser extent fucosylates glycolipids gangliosides GA1 and GM1a (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:O09160}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O09160}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250|UniProtKB:O09160}.
Interaction partners:
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6
- Alpha-
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- Beta-1,3-galactosyltransferase 5
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
- Beta-1,3-galactosyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
Sequence:
MWLRSHRQLCLAFLLVCVLSVIFFLHIHQDSFPHGLGLSILCPDRRLVTPPVAIFCLPGTAMGPNASSSCPQHPASLSGTWTVYPNGRFGNQMGQYATLLALAQLNGRRAFILPAMHAALAPVFRITLPVLAPEVDSRTPWRELQLHDWMSEEYADLRDPFLKLSGFPCSWTFFHHLREQIRREFTLHDHLREEAQSVLGQLRLGRTGDRPRTFVGVHVRRGDYLQVMPQRWKGVVGDSAYLRQAMDWFRARHEAPVFVVTSNGMEWCKENIDTSQGDVTFAGDGQEATPWKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLKIFKPEAAFLPEWVGINADLSPLWTLAKP
Protein: Kelch-like protein 22 (Q53GT1)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not lead to PLK1 degradation. The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway. It is therefore an amino acid-dependent activator within the amino acid-sensing branch of the TORC1 pathway, indirectly regulating different cellular processes including cell growth and autophagy.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:29769719}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23455478}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23455478}. Nucleus {ECO:0000269|PubMed:29769719}. Lysosome {ECO:0000269|PubMed:29769719}. Note=Mainly cytoplasmic in prophase and prometaphase. Associates with the mitotic spindle as the cells reach chromosome bi-orientation. Localizes to the centrosomes shortly before cells enter anaphase After anaphase onset, predominantly associates with the polar microtubules connecting the 2 opposing centrosomes and gradually diffuses into the cytoplasm during telophase (PubMed:23455478). Localizes to the nucleus upon amino acid starvation (PubMed:29769719). Relocalizes to the cytosol and associates with lysosomes when amino acids are available (PubMed:29769719). {ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:29769719}.
Interaction partners:
- Cullin-3
- Kelch-like protein 13
- E3 ubiquitin-protein ligase RBX1
- Leucine-zipper-like transcriptional regulator 1
- Kelch-like protein 9
- Kelch-like protein 21
- Kelch-like protein 20
- Speckle-type POZ protein
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
- Kelch-like protein 12
Sequence:
MAEEQEFTQLCKLPAQPSHPHCVNNTYRSAQHSQALLRGLLALRDSGILFDVVLVVEGRHIEAHRILLAASCDYFRGMFAGGLKEMEQEEVLIHGVSYNAMCQILHFIYTSELELSLSNVQETLVAACQLQIPEIIHFCCDFLMSWVDEENILDVYRLAELFDLSRLTEQLDTYILKNFVAFSRTDKYRQLPLEKVYSLLSSNRLEVSCETEVYEGALLYHYSLEQVQADQISLHEPPKLLETVRFPLMEAEVLQRLHDKLDPSPLRDTVASALMYHRNESLQPSLQSPQTELRSDFQCVVGFGGIHSTPSTVLSDQAKYLNPLLGEWKHFTASLAPRMSNQGIAVLNNFVYLIGGDNNVQGFRAESRCWRYDPRHNRWFQIQSLQQEHADLSVCVVGRYIYAVAGRDYHNDLNAVERYDPATNSWAYVAPLKREVYAHAGATLEGKMYITCGRRGEDYLKETHCYDPGSNTWHTLADGPVRRAWHGMATLLNKLYVIGGSNNDAGYRRDVHQVACYSCTSGQWSSVCPLPAGHGEPGIAVLDNRIYVLGGRSHNRGSRTGYVHIYDVEKDCWEEGPQLDNSISGLAACVLTLPRSLLLEPPRGTPDRSQADPDFASEVMSVSDWEEFDNSSED
Protein: Transcription elongation factor, mitochondrial (Q96QE5)
Organism: Homo sapiens (Human)
Function: Transcription elongation factor which increases mitochondrial RNA polymerase processivity. Regulates transcription of the mitochondrial genome, including genes important for the oxidative phosphorylation machinery.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:21278163}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:21278163}.
Interaction partners:
- DNA-directed RNA polymerase, mitochondrial
- Transcription termination factor 1, mitochondrial
- Dimethyladenosine transferase 2, mitochondrial
- Large ribosomal subunit protein bL12m
- U3 small nucleolar RNA-associated protein 6 homolog
- Cytokine receptor-like factor 3
- Twinkle mtDNA helicase
Sequence:
MSGSVLFTAGERWRCFLTPSRSSLYWALHNFCCRKKSTTPKKITPNVTFCDENAKEPENALDKLFSSEQQASILHVLNTASTKELEAFRLLRGRRSINIVEHRENFGPFQNLESLMNVPLFKYKSTVQVCNSILCPKTGREKRKSPENRFLRKLLKPDIERERLKAVNSIISIVFGTRRIAWAHLDRKLTVLDWQQSDRWSLMRGIYSSSVYLEEISSIISKMPKADFYVLEKTGLSIQNSSLFPILLHFHIMEAMLYALLNKTFAQDGQHQVLSMNRNAVGKHFELMIGDSRTSGKELVKQFLFDSILKADPRVFFPSDKIVHYRQMFLSTELQRVEELYDSLLQAIAFYELAVFDSQP
Protein: Zinc finger and SCAN domain-containing protein 18 (Zinc finger protein 447) (Q8TBC5)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- PiggyBac transposable element-derived protein 1
- Zinc finger protein 396
- Zinc finger and SCAN domain-containing protein 1
- Zinc finger and SCAN domain-containing protein 32
- Zinc finger and SCAN domain-containing protein 20
- SCAN domain-containing protein 1
- Zinc finger protein 174
Sequence:
MLPLEKAFASPRSSPAPPDLPTPGSAAGVQQEEPETIPERTPADLEFSRLRFREFVYQEAAGPHQTLARLHELCRQWLMPEARSKEQMLELLVLEQFLGILPDKVRPWVVAQYPESCKKAASLVEGLADVLEEPGMLLGSPAGSSSILSDGVYERHMDPLLLPGELASPSQALGAGEIPAPSETPWLSPDPLFLEQRRVREAKTEEDGPANTEQKLKSFPEDPQHLGEWGHLDPAEENLKSYRKLLLWGYQLSQPDAASRLDTEELRLVERDPQGSSLPEGGRRQESAGCACEEAAPAGVLPELPTEAPPGDALADPPSGTTEEEEEQPGKAPDPQDPQDAESDSATGSQRQSVIQQPAPDRGTAKLGTKRPHPEDGDGQSLEGVSSSGDSAGLEAGQGPGADEPGLSRGKPYACGECGEAFAWLSHLMEHHSSHGGRKRYACQGCWKTFHFSLALAEHQKTHEKEKSYALGGARGPQPSTREAQAGARAGGPPESVEGEAPPAPPEAQR
Protein: Transducin family protein / WD-40 repeat family protein (F4JHM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Vacuolar sorting protein 18
- Vacuolar protein-sorting-associated protein 11 homolog
- Protein VACUOLELESS1
- Vacuolar protein-sorting-associated protein 33 homolog
- Vacuolar sorting protein 39
- Vacuolar sorting protein 3
- Vacuolar protein sorting-associated protein 41 homolog
- Homeodomain-like superfamily protein
- Ras-related protein RABF2a
- At4g31270
Sequence:
MELDLDSFLVSDSDSDSDLDSSSVPHRTVDEILNASSSSSASSSPPSSPPSINRRKQDDPNRRLSEALTNVAVLRPESELHRGFPPTRRNSTSSSSLRQLPLPSLLAGVRSNVKPGAALAAAVAASRLVPTPHAAIIKSRRASSASSELLLQVSNQEEDDHEVLSSNGDSVGVAAGSVSADDFRSFGGESLLEDEDNGVSGVASLEDEAKVMEVQASDITESLNPDLVTVSSGFDSEGNVSTEKEAETTMEAGNAAIDDDTDETMLVASLVESSESQHLTDSEGKCDDAKVSNDEESSVGDVKSDKSDIIIPESKKEGGDAFIPDDGSSMSGISELVEERIAELENERMSKRERLKSQSFRKQLVLAEEFEKKQAYTGLHWEEGAAAQPMRLEGVKIGSTNLGYFDVDADNVISRTISSQAFKRDHGSPQVLAVHLNYIAVGTSKGVIVVVPSKYSSDHADQMESKMIWLGLQGERSQSPVTSVCFNQIGSLLLAGYGDGHVTVWDMQRASIAKVITEHTAPVVYAFFLGRDSQGSRQFKVITSDTKGVVFKHSFSYARLLNMYTVETQCLLDGQKNGTVLSASPLPDENFGSSLVSSKGGNSAVPSSSISSMMGGVVGVGSTWKLFNEDSTSVEEGVVIFATYQTGLVVKLIPNLEVYAQLPRPEGVREGSMPYTAWRRSTENYSKEAEDRVSFLVIAWDRRVQVAKLVKSDIKEYAKWSLDSPAIGVVWLDDQLLVIPTVTGHLYLFTRDGVVIHQTNFSVAGSSGNDLISYHTYFTNVFGNPEKAYHNSMGVRGASVYILGTAHLVISRLLPWKERVDVLRRGGDWMGAFNMAMSLFNGQAHGVVDLPKTVDAIREAIAPSLAELLLSYVDEVFSYISIAFSNQIENNGVTHEPSSGINNVNLEIEEQYNRVGGVAVEFCVHINRMDLLFDEIFSRFVAVQQRDTFLELLEPYILRDMLGSLPPEIMQALVEHYSRKGWLQRIEQCVLHMDISSLDFNQVVRICREHGLYGALLYLFNKGLDDFRSPLEELLIVLRNSEKQRATAIGYRMLVYLKYCFLGLAFPPGHGTLNPTRWPSLRSELIQFLLEKSNAHDSSTCVTSRLNYLNLYHLLEMDTEATLDVLRYAFVENEMVKHESHLLEYGEVSVESKTDGSLPEVSNDILIQNLVDALVHVPDWGVSNESGDPIDSKSDKNWPSKEDTSHLFEFVAYYAARGRVSISKSVLAQILDYLTSDHILPTYNVSSKMRENQLLNLLKAVPETDWDADYVSQLCEKAHFYQVCGYIHIIDRRYVAALDSYVKEADEPIHLFCYVNKMLSQLSGDEFTAFQSAIISRIPELLDLSRQGAFFLIICNLKDTIKRIQEQLHSHPRSLFLYLKTVIEVYLSGSLDFSRLRKHEAVDSSGENIRRDIPKEAKIYLEGLNDFPKFIQDNPVNVTDDMIELYVELLCKYEPKSVLKFLETFDSYRVEHCLRLCQEYGIVDAAAFLLERVGDAGSALSLTLSGLNEKYVELEIAVECLMSEMKLGASEGASLEHFSSALELKEVHDIQGVLQACIGLCQRNTPRLNPEESEILWFRFLDTFCEPLMESYREPKNTDGINKGSLGVKSLERHVNESDVAIKWRIPRSDTAATHILRKLISQFIKEIVEGMIGYVRLPTIMTKLLSDNGTQEFGDFKLTILGMLGTYGFERRILDTAKSLIEDDTFYSMNLLKKGASHGYAPRSLLCCICSCPLTKTFSALRVRVFNCGHATHLQCEPSENETSTSASSIHVSSSGCPVCMTKKTSKSSLKGKSFYRDYGLISTVSSNAGSSQRASPYSHENEMSDHSHNQQLSRFEILTNLQKDQRLVQIESLPRLRLAPPAVYHEKVSRLSGFTPGESSGKDTKPVKTGQGKKPKTKGSIFGSTFGKSFL
Protein: Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.3 (F4KB17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May participate in a complex which severs microtubules in an ATP-dependent manner (By similarity). Microtubule severing may promote rapid reorganization of cellular microtubule arrays (By similarity). Confers precision to microtubule (MT) severing by specific targeting of KTN1 to MT cleavage sites such as crossover or branching nucleation sites. Together with other KTN80s, regulates cell elongation by modulating MT organization.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28978669}. Note=Present in dynamic discrete particles specifically localized to microtubule (MT) crossovers and branching nucleation sites. {ECO:0000269|PubMed:28978669}.
Interaction partners:
- Uncharacterized protein
- Katanin p60 ATPase-containing subunit A1
- AT2G34560 protein
- Protein ORGAN SIZE RELATED 1
- Myb family transcription factor PHL11
- Protein PHYTOCHROME-DEPENDENT LATE-FLOWERING
- Transducin/WD40 repeat-like superfamily protein
- Transcription initiation factor TFIID subunit 13
- Actin-interacting protein 1-2
- THO complex subunit 6
Sequence:
MNTKRAYKLQEFVAHSAAVNCLKIGRKSSRVLVTGGEDHKVNLWAIGKPNAILSLYGHSSGIDSVTFDASEGLVAAGAASGTIKLWDLEEAKVVRTLTGHRSNCVSVNFHPFGEFFASGSLDTNLKIWDIRKKGCIHTYKGHTRGVNVLRFTPDGRWIVSGGEDNVVKVWDLTAGKLLHEFKSHEGKIQSLDFHPHEFLLATGSADKTVKFWDLETFELIGSGGTETTGVRCLTFNPDGKSVLCGLQESLKIFSWEPIRCHDGVDVGWSNLSDMNVHEGKLLGCSYNQNCVGVWVVDLSRTEPMSGGATQSNSHPEKTSGSGRDQAGLNDNSSKVILGKLPGSQKVDPLLKETKSLGKLSVSQNSDPLPKDTKSTGRSSVSQSSDPLVKEPKPLGRFSATHSSDTVKESRTLSSTGSVSDSPHRVTLTSAPKSASGISTVVPNAAASKRNFGKANPKANPPVVNKEDYFPVIVPRTEPIIEQASESRAELDIIGRTMPYSLQSKAADSRRLSSSRNEPDLPTSSLLERSQSQPIEPITLQDGNTYPSDEGGSWDTAERTNKESKCRVFGRFNSRSLVRSPPRNHDENSDLISYNANRDSSPTESRKGGRLHSLVLNRERRGRFSNFEGPVSSSSGGNMTAPNSRPSNMLKQRGNHVPVDQGITSASEEDIVADIMGQHDQFVSSMHSRLAKLQVVRRYWERNDIKNSISSIEKMADNAVIADVLLIVNERPEILTLDTCTSLLPLLTALLGSNMDSHLSVCLDLLLKLVRMYGSQIYSSLSAPSSVGVDIEAEQRMERYSCCFVEFEKIKACLPSLARRGNLVAKTLHELNLTFQEVSS
Protein: Guanine nucleotide-binding protein subunit alpha-13 (G alpha-13) (G-protein subunit alpha-13) (Q6Q7Y5)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF1/p115RhoGEF, ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG) (By similarity). GNA13-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1) (By similarity). Promotes tumor cell invasion and metastasis by activating RhoA/ROCK signaling pathway (By similarity). Inhibits CDH1-mediated cell adhesion in process independent from Rho activation (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:12176367}; Lipid-anchor {ECO:0000269|PubMed:12176367}. Melanosome {ECO:0000250|UniProtKB:Q14344}. Cytoplasm {ECO:0000250|UniProtKB:Q14344}. Nucleus {ECO:0000250|UniProtKB:Q14344}. Note=Cytoplasmic in adult somatic cells, but mainly nuclear in spermatids in the testes. Translocates from the cytoplasm to the nucleus during spermatogenesis, hence predominantly observed in the cytoplasm of round spermatids but localized in the nuclei of elongating or elongated spermatids and testicular spermatozoa. {ECO:0000250|UniProtKB:Q14344}.
Interaction partners:
- Rho guanine nucleotide exchange factor 11
- Rho guanine nucleotide exchange factor 1
- Sphingosine 1-phosphate receptor 2
- Rho guanine nucleotide exchange factor 12
- Sphingosine-1-phosphate receptor 3
- Estrogen receptor
- Guanine nucleotide-binding protein subunit alpha-12
- Transforming protein RhoA
- Lysophosphatidic acid receptor 1
- Proteinase-activated receptor 1
Sequence:
MADFLPSRSVLSVCFPGCVLTNGEAEQQRKSKEIDKCLSREKTYVKRLVKILLLGAGESGKSTFLKQMRIIHGQDFDQRAREEFRPTIYSNVIKGMRVLVDAREKLHIPWGDNKNQVHGDKLMAFDTRAPMAAQGMVETRVFLQYLPAIRALWDDSGIQNAYDRRREFQLGESVKYFLDNLDKLGVPDYIPSQQDILLARRPTKGIHEYDFEIKNVPFKMVDVGGQRSERKRWFECFDSVTSILFLVSSSEFDQVLMEDRLTNRLTESLNIFETIVNNRVFSNVSIILFLNKTDLLEEKVQVVSIKDYFLEFEGDPHCLRDVQKFLVECFRGKRRDQQQRPLYHHFTTAINTENIRLVFRDVKDTILHDNLKQLMLQ
Protein: ADP-ribosylation factor-binding protein GGA1 (Gamma-adaptin-related protein 1) (Golgi-localized, gamma ear-containing, ARF-binding protein 1) (Q9UJY5)
Organism: Homo sapiens (Human)
Function: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif. Mediates export of the GPCR receptor ADRA2B to the cell surface. Required for targeting PKD1:PKD2 complex from the trans-Golgi network to the cilium membrane (By similarity). Regulates retrograde transport of proteins such as phosphorylated form of BACE1 from endosomes to the trans-Golgi network.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15886016}; Peripheral membrane protein. Endosome membrane {ECO:0000269|PubMed:15886016}; Peripheral membrane protein. Early endosome membrane {ECO:0000269|PubMed:15886016}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Rab GTPase-binding effector protein 1
- ADP-ribosylation factor 1
- Cation-independent mannose-6-phosphate receptor
- Coiled-coil domain-containing protein 91
- ADP-ribosylation factor-binding protein GGA2
- Sortilin-related receptor
- ADP-ribosylation factor-binding protein GGA3
- Beta-secretase 1
- Cation-dependent mannose-6-phosphate receptor
- Sortilin
Sequence:
MEPAMEPETLEARINRATNPLNKELDWASINGFCEQLNEDFEGPPLATRLLAHKIQSPQEWEAIQALTVLETCMKSCGKRFHDEVGKFRFLNELIKVVSPKYLGSRTSEKVKNKILELLYSWTVGLPEEVKIAEAYQMLKKQGIVKSDPKLPDDTTFPLPPPRPKNVIFEDEEKSKMLARLLKSSHPEDLRAANKLIKEMVQEDQKRMEKISKRVNAIEEVNNNVKLLTEMVMSHSQGGAAAGSSEDLMKELYQRCERMRPTLFRLASDTEDNDEALAEILQANDNLTQVINLYKQLVRGEEVNGDATAGSIPGSTSALLDLSGLDLPPAGTTYPAMPTRPGEQASPEQPSASVSLLDDELMSLGLSDPTPPSGPSLDGTGWNSFQSSDATEPPAPALAQAPSMESRPPAQTSLPASSGLDDLDLLGKTLLQQSLPPESQQVRWEKQQPTPRLTLRDLQNKSSSCSSPSSSATSLLHTVSPEPPRPPQQPVPTELSLASITVPLESIKPSNILPVTVYDQHGFRILFHFARDPLPGRSDVLVVVVSMLSTAPQPIRNIVFQSAVPKVMKVKLQPPSGTELPAFNPIVHPSAITQVLLLANPQKEKVRLRYKLTFTMGDQTYNEMGDVDQFPPPETWGSL
Protein: Zinc finger and BTB domain-containing 16b (Zinc finger and BTB domain-containing protein 16-A) (E7FGS1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Si:ch73-206d17.1
Sequence:
MDLTKMGAIHLQNPSHPTTLLQKANQMRLSGTLCDVVIMVDSQEFHAHRTVLACASKMFEILFHRNSQHYTLDFLSPKTFQQILEYAYTATLQAKLEDLDDLLYAAEILEIEYLEEQCLKILETIQASEENDTDVNMNENGAEDVEDRRIKYLKSAFISKKHSIQDGGYGTAARHRLALVSMVDKRSSESAQLGLSTVSPTKAAVEGLMSMGQSVLQGNIGQSFSHNIGNSSPLIDKIKTEMMQVDEDYQHEGGFPRNGEGGGDSRQHRDTPGTPTRGSVITSARELHSTDSSVDSQGDNNQASLISMASLADRHFASLCSIPSNHKSESMLPVPVSMASSLHVPPSLAMSMDFSAYGGLFHQSLIQREFFSKLGDFAVNVKHEVHTQKERCEVCDMELPDNEAAEQHRKLHGGVKTFGCEFCGKQFLDSLRLRMHMLSHSAGPKALVCDQCGAQFSKEEALEAHRQTHTGSDMAVFCLLCGKRFQTQKALQQHMEIHAGMRSYICSECERTFPSHTALKRHLRSHTGDHPFECEFCGSCFRDESTLKGHKRIHTGEKPYECNGCGKKFSLKHQLETHYRVHTGEKPFECKLCHQRSRDYSAMIKHLRTHNGASPYQCTICQEYCPSLSSMQKHMKAHKPEDVPPDWRIEKTYLYLCYV
Protein: Nucleoporin NDC1 (Nuclear division cycle protein 1) (Nuclear pore protein NDC1) (P32500)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB), probably by playing a key role in de novo assembly and insertion of both structures in the nuclear envelope. In SPB duplication NDC1 is required for the insertion of the cytoplasmic side of the SPB in the nuclear envelope, thus allowing for the assembly of the nucleoplasmic SPB side. NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Multi-pass membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Central core structure of the nuclear pore complex. Spindle pole body, central plaque.
Interaction partners:
- Nucleoporin POM152
- Nucleoporin POM34
- Nucleoporin ASM4
- Nucleoporin NUP53
- Reticulon-like protein 1
- Nucleoporin NUP170
- Nucleoporin NUP188
- Nucleoporin NUP82
- Nucleoporin NUP159
- Nucleoporin NUP157
Sequence:
MIQTPRELLNPRYTYHTIFSDVCKTRFNHLVTRLFFICSIIQTVVISLLALPHSPLWELALAFIPNILALNLVSLLIIVTRKNYMHVKNFGFANSLTFILGQLLSVKFLVYQGVYSMGSILLSFVLGVVFGRGGSGWKPYYKLFIWLVVPTIYNLQHHVTDADKLSFNCENFFQAPQDYVLERVKRIMEKSVILSVISMFVLPIFTTVFFSRQKSGLFDSFTNGVLAVTNLLIISCIIFITFEFINIAFDAHMSIGCLHKGKLISNLSSTPMETLLSGLSADKPFTRLTAYQELAYRATSLDPSLRAPIYHSKFRSSSGNTWSLILNECLKTIQINNEKVVQYLRSVQDLGGSATARHKKKVENLDYMYENGKLTSANERLFGNRPSMMAPLRDNGLLDESPNRLRVRTDDSVLLNRGNKKRHRSSYYDNDLDETTQTFNGSIFTHETTFMTAMRLMLKKLKNSIMSFIFPSYAERQSSDESDNYRLLPNGSNKAQISIIDIWSISKKRQAEKLVPLPICHANSVVALTGLLIRSKTEDPKGGIIASVGDILKTLERSICALGEFADWDPESMAYTAFQTQRTAQDRVQQDSEDEDSMKDTTDMISVLYQLSTSAFMEIVLEYNVALNDVYLDADVAKLANWFLEVYASGNPNAT
Protein: Truncated MHC class I antigen splice variant Bl.2a (Q4VCP2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAQRTLFLLLAAALTMIETRAVFRPGLGEPRFISVGYVDNTQFVSFDSDAENPRSEPRAPWMEQEGPEYWERETQIAKDNEQSFGWSLRNLIHYYNQSKGDPPKAHVTHHPRPAGDVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWAAVVVPLGKEQNYTCHVYHEGLPEPLTLRWEPPPSTGSNMVNIAVLVVLGAVIIIEAMVAFVLKSSRKIAILPGPAGTKGSSAS