wanglab/gogpt-training-data huggingface dataset:
Protein: Cell wall protein RHD3 (LDG family protein 7) (Predicted GPI-anchored protein 29) (Repressed during hyphae development protein 3) (Q5A5U4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the cell wall involved in virulence. Does not seem to have a major role in maintaining cell wall integrity but plays a role in the relationship between C.albicans and the host.
Subcellular location: Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Chitinase 2
- Yeast-form wall Protein 1
Sequence:
MKFLAILSLSSSALATISSIQLFAKSDDSKVDGLGLYSKHEGAAIDYLFLGKNGADLKYDDEKKQIFQELKTSSITVRQSFTLGGDVYELGATDNFIPVTINKDGTLSFTGDDKVYASKNVNDPYRYSESEYAVSNKKTDDSAPITIVAKFSDDKAAETSGVAQAASSSAGPAQASVSNFEGAAGQNKLSYGVGMAAVVAGLVM
Protein: Isovaleryl-coA dehydrogenase, putative (EC 1.3.99.10) (Q387A0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Probable enoyl-CoA hydratase, mitochondrial
- methylcrotonoyl-CoA carboxylase
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- 3-methylcrotonyl-CoA carboxylase, putative
- Electron transfer flavoprotein subunit alpha
- Electron transfer flavoprotein subunit beta
- propanoyl-CoA C-acyltransferase
- Nonspecific lipid-transfer protein, putative
- Methylglutaconyl-CoA hydratase, mitochondrial, putative
Sequence:
MRSYRLASIRRHYTALVAPCGLRFFSPSTTVNLDYLLNPTPEHKMLRETVQRFAAERVETQAKQSDIDMHFNVDLLRELGDLGVLGVTIPEGDGGAGMDATAAVVIHHELSKVDPGFCLAYLAHSMLFVNNFYHASTAAQRERWLPKVLTGEHIGAMGMSEPGAGTDVLGMLTTATKESNGKYILNGGKTWVTNGTVADLVLVYAKVDGKITAFVVEKGASGFSVGKKIDKCGMRGSHMCQLFFDNVVLGEENLLGTEGKGLVAMMRNLEVERLTLAAMAVGIADRCVELMTCYANERKTFGKHIWNYGQIQRYIAETFAETEAAKSLTYAVSRSVAPGNCNRLGSDAVKLFAAPVAKRAADNAMQVMGGMGYARDMPVERLWRDAKLLEIGGGTLEAHHKNITKDLINSL
Protein: 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial (EC 1.3.1.124) (2,4-dienoyl-CoA reductase [NADPH]) (4-enoyl-CoA reductase [NADPH]) (Short chain dehydrogenase/reductase family 18C member 1) (Q16698)
Organism: Homo sapiens (Human)
Function: Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in mitochondria. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:7818482}.
Interaction partners:
- Oxidative stress-induced growth inhibitor 2
- Calbindin
- Securin
- Carbonic anhydrase 7
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Enoyl-CoA delta isomerase 1, mitochondrial
- [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
- Glyceraldehyde-3-phosphate dehydrogenase
- Peroxisomal multifunctional enzyme type 2
Sequence:
MKLPARVFFTLGSRLPCGLAPRRFFSYGTKILYQNTEALQSKFFSPLQKAMLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVLISGEFNDLRKVTKEQWDTIEELIRKTKGS
Protein: UV-B-induced protein At3g17800, chloroplastic (Q9LVJ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Pentatricopeptide repeat
- Electron transporter, putative
- Thioredoxin domain-containing protein
- AT3g29240/MXO21_9)
- ARM repeat superfamily protein
- At5g52960
- At1g63610
- At4g33110
- Uncharacterized protein At3g49140
- MAR-binding filament-like protein
Sequence:
MDALTSSLVRSPIVPSRTSDNGSGSMFLTASGPGFTRSGSSRLQLRLRQNASARSSRSLQSLTTTAKTRRSFVVRASSASNDASSGSSPKPIAPLQLQSPAGQFLSQILVSHPHLVPAAVEQQLEQLQTDRDSQGQNKDSASVPGTDIVLYRRIAELKENERRRTLEEILYALVVQKFMEANVSLVPSVSPSSDPSGRVDTWPTKVEKLERLHSPEMYEMIHNHLALILGSRMGDLNSVAQISKLRVGQVYAASVMYGYFLKRVDQRFQLEKTMKILPGGSDESKTSVEQAEGTATYQAAVSSHPEVGAFAGGVSAKGFGSEIKPSRLRSYVMSFDAETLQRYATIRSREAVGIIEKHTEALFGKPEIVITPEGTVDSSKDEQIKISFGGMKRLVLEAVTFGSFLWDVESHVDARYHFVLN
Protein: DCN1-like protein 5 (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5) (Q5RDF9)
Organism: Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs). May play a role in DNA damage response and may participate in cell proliferation and anchorage-independent cell growth.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BTE7}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BTE7}. Note=Subcellular localization is independent of the interaction with cullins. {ECO:0000250|UniProtKB:Q9BTE7}.
Interaction partners:
- NEDD8-conjugating enzyme UBC12
- Cullin-2
- Cullin-3
- UBE2F isoform 2
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
Sequence:
MPVKKKRKSPGVAAAVAEDGGLKKCKISSYCRSQPPARLISGEEHFSSKKCLAWFYEYAGPDEVVGPEGMEKFCEDIGVEPENIIMLVLAWKLEAESMGFFTKEEWLKGMTSLQCDCTEKLQNKFDFLRSQLNDISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTWPLFSVFYQYPEQSKYRVMNKDQWYNVLEFSRAVHADLSNYDEDGAWPVLLDEFVEWQKVRQTS
Protein: Dynein light chain roadblock (Q7ZUX8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR009998}.
Interaction partners:
- Dynein light chain Tctex-type 1
- Dynein light chain
- Si:dkey-148f10.4.
- Tctex1 domain-containing 2.
- Dynein light intermediate chain
- Dynein light chain Tctex-type 1
- Dynein light intermediate chain
- WD repeat domain 34
- Cytoplasmic dynein 2 intermediate chain 1 isoform X2
- Cytoplasmic dynein 2 light intermediate chain 1
Sequence:
MAEVEETIKRIQSQKGVQGIIIVNAEGIPIKSTLDNTSTVQYAANIHQLLMKARGIVRDIDPQNDLTFLRVRSKKNEIMIAPDKDYFLIVIQNPTE
Protein: 4-hydroxybenzoate polyprenyltransferase, mitochondrial (4-HB polyprenyltransferase) (EC 2.5.1.39) (Coenzyme Q biosynthesis protein 2) (Para-hydroxybenzoate--polyprenyltransferase) (PHB:PPT) (PHB:polyprenyltransferase) (Q9VHS7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03189}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03189}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03189}.
Interaction partners:
- Decaprenyl diphosphate synthase subunit 2, isoform A
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Coenzyme Q8
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS1
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Dihydroorotate dehydrogenase
- UbiA prenyltransferase domain-containing protein 1 homolog
Sequence:
MYALRHLRLQSARHFRSSYAAAATTKHMLPRQPARVLIGDWSTWDKSRLQDVCSRSSSTATEPVKQQTPLQELVSAAKPYAQLMRIDRPIGTYLLFWPCAWSIALSADAGCWPDLTMLGLFGTGALIMRGAGCTINDLWDKDIDAKVERTRLRPLASGQISQFDAIVFLSAQLSLGLLVLVQLNWQSILLGASSLGLVITYPLMKRVTYWPQLVLGMAFNWGALLGWCATQGSVNLAACLPLYLSGVCWTIVYDTIYAHQDKLDDLQIGVKSTALRFGENTKVWLSGFTAAMLTGLSAAGWACDQTVPYYAAVGVVGAHLVQQIYSLNIDNPSDCAKKFISNHQVGLILFLGIVLGTLLKSDESKKQRQSSLTTSTASSYVPALPQKPEVLS
Protein: ADP-ribosylation factor-like protein 4D (ADP-ribosylation factor-like protein 4L) (P49703)
Organism: Homo sapiens (Human)
Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in GDP-bound form.
Subcellular location: Nucleus, nucleolus {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:17398095}. Nucleus {ECO:0000269|PubMed:17398095}. Cytoplasm {ECO:0000269|PubMed:17398095}.
Interaction partners:
- Cytohesin-2
Sequence:
MGNHLTEMAPTASSFLPHFQALHVVVIGLDSAGKTSLLYRLKFKEFVQSVPTKGFNTEKIRVPLGGSRGITFQVWDVGGQEKLRPLWRSYTRRTDGLVFVVDAAEAERLEEAKVELHRISRASDNQGVPVLVLANKQDQPGALSAAEVEKRLAVRELAAATLTHVQGCSAVDGLGLQQGLERLYEMILKRKKAARGGKKRR
Protein: Checkpoint signal transducer rad24 (P42656)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts in cell cycle and stress checkpoint signaling by sequestering signal transducers regulated by the checkpoints. Required for the DNA damage checkpoint that ensures that DNA damage is repaired before mitosis is attempted. During environmental stress, sequesters srk1-phosphorylated cdc25 in the cytoplasm to delay the G2/M transition. Sequesters byr2 in the cytoplasm to prevent its translocation to the plasma membrane. Sequesters ran1/pat1-phosphorylated mei2 from its non-coding RNA activators (including meiRNA), to prevent meiotic induction in vegetative cells and to regulate meiosis I.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:12242289}.
Interaction partners:
- Checkpoint signal transducer rad25
- Cell division control protein 42 homolog
- Serine/threonine-protein kinase shk1/pak1
- M-phase inducer phosphatase
- Serine/threonine-protein kinase chk1
- Tyrosine-protein phosphatase CDC14 homolog
- Serine/threonine-protein kinase srk1
- Uncharacterized bHLH domain-containing protein C3F10.12c
- Negative regulator of sexual conjugation and meiosis
- Serine/threonine-protein kinase orb6
Sequence:
MSTTSREDAVYLAKLAEQAERYEGMVENMKSVASTDQELTVEERNLLSVAYKNVIGARRASWRIVSSIEQKEESKGNTAQVELIKEYRQKIEQELDTICQDILTVLEKHLIPNAASAESKVFYYKMKGDYYRYLAEFAVGEKRQHSADQSLEGYKAASEIATAELAPTHPIRLGLALNFSVFYYEILNSPDRACYLAKQAFDEAISELDSLSEESYKDSTLIMQLLRDNLTLWTSDAEYSAAAAGGNTEGAQENAPSNAPEGEAEPKADA
Protein: Actin, cytoplasmic 2 (EC 3.6.4.-) (Gamma-actin) [Cleaved into: Actin, cytoplasmic 2, N-terminally processed] (P63259)
Organism: Rattus norvegicus (Rat)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P63261}.
Interaction partners:
- Actin, cytoplasmic 1
- Actin-related protein 2/3 complex subunit 5-like protein
- Cofilin 2
- Alpha-actinin-1
- Alpha-actinin-4
- Cofilin-1
- Profilin-4
- Myosin-9
- Profilin-2
- Actin-related protein 2/3 complex subunit 3
Sequence:
MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Aryl hydrocarbon receptor nuclear translocator (Q1JPT1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTSANPDMSEVPSLAMTSSNGSHSNGVQKANKRQATSDYEDDEGGKLFRCDDDGGGSNDKERFARENHSEIERRRRNKMTAYITELSDMVPACSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGTYKPSFLTDQELKHLILEAADGFLFVVSCETGRVVYVSDSVTPVLNQAQSDWLGSSLYDQLHPDDVEKLREQLSTTENNNNSGRMLDMKTGTVKKEGGQATVRMSMGARRSFICRMRCGVCPVEPVSLNRLNFLRTRNRNGLGSAKDGEQQYVVVHCTGYIRSWPPAGMNLSEEEADNNQGNRFCLVAIGRLQVTCCPSDTSINNISVPVEFISRHNSQGVYTFVDHRCTATVGFQTQELLGKNILDFAHPEDQGLLRDSLQQVVKLRGQVMSVMFRFQSKSREWVWMRTSSFTFQNPFSEEIEYIICTNTNVK
Protein: ALK and LTK ligand 2b (Augmentor alpha-2) (AUG-alpha-2) (E7FAP8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cytokine that acts as a physiological ligand for receptor tyrosine kinases LTK and ALK. Required for neural crest cell differentiation and iridophore development during embryonic iridophore development and adult stripe development by acting as a receptor for LTK. Also required for iridophore formation in the adult eye.
Subcellular location: Secreted {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q6UX46}.
Interaction partners:
- ALK tyrosine kinase receptor
- Tyrosine-protein kinase receptor
- Small RNA 2'-O-methyltransferase
Sequence:
MCFALSLSIYKHTGTPPNKCRLNSALKRNRATVRLDIGQRGSLCPPFSMSAVRPPVFIGLLLLILTTGYCKPRDRDETSLLELLMDRVRQTQEHHSEGNTQHPPQIIEHSLETKDVNKVTKSYQHERILEVFPRDLRQKDKFLKHLTGPLYFSPKCSKLFYKLYNNTRDCTIPAYYKRCARLLTRLAGSQRCTEG
Protein: Histidine--tRNA ligase, chloroplastic/mitochondrial (EC 6.1.1.21) (Histidyl-tRNA synthetase) (HisRS) (Histidyl-tRNA synthetase 1) (AtHRS1) (O82413)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:9684861}. Mitochondrion {ECO:0000269|PubMed:9684861}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit alpha
- Isoleucine--tRNA ligase, chloroplastic/mitochondrial
- Lysine--tRNA ligase, chloroplastic/mitochondrial
- Tryptophan--tRNA ligase, chloroplastic/mitochondrial
- Valine--tRNA ligase, chloroplastic/mitochondrial 2
- Tryptophan--tRNA ligase, cytoplasmic
- Valine--tRNA ligase, mitochondrial 1
- Isoleucine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Cysteine--tRNA ligase 1, cytoplasmic
Sequence:
MRAIHIVTTRLSSSFRPILLLDLVSSCSPPRQFSIPRRLICAAANGGGRSGSIVAPLVTEEDFHKKIDVNPPKGTRDFPPEDMRLRNWLFNHFKEVSRLYGYEEVDYPVLETEALFIRKAGEEIRDQLYCFEDRGNRRVALRPELTPSLARLVIQKGKSVSLPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPQVTAEAELISSIVTFFKRIGITASDVGFKVSSRKVLQELLKKYGVPEDLFGRVCIIIDKIEKIPIDEIKKELGFTGISEDAIEQLLQVLSVKSLDDLEDIIGGAGEAIADLKQLFSLAEKFGYSEWIQFDASVVRGLAYYTGIVFEGFDRKGKLRAICGGGRYDRLLSTYGGDDFPACGFGFGDAVIVELLKEKDLLPELGQEVENIVCALDKDLQGAAATVATALRDKGQTVDLVLESKPLKWVFKRAARVNARRLVLVGKTEWEDGSVSVKVLSSGEQFQVKLSDLE
Protein: Probable prefoldin subunit 6 (O14450)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity).
Interaction partners:
- Probable prefoldin subunit 3
- Probable prefoldin subunit 1
- Probable prefoldin subunit 2
- Probable prefoldin subunit 4
- Probable prefoldin subunit 5
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit delta
- Microtubule-associated protein ssm4
- Probable T-complex protein 1 subunit beta
- Meiotic coiled-coil protein 2
Sequence:
MEELAKKYQNLQTELSTYVESLKKLETQLQENTTVLNELEKVAPDSNIYKQIGPTLVKQSHEEAKTNVKTRLDFINKEIARLENQTKISQEEFSKVKGAIIQAQAAAAPPNPAS
Protein: Ground-like domain-containing protein (Q21835)
Organism: Caenorhabditis elegans
Interaction partners:
- Neuropeptide-Like Protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- GRounDhog
- Ground-like domain-containing protein
Sequence:
MNLLIFLLCYFLGSPHYSEANKIKLKSSGRSADINHDSPCIWNKTQSWVHPYQSITVECCDEELSKLIHKTILDAGNNAKLGNLAKFIQRRSQLFYHMSFETIVSRENFAISTHYHGTHSCRVHDNNLYYLVYETPVQYDPFNMKTEDYLASIDSADPLGSTKPANLRGDFPDVREDSTAGEDLSVQPSIGNILQYPNKFAWPDPDEEVSKKIMLAEQDAIRSINELMESVTEISVMNSGAVVNSTDSLNITEIELPNPTPIPRNFANLREKDRLPENTHCDKERKDGNRCCDGRLASTMRDAMRQMATSPDFGQGKEGIIAAELQQKVQQRFQKSYEIIVSQSDFVISTYTAGDNFCKFDNKGFYILAYVSPKQYDIDEKEDEMKLAATSNKDPLGANTTMFENEAPWHVALKLDTYGDRAGYPVGSHCTQARTGSKCCSLILFNAMKSGYDSHVATSNFDPYDIRNISKAVQWSVEEILQHSAEVIVSLDDFAYATYNNNSYTCKYRVDKYHILAYTTPNHDLDNYDEMATSIIDSEPEAQIVYPAVDRTANQIPFQNTPSPYWTTPVPIPTQVYMPMQYTQQPMQPMYNQQPFFNQQPMFNQQPMYLQPAFNQAPLPYQYPAQPSQFNPFLASFRRFKRQIGRTPYPIHQNVYNDIGSAKPFNCPADLSGLSGMACCDGGLQFEANKVIDQAKQEPDFDKHNTRNLAKLMTRAVQKRFGTTFESVVAEADFSWGTNKFNGRTCKIDSQGYNALTYQSSSKPPPPSDFIDIPNDPTLGGPTGSSGGGGGGSNSNSGGGGGNGGGGNGGGGNGNGGGAGDGNGGAGAGNGNGAGAGNGNGAGAGNGNGAGAGNGNGAGAGNGNGAGAGDASAAAAAAQAQAAAAAQAQAAAAAAAQQAAAAAAAANAQQAAAAAAAAANPLSALVAATGACFSLDTWVTTPTGKKRMDQIDIGDYVLTADLEKTYFTPITLWIHREPEKVQEFLTIMTEYGKTLRITSRHFMYRNKCGKSYPQYIKMLPHDGEAIFASDLEVGDCVVVLYKGKYRQQKIETITRSVRTGIYSPLTNNGRIIVNDMLASCYSEIQQNTLQTTFFWAYDKLRSVLVEFFGDLYNNKIELPTGTTLSRDIISLIVPIQK
Protein: Interleukin-3 (IL-3) (Hematopoietic growth factor) (Mast cell growth factor) (MCGF) (Multipotential colony-stimulating factor) (P-cell-stimulating factor) (P08700)
Organism: Homo sapiens (Human)
Function: Cytokine secreted predominantly by activated T-lymphocytes as well as mast cells and osteoblastic cells that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells. Stimulates also mature basophils, eosinophils, and monocytes to become functionally activated. In addition, plays an important role in neural cell proliferation and survival. Participates as well in bone homeostasis and inhibits osteoclast differentiation by preventing NF-kappa-B nuclear translocation and activation. Mechanistically, exerts its biological effects through a receptor composed of IL3RA subunit and a signal transducing subunit IL3RB. Receptor stimulation results in the rapid activation of JAK2 kinase activity leading to STAT5-mediated transcriptional program (By similarity). Alternatively, contributes to cell survival under oxidative stress in non-hematopoietic systems by activating pathways mediated by PI3K/AKT and ERK.
Subcellular location: Secreted.
Interaction partners:
- Cytokine receptor common subunit beta
- Interleukin-5
- Interleukin-3 receptor subunit alpha
- Interleukin-6
- Granulocyte-macrophage colony-stimulating factor
- Interleukin-2
- Kit ligand
- Interleukin-1 alpha
- Interleukin-7
- Interleukin-5 receptor subunit alpha
Sequence:
MSRLPVLLLLQLLVRPGLQAPMTQTTPLKTSWVNCSNMIDEIITHLKQPPLPLLDFNNLNGEDQDILMENNLRRPNLEAFNRAVKSLQNASAIESILKNLLPCLPLATAAPTRHPIHIKDGDWNEFRRKLTFYLKTLENAQAQQTTLSLAIF
Protein: Exonuclease V, mitochondrial (Exo V) (EC 3.1.-.-) (Defects in morphology protein 1) (P38289)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Single strand DNA specific 5' exonuclease involved in mitochondrial DNA replication and recombination. Releases dinucleotides as main products of catalysis. Has the capacity to slide across 5'double-stranded DNA or 5'RNA sequences and resumes cutting two nucleotides downstream of the double-stranded-to-single-stranded junction or RNA-to-DNA junction, respectively.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MLGRALINKYGFLIHPRRFVHLNDKSLDGTFILPSKKNHMYDVPTNDPSGILNASDIDRINNLPFFDNTSPTKETNTKEGALLSEKLASVKELFGEDPENPSFINYRFPRGLENPYFDIQVNQLKKKRLSVTQLCTTQNWCELRNFYDFYSQNLSNQLLNLKFQVQKGKKIHKSLEDETHPELNQYKSFTHNFLALTKLSMDIDNDMDALLDNWFNSINRLVSLFTKGDGHAREIVCHGFINLEDGKLVEHLLNSDSKTKENVIISGVIDHLTLRNRHNHQVQKGAAHLDTEYQSWGNILTNLLSNLKELKSNNEIVISDIKTRSVPKIPSIESVIESSKLQTMYYKFFFSHLSQDMTQTYHSFLINAQRRGLDVDAPINPTKILTFILTNPLFANDVKNLLYGLPINHSAFDNDAKGSNTFDMTAFNDLLDRGPTSFNVPIEQDEDSSESTKCVSLRDYGHFYTKWKTPLTLKYFAARLSQIYFIVGNLVSNDLMIEYYYHNDNFHNIIFPYDPLKLGTHAHDSAMVWFGGRDMHPIEPTQKNFNTYCKFCDYRHVCSWKNKNELKLIDLGKELKKIILESSMK
Protein: AP-2 complex subunit sigma (Adaptin small chain) (Adaptor-related protein complex 2 subunit sigma) (Clathrin assembly protein 2 sigma small chain) (Sigma2-adaptin) (Q54H39)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity).
Subcellular location: Cell membrane. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. {ECO:0000250}.
Interaction partners:
- AP-2 complex subunit mu
- AP-2 complex subunit alpha-2
- AP-1 complex subunit beta
- AP-4 complex subunit beta
- AP-4 complex subunit epsilon
- AP-1 complex subunit gamma
- AP-3 complex subunit delta
- Clathrin heavy chain
- Epidermal growth factor receptor substrate 15 homolog
- SH3 and F-BAR domain-containing protein DDB_G0274695
Sequence:
MIHFILIQNRQGKTRLSKWYTPYEDVEKRKLSHEIHKIVNSRETKFTNFVEFRTHRIVYRRYAGLFFSVCVDPTDNELFCLEAIHLFVEVLDAYFGNVCELDLVFNFYKVYAIIDEVFLAGELMEPSKHVILQRMEFLDNLP
Protein: DNA polymerase (EC 2.7.7.7) (D6XGL4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU366014}.
Interaction partners:
- Protein artemis
- Mitochondrial DNA polymerase beta-PAK
- DNA primase
- Polynucleotide kinase 3'-phosphatase, putative
- DNA-directed DNA polymerase
- Flap endonuclease 1
- ATP-dependent DNA helicase PIF5
Sequence:
MLRRTFFRLSLDNRENIIRIFTEMADLNNALGEKYKVQSYNRAVRSLKTHLDLPLRTVEDLEKFPGIGSKLLKKAEEIIRTGKLDELEKKTKPKLKAIQELTQIHGFGPRAAATLFDREGIFTVEDLIEKADQIQLTEQQRVGVRYFHDINEKIPMHESILHENFLRECALRRLGSDYEIQICGSYRRRHPFSGDIDAILARSLNAPPLDAPVTTTGVLTILVEYLQEQRYLEATMALGPLKYMGMGRLPPRTTGGATKTYKARRVDIRLIETKSVPTALLTFTGSKNFNVIMRQAAISKGYLLNEYGLFKVGTSDEVRVLQERVRARKAAGLSKSQMKQEDPYSSSSVTEEGAEPFVSSISGNSAKMETLGMTKEELEAKRVHVTCEKDVFDVLGMPYAKPENRDP
Protein: Aminopeptidase (EC 3.4.11.-) (F1M9V7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Angiotensinogen
- Angiotensin-converting enzyme
- Neprilysin
- Cytosol aminopeptidase
- Sucrase-isomaltase, intestinal
- Angiotensin-converting enzyme
- Dipeptidyl peptidase 4
Sequence:
MWLAAAVPSLARRLLLLGSPPPPLLLLLSRSSSRRRRLHSLGLAAMPEKRPFERLPTEVSPINYSLCLKPDLLDFTFEGKLEAAAQVRQATNQIVMNCADIDIITASYAPEGDEEIHATGFNYQNEDEKVTLSFPSTLQTGTGTLKIDFVGELNDKMKGFYRSRYTTPAGEVRYAAVTQFEATDARRAFPCWDEPAIKATFDISLVVPKDRVALSNMNVIDRKPYPDDENLVEVKFARTPVMSTYLVAFVVGEYDFVETRSKDGVCVRVYTPVGKAEQGKFALEVAAKTLPFYKDYFNVPYPLPKIDLIAIADFAAGAMENWGLVTYRETALLIDPKNSCSSSRQWVALVVGHELAHQWFGNLVTMEWWTHLWLNEGFASWIEYLCVDHCFPEYDIWTQFVSADYTRAQELDALDNSHPIEVSVGHPSEVDEIFDAISYSKGASVIRMLHDYIGDKDFKKGMNMYLTKFQQKNAATEDLWESLESASGKPIAAVMNTWTKQMGFPLIYVEAEQVEDDRVLKLSQKKFCASGPYVGEDCPQWMVPITISTSEDPNQAKLKILMDKPEMSVVLKNVKPDQWVKLNLGTVGFYRTQYSSAMLESLLPGIRDLSLPPVDRLGLQNDLFSLARAGIISTVEVLKVMEAFVNEPNYTVWSDLSCNLGILSTLLSHTDFYEEIQEFVKDVFSPIGERLGWDPKPGEGHLDALLRGLVLGKLGKAGHKATLEEARRRFKEHVEGKQILSADLRSPVYLTVLKHGDGTTLDIMLKLHKQADMQEEKNRIERVLGATLSPELIQKVLTFALSEEVRPQDTVSVIGGVAGGSKHGRKAAWKFIKDNWEELYNRYQGGFLISRLIKLSVEGFAVDKMAGEVKAFFESHPAPSAERTIQQCCENILLNAAWLKRDADSIHQYLLQRKASPPSV
Protein: Tail tip protein L (Gene product 18) (gp18) (O64332)
Organism: Escherichia phage N15 (Bacteriophage N15)
Function: Part of the distal tail tip complex which plays a role in DNA injection during entry, and in tail assembly initiation during exit. The tail tip complex is assembled successively with three tail central fiber proteins J, one tail tip protein I, one tail tip protein L and one tail tip protein K. The tail tip complex interacts with tail measure protein to initiate tail tube assembly. The formation of the tail tip complex is completed by the addition of tail tip protein M, which is followed by tail tube polymerization.
Subcellular location: Virion {ECO:0000250|UniProtKB:P03738}. Host cytoplasm {ECO:0000250|UniProtKB:P03738}.
Interaction partners:
Sequence:
MSLNADYQKLEPGNEVRLFSVDGTAFGMSDVLRFHAHNIAHTPEEIEAAGGDENKLPAKSIWWQGEEYKAWPCQVEGIEATTDGTSPQPKLTVANLDSSISALCLAYDDLLQAKVTIHDTLAKYLDARNFPQGNPTADPSQEKLKVFYIDARNTETDEVVEFILSSPMDLQGRMIPTRQLHSLCSWCIRNKYRTGDGCDYAGTRYFDKHNNPVDDPSLDECNGTLTACKLRHGDSNELPFGGFPGTSLIRS
Protein: Geranyltranstransferase (EC 2.5.1.10) (A6Q6L6)
Organism: Sulfurovum sp. (strain NBC37-1)
Interaction partners:
- Isoprenyl transferase
- Geranylgeranyl hydrogenase
- Polyprenyl synthetase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- Transketolase
- Ribonuclease J
Sequence:
MQRFETYLSENLPEVTSFHPVYEEALGAMLQAGGKRFRPMLLLSIVDTYEPMLYDSALPVALALEMFHTYSLIHDDLPAMDDADLRRGHQTLHKRFDEVTAILAGDALNSDAFYLIAKAPLREDVKIKLVELLARDGGSRGMVLGQAIDCYFENRPLTIDEVKVLHTNKTAKLIAVSLQMGAVIVRLAPDVQKALYDFGIDLGLLFQIQDDIIDETQTEEEAGKTTGNDADKNSFVNLLGLENTVVQADTLAKDLQRRFEDFDEKLQMALQPLMNKYLYRHNKG