wanglab/gogpt-training-data huggingface dataset:
Protein: PFTAIRE-interacting factor 1A, isoform H (PFTAIRE-interacting factor 1A, isoform J) (A0A0B4JDD0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI03639p
- Cortactin, isoform A
- Proteasome inhibitor PI31 subunit
- Eukaryotic translation initiation factor 3 subunit M
- Tropomyosin-1, isoforms 9A/A/B
- LIM and SH3 domain protein Lasp
- Myosin heavy chain 95F
- Yuri gagarin, isoform B
- Calmodulin-related protein 97A
- Dynamin
Sequence:
MAENQTKTTSSKGCNTMSRTAHILAPHNGTVVRRTDPGSKLKESFHTEKHDIEDWQTMAKNKLKRKKKLSSSLTSVGDTVNQEKRTRIEGIQLHCRGKLRPKETQSFEAEKGPSAGSQKQLGKAEKDRERPVIIGGVTTTNVIAAPPQRIKRKLQENMDTIQKLNALTEQLRLEVNELKSSLITERGAVRALRAQNDADSRRWKSEVKKLQHTLEMAKKSNGIKKAIESGPESSGAHVTADGLINYEIQRLTNEIAVLKEANRNKEEKTQIMGQADRLKAADMRQLKNAYENRLTHIQKSAKIEITRLLEEIKTKERNIGQLRKDLLALQSPKKLKQNEAKVPATTKPKTNPNETSQKPKKPTTKAAGETKAKTEPDTDTDISEQNPIRQAQVTPEITQLKNIELINNTKNAHKSALEMRTTMKSSQPNGLDDAPTRMRAPDEMRATTWMTTLVGSNCHSHSHSHPAVAKSKDPNSDTDSALSSAPPSISPQPPSSGSDSGVIWQTLQDLDKLQKEAEMYQKENERLQTEVQLMKQELDAAEKAAISRAKKQAQIGELMQRIKELEEMQSSLEDEASELREQNELLEFRILELEDDSDKMESTCEGHCQSLQDLLEQSAQRLEDRDKRCLQQLLQCVQQLDLDTMMPGDQNRTETPKRHNSTHSHSHSHSHSQSHNHRIVATVQPYSNCATPTAPPTPSKRHCNQVSSWQSSSLSESGVFVECDLLSNPNPIGHPHLQFYQERLEQLEGKLLIYESSGETQARHLAQRLQRELQLEKDLKELADRVELLIEQNAQLEEAKCEFEEAENDTRLHLQRNEVELEILRQRNVELEFGKEALGAKYQDCRAEVLILREDLAAAETQLEHLQAERKQARKELQDLRRSLPLLLIFRLLSLAKMGNEESSPGGSPRLSSGYTSSIHQDRDFSAKIQTTEFDLGQAGFTDSGEEREIVYLKEEVKSLRSQLKELNARHYEAMETADSHWVDLEQQYKEREEAQQAKEASLKQKIAQLQDCLREDSRAATEKIQQLEEGELSLKSCLVRMTKEHRDLLTENRTLQCSLESLMAKMEKEAEHKMPLTEALENERRKTQALMDDLIFAKKVQQNTEDQLRQETDALRTQIFNIKKDYLHIEVTNGELKEEVGTLENKIRQMENQMRDSEERARCLEDELRTKDEQCQLLERKLGVMPEGYSLADELHDSPAKRAKKDEVPSLQAASQGLGVALLDLEGRDFGLPLHKDFQAIACSVKQLADTLLSQSPSENARL
Protein: F-box protein HRT3 (High level expression reduces Ty3 transposition protein 3) (Q12347)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity).
Interaction partners:
- Suppressor of kinetochore protein 1
- Cell division control protein 53
- F-box protein YLR352W
- F-box protein YDR306C
- F-box protein UCC1
- Non-SCF-type F-box protein ROY1
Sequence:
MIVDYEKDPRAKEAIAIWEKGVLKEKDGSMSDAINFYRSALKIHDNVESLYRKKILDEWMLHKKLSGLSMTTDAPDEQNETGKDDLSVEENAELQPCWILEILPDDILLRIIKKVILMSGESWVNLSMTCSTFSKLCFHDSVPFKTFAKYIYSKQIYDKMAMDLNGITDINTFEKEIWRGDDYRMLRERPYIKFEGVYISVVNYVRYGSNAESSLSLLKPVHMITYYRYFRFYENGQCLRLLSTDEPSAVVKHFSKENKPRHSHMCYWSLGFDYDFGHLKITRSDEKYTFIEEFQIKNQGNKRYQRLKWLSSIVVDKEGNASNCSLRNEKSFFFSRVKSFKDPG
Protein: Protein SDA1 (E7EW05)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|RuleBase:RU365057}.
Interaction partners:
Sequence:
MSNRNNNKLPSNLPQLQNLIKRDPPAYIEEFLQQYNHYKSNVEIFKLQPNKPSKELAELVMFMAQISHCYPEYLSNFPQEVKDLLSCNHTVLDPDLRMTLYTHIVTDIKNINAKHKNNKVNVVLQNFMYTMLRDSNATAAKMSLDVMIELYRRNIWNDAKTVNVITTACFSKVTKILVAALTFFLGKDEDEKQDSDSESEDDGPTARDLLVQYATGKKSSKNKKKLEKAMKVLKKQKKKKKPEVFNFSAIHLIHDPQDFAEKLLKQLECCKERFEVKMMLMNLISRLVGIHELFLFNFYPFLQRFLQPHQREVTKILLFAAQASHHLVPPEIIQSLLMTVANNFVTDKNSGEVMTVGINAIKEITARCPLAMTEELLQDLAQYKTHKDKNVMMSARTLIHLFRTLNPQMLQKKFRGKPTEASIEARVQEYGELDAKDYIPGAEVLEVEKEENAENDEDGWESTSLSEEEDADGEWIDVQHSSDEEQQEISKKLNSMPMEERKAKAAAISTSRVLTQEDFQKIRMAQMRKELDAAPGKSQKRKYIEIDSDEEPRGELLSLRDIERLHKKPKSDKETRLATAMAGKTDRKEFVRKKTKTNPFSSSTNKEKKKQKNFMMMRYSQNVRSKNKRSFREKQLALRDALLKKRKRMK
Protein: U3 small nucleolar RNA-associated protein 25 homolog (Digestive organ expansion factor homolog) (UTP25 small subunit processor component) (Q68CQ4)
Organism: Homo sapiens (Human)
Function: Component of the ribosomal small subunit processome for the biogenesis of ribosomes, functions in pre-ribosomal RNA (pre-rRNA) processing (By similarity). Essential for embryonic development in part through the regulation of p53 pathway. Controls the expansion growth of digestive organs and liver. Also involved in the sympathetic neuronal development (By similarity). Mediates, with CAPN3, the proteasome-independent degradation of p53/TP53.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:22002106, ECO:0000269|PubMed:27657329}.
Interaction partners:
- Something about silencing protein 10
- U3 small nucleolar ribonucleoprotein protein MPP10
- WD repeat-containing protein 36
- Nucleolar protein 6
- Ribosomal RNA processing protein 36 homolog
- Neuroguidin
- Activator of basal transcription 1
- U3 small nucleolar ribonucleoprotein protein IMP4
- Nucleolar protein 14
- Protein RRP5 homolog
Sequence:
MGKRGSRSQSQLLNTLTKKQKKHLRDFGEEHPFYDRVSRKEAKPQICQLSESSDSSDSESDSESEPQQVSGYHRLLATLKNVSEEEEEDEEEEEEEDSIVDDAEMNDEDGGSDVSVEEEMAAESTESPENVALSADPEGKEDGEEPPGTSQTSPEEFTDAKHESLFSLETNFLEEESGDNSSLKASQDPFLQHVNKELKEKAIQAVATNPKTTHELKWPILGQLFFSSKFQKLETFKPPKDIDLKSLHLQKPLESTWTKTNSQFLSGPQKSSSPFTPLQKELFLIMNSYRDLFYPERTALKNGEEIRHVYCLHVINHILKANAQVLGNNSRRRSQKFGVGDDDDFRDQGLTRPKVLIVVPFREAALRVVQLFISLLEGDSKKKIIVSNKKRFQGEYGSDPEERPPNLKRPEDYEAVFVGNIDDHFRIGVAILQRSIRLYAPFYSSDILIASPLGLRTIIGGEGEKKRDFDFLSSIELLIIDQADIYLMQNWEHVLHLMNHMNLLPLDSHGVDFSRVRMWSLNNWSKYYRQTLLFGALQDAQINSVFNKYCVNMQGQVAVRNVPMTGSISHVLVQLPHVFQRMEAENLASVIDARFNFFVNKILPQYRDAVMSHTLIYIPSYFDFVRLRNYFKKEELNFTHICEYTQKSGVSRARHFFLQGEKQFLLFTERFHFYKRYTIKGIRNLIFYELPTYPHFYSEICNMLRATNRGEEATWTCTVLYSKYDAQRLAAVVGVERAAQMLQSNKNVHLFITGEK
Protein: Bacteriocin weissellin-A (B3A0N4)
Organism: Weissella paramesenteroides (Leuconostoc paramesenteroides)
Function: Highly active against Gram-positive bacteria M.flavus strain ATCC 400, M.luteus strain CECT241, C.soprogenes strain NCTC533, L.monocytogenes strain ATCC 19111, L.inocua strain ATCC BAA-680D and S.carnosus strain LMG13564. Less active against B.cereus strain LMG13569, C.thiaminolyticum strain ATCC 15579, E.faecalis strain NCTC8176, L.lactis strain LM0230, L.casei strain ATCC 344, L.lactis strain IL1403, L.jensenii strain ATCC 25258, L.plantarum strain CECT220, L.brevis strain ATCC 8287, L.bulgaricus strain LMG13551, P.acidilactici strain ATCC 25740, P.pentosaceus strain ATCC 33316 and P.pentosaceus strain LMG13560. Weakly active against L.mesenteroides strain ATCC 19254, L.lactis strain ATCC 1454, L.sakei strain CECT906T, L.lactis subsp. cremoris strain MC1363 and L.curvatus strain ATCC 51436. Not active against Gram-negative bacterium S.enteritidis strain ATCC 13076. The mode of action appears to be non-lytic. Inactivated by proteinase K, but insensitive to trypsin, alpha-chymotrypsin, pepsin and papain.
Subcellular location: Secreted {ECO:0000269|PubMed:21511463}. Note=Partly adsorbed to cell wall. {ECO:0000269|PubMed:21511463}.
Interaction partners:
Sequence:
KNYGNGVYCNKHKCSVDWATFSANIANNSVAMAGLTGGNAGNK
Protein: Uncharacterized protein YBL039W-B (P0C268)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized membrane protein YIL089W
- Outer mitochondrial transmembrane helix translocase
- Sorting assembly machinery 35 kDa subunit
- Uncharacterized protein YKL065W-A
- Uncharacterized protein YGR168C
- Unfolded protein response-inducible protein 1
- 2-hydroxyacyl-CoA lyase
Sequence:
MGFFNNNPVIEFFHRITRKPSTIAMWVFAGLICSSTFYLMFMSSPTIDFNSKSKKKNDK
Protein: Mediator of RNA polymerase II transcription subunit 15 (Mediator complex subunit 15) (G3V1P5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364148}.
Interaction partners:
Sequence:
MRKAGVAHSKSSKDMESHVFLKAKTRDEYLSLVARLIIHFRDIHNKKSQASVSDPMNALQSLTGGPAAGAAGIGMPPRGPGQSLGGMGSLGAMGQPMSLSGQPPPGTSGMAPHSMAVVSTATPQTQLQLQQVALQQQQQQQQFQQQQQAALQQQQQQQQQQQFQAQQSAMQQQFQAVVQQQQQLQQQQQQQQHLIKLHHQNQQQIQQQQQQLQRIAQLQLQQQQQQQQQQQQQQQQALQAQPPIQQPPMQQPQPPPSQALPQQLQQMHHTQHHQPPPQPQQPPVAQNQPSQLPPQSQTQPLVSQAQALPGQMLYTQPPLKFVRAPMVVQQPPVQPQVQQQQTAVQTAQAAQMVAPGVQVSQSSLPMLSSPSPGQQVQTPQSMPPPPQPSPQPGQPSSQPNSNVSSGPAPSPSSFLPSPSPQPSQSPVTARTPQNFSVPSPGPLNTPVNPSSVMSPAGSSQAEEQQYLDKLKQLSKYIEPLRRMINKIDKNEDRKKDLSKMKSLLDILTDPSKRCPLKTLQKCEIALEKLKNDMAVPTPPPPPVPPTKQQYLCQPLLDAVLANIRSPVFNHSLYRTFVPAMTAIHGPPITAPVVCTRKRRLEDDERQSIPSVLQGEVARLDPKFLVNLDPSHCSNNGTVHLICKLDDKDLPSVPPLELSVPADYPAQSPLWIDRQWQYDANPFLQSVHRCMTSRLLQLPDKHSVTALLNTWAQSVHQACLSAA
Protein: Probable S-adenosylmethionine synthase 1 (AdoMet synthase 1) (EC 2.5.1.6) (Methionine adenosyltransferase 1) (MAT 1) (O17680)
Organism: Caenorhabditis elegans
Function: Catalyzes the formation of S-adenosylmethionine (SAM) from methionine and ATP (By similarity). The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate (By similarity). May be required for the majority of global SAM production under normal growth conditions.
Interaction partners:
- Probable methionine synthase
- Tyrosine aminotransferase
- Hcy-binding domain-containing protein
- S-adenosylmethionine decarboxylase proenzyme
- Adenosylhomocysteinase
- Probable methylenetetrahydrofolate reductase
- Methyltransf_11 domain-containing protein.
- PABS domain-containing protein
- Putative choline-phosphate cytidylyltransferase
- Phosphoethanolamine N-methyltransferase 2
Sequence:
MSSKFLFTSESVSEGHPDKMCDQISDAVLDAHLKQDPNAKVACETVTKTGMVMLCGEITSKAVVDYQVLVRRVIEKIGFTDSSIGFDHKTCNVLVALEQQSPEIAAGVHVNKDGEDVGAGDQGIMFGYATDETEETMPLTLILSHKINAELHKLRRNGTLPWVRPDSKSQVTIEYESRHGATIPLRVHTVVVSTQHSPDVTLEKLRETILADVIKKVIPASLLDESTVFHINPCGTFIVGGPMGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDPTKVDRSAAYAARWVATSLVKAGLAKRVLVQLSYAIGIAKPISVLVYAFGTSPLTDEELHQIVEDSFDLTPGKIIKELDLKRPIYEKTAENGHFGHSEFPWEQPKALKISPALLEKAKGNPIPATSAIAH
Protein: Ubiquitin-fold modifier 1 (Q5BJP3)
Organism: Rattus norvegicus (Rat)
Function: Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to lysine residues of substrate proteins as a monomer or a lysine-linked polymer. The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress. Ufmylation of TRIP4 regulates nuclear receptors-mediated transcription.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P61960}. Cytoplasm {ECO:0000250|UniProtKB:P61960}.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme 5
- Ubiquitin-fold modifier-conjugating enzyme 1
- Ufm1-specific protease 2
- UFM1-specific peptidase 1.
- E3 UFM1-protein ligase 1
- Ubiquitin-like protein NEDD8
- DDRGK domain-containing protein 1
- Ubiquitin-related modifier 1
- NEDD8-activating enzyme E1 catalytic subunit
Sequence:
MSKVSFKITLTSDPRLPYKVLSVPESTPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRLIPRDRVGSC
Protein: Alanine--tRNA ligase, cytoplasmic (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Protein lactyltransferase AARS1) (EC 6.-.-.-) (Protein sticky) (Sti) (Q8BGQ7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03133}. Note=Translocates to the nucleus in response to increased levels of lactate; nuclear translocation is dependent on KPNA4. {ECO:0000255|HAMAP-Rule:MF_03133}.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Glycine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Threonine--tRNA ligase 1, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Asparagine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase
- Isoleucine--tRNA ligase, mitochondrial
Sequence:
MDATLTAREIRERFINFFRRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTIDPSHPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALELLTQEFGIPVERLYVTYFGGDEAAGLEPDLECRQIWQNLGLDEARILPGNMKDNFWEMGDTGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNRESDGVLKPLPKKSIDTGMGLERLVSVLQNKMSNYDTDLFMPYFEAIQKGTGARPYTGKVGAEDADGIDMAYRVLADHARTITVALADGGRPDNTGRGYVLRRILRRAVRYSHEKLNASRGFFATLVDVVVQSLGDAFPELKKDPEMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDCKTIPGDTAWLLYDTYGFPVDLTGLIAEEKGLVVDMNGFEEERRLAQLKSQGKGAGDEDLIMLDIYAIEELRAKGLEATDDSPKYNYQSDSSGSYVFECTVATVLALRREKMFVDEVVTGQECGVVLDKTCFYAEQGGQIYDEGYLVKVDDSSEDKTEFTVKNAQVRGGYVLHIGTIYGNLKVGDQVRLFIDEPRRRPVMSNHTATHILNFALRSVLGEADQKGSLVAPDRLRFDFTAKGAMSTQQIKKAEEIVNGMIEAAKPVYTQDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPCGPAGSLTSVEFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKSETLKKSLSAMEAKVKAQTAPNKDVQREIADLGEALATAVIPQWQKDEQRETLKSLKKVMDDLDRASKADVQKRVLEKTKQLIDSNPNQPLVILEMESGASAKALNEALKLFKTHSPQTSAMLFTVDNEAGKITCLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDMSAQATGKNVGCLQEALQLATSFAQLRLGDVKN
Protein: Cell division cycle protein 16 homolog (Abnormal embryogenesis protein 27) (Anaphase-promoting complex subunit 6) (APC6) (G5EG38)
Organism: Caenorhabditis elegans
Function: Probable component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (By similarity). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins (By similarity). Developmental role in early embryogenesis and the metaphase to anaphase transition in oocyte and spermatocyte meiosis and mitosis in germ cells. Required for embryonic anterior-posterior axis formation. Plays a role in regulating the abundance of glr-1 receptors in postmitotic neurons, which may in turn control animal locomotion. Involved in regulating GABA neurotransmitter release at neuromuscular junctions in GABA motor neurons.
Subcellular location: Cell junction {ECO:0000269|PubMed:24321454}. Synapse {ECO:0000269|PubMed:24321454}.
Interaction partners:
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit 11
- Cell division cycle protein 23 homolog
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 2
- Abnormal embryogenesis protein 30
- Anaphase-promoting complex subunit 1
- WD repeat-containing protein fzy-1
- Protein gfi-3
- Anaphase-promoting complex subunit 1
Sequence:
MSAISPDTKSFAIPTLADEGSSSKPASSLDLPKHESIRFKPIKTLASRIDGSEYYDEASMEKVMEMLEIGRTDEAVAYADTLYSNIIDDEQQDIVTIAEYVKILVVLRQWRRISHIIARGNYHQIHIVFAYYAATALFQRKLYEDVAELSVGHLLPSNGQIGPLPVRTLSQVTGRYVEEERMKYSFANMAELDNSSKKLRMVPALMITIAESFLKLMNRDAAMICINYALSLDNTTLHVERLMAKYNLVEPAMWEKYRKVRNEQLKLHEGNHDPRILMERAQRAYEMGRFRETKKITDELFDLFGPHPECIILRIHCLTMLKDSRSLLELGHQLVSDDPHIPLPWYCVAMYYYSIGANSRARNFISKCTMMDSTFAEGWVAFGHILHYEVEHEQSMSCYYRASKLVDKSSEPFLYTSLQYSTHSQKLSKKFMGEAVARAPNDPLIRHEEACVAYTAKSYAEADILFRTVLYMVTETDEIIPIEEVLKKKIDDFWHPMLNNIGHIARRQGRLNEAIMFYQKAIRMEPKFVDAIASTALCYAVLGNIDKATEFFNKALAIDPFNETIRQCLSKMIQASKESYSVDQQTLPPAYNSETYFGAQEILPYCAIRKPRNDGFVVPSIVSSSQPFMSMLRDRLRRQDQLYAQEPDNDAGNQV
Protein: Perilipin (A0A140VJN8)
Organism: Homo sapiens (Human)
Subcellular location: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
Interaction partners:
Sequence:
MSADGAEADGSTQVTVEEPVQQPSVVDRVASMPLISSTCDMVSAAYASTKESYPHIKTVCDAAEKGVRTLTAAAVSGAQPILSKLEPQIASASEYAHRGLDKLEENLPILQQPTEKVLADTKELVSSKVSGAQEMVSSAKDTVATQLSEAVDATRGAVQSGVDKTKSVVTGGVQSVMGSRLGQMVLSGVDTVLGKSEEWADNHLPLTDAELARIATSLDGFDVASVQQQRQEQSYFVRLGSLSERLRQHAYEHSLGKLRATKQRAQEALLQLSQVLSLMETVKQGVDQKLVEGQEKLHQMWLSWNQKQLQGPEKEPPKPEVESRALTMFRDIAQQLQATCTSLGSSIQGLPTNVKDQVQQARRQVEDLQATFSSIHSFQDLSSSILAQSRERVASAREALDHMVEYVAQNTPVTWLVGPFAPGITEKAPEEKK
Protein: Monothiol glutaredoxin-S14, chloroplastic (AtGRXcp) (AtGrxS14) (CAX-interacting protein 1) (CXIP1) (Q84Y95)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May only reduce GSH-thiol disulfides, but not protein disulfides (Potential). Probably involved in the regulation of the redox state of the BOLA proteins (Potential). May act as Fe-S cluster donors to Fe-S cluster-requiring proteins. May protect cells against protein oxidative damage. May regulate CAX cation transporters. The GRXS14-BOLA1 heterodimer binds a labile, oxygen sensitive Fe-S cluster.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16829529}.
Interaction partners:
- Protein BOLA2
- Protein BOLA1
- SufE-like protein 1, chloroplastic/mitochondrial
- Protein BOLA4, chloroplastic/mitochondrial
- Iron-sulfur assembly protein IscA, chloroplastic
- Glutaredoxin-C1
- NifU-like protein 3, chloroplastic
- NifU-like protein 5, mitochondrial
- NifU-like protein 4, mitochondrial
- NifU-like protein 2, chloroplastic
Sequence:
MALRSVKTPTLITSVAVVSSSVTNKPHSIRFSLKPTSALVVHNHQLSFYGSNLKLKPTKFRCSASALTPQLKDTLEKLVNSEKVVLFMKGTRDFPMCGFSNTVVQILKNLNVPFEDVNILENEMLRQGLKEYSNWPTFPQLYIGGEFFGGCDITLEAFKTGELQEEVEKAMCS
Protein: Septin homolog spn6 (Q09883)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Septin-like protein involved in the correct orientation of forespore membrane extension during sporulation.
Subcellular location: Cytoplasm. Forespore membrane; Peripheral membrane protein. Note=The sporulation-specific septin complex associates to the forespore membrane and forms partial or complete ring-like structures that curl around each haploid nucleus.
Interaction partners:
- Septin homolog spn5
- Septin homolog spn2
- Septin homolog spn7
- Septin homolog spn3
- Septin homolog spn1
- Septin homolog spn4
- Chromosomal passenger complex protein bir1
Sequence:
MSLTENLQLLLNLDSLPSKRENLIKRKECGLTIMLCGASGTGKTTFFNTLFATSLQPEKSYETAKETIAKKTLEVKKNKAVIEEDGFHINLTVLDTPGFGDFIDNTSCWNTVAEYLDEQHERYLIHDQNSLRVPRKDTRVHVCLYFITPVSFGMLPLDVLAMKELSTHVNLVPVIAKADTFTTPELTQIKQKIRRILEAQSIDVFHPSTEYSDYETAELLDSSLPYAIISSVNEVCKDDGEKSQGRRYPWGTSEIYEETHCDFLKLKKLLINRHMLELINTTETNIYERYRREQLTNRKSGIPKLKKEHYERLNNEKRAIQQKITQMTNETESFFQAKEEKMIETRDALNSELSEYHERIRALETQIESLKSYKGRGHKK
Protein: Cytoplasmic dynein intermediate light chain DYN3 (Dynein protein 3) (Q04949)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cytoplasmic dynein which acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15642746}. Note=Concentrates at motile dots in the cytoplasm corresponding to the plus ends of cytoplasmic microtubules.
Interaction partners:
- WD repeat-containing protein PAC11
- Dynein heavy chain, cytoplasmic
- Dynein light chain 1
- Protein NIP100
- Nuclear migration protein NUM1
- Protein LDB18
- Nuclear migration protein JNM1
- Nuclear distribution protein nudE homolog 1
- Nuclear distribution protein PAC1
- Karyogamy protein KAR9
Sequence:
MDNCNAWDKLLSQNESTINSTETATITAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYICEDHTEEKREEAQRLKYQELLKHFCEDRDMKDHIEMVKRSEILIPKGCDSIGLIKTVDERFEPTEVKEQHFLARYMDFIPTIDKIREDRKTTSGIDLDKLYPLEVFKVNIQEELGKMFAKYRENSRI
Protein: Dynamin-2A (EC 3.6.5.5) (Dynamin-like protein 6) (Dynamin-related protein 2A) (Q9SE83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Microtubule-associated force-producing protein involved in clathrin-mediated vesicle trafficking from the trans-Golgi network to the central vacuole. Able to bind and hydrolyze GTP. Binds specifically to phosphatidylinositol 3-phosphate (PtdIns3P).
Subcellular location: Cytoplasm, cytosol. Golgi apparatus membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton, phragmoplast. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:12207647}. Note=Localized in the forming cell plate during cytokinesis.
Interaction partners:
- Dynamin-2B
- Dynamin
- SH3 domain-containing protein 3
- Clathrin heavy chain 2
- SH3 domain-containing protein 1
Sequence:
MEAIDELSQLSDSMKQAASLLADEDPDETSSSKRPATFLNVVALGNVGAGKSAVLNSLIGHPVLPTGENGATRAPIIIELSRESSLSSKAIILQIDNKSQQVSASALRHSLQDRLSKGASGKNRDEINLKLRTSTAPPLKLVDLPGLDQRIVDESMIAEYAQHNDAILLVIVPASQASEISSSRALKIAKEYDPESTRTIGIIGKIDQAAENSKALAAVQALLSNQGPPKTTDIPWVAVIGQSVSIASAQSGSGENSLETAWRAESESLKSILTGAPQSKLGRIALVDTLASQIRSRMKLRLPSVLSGLQGKSQIVQDELARLGEQLVNSAEGTRAIALELCREFEDKFLLHLAGGEGSGWKVVASFEGNFPNRIKQLPLDRHFDLNNVKRVVLEADGYQPYLISPEKGLRSLIKIVLELAKDPARLCVDEVHRVLVDIVSASANATPGLGRYPPFKREVVAIASAALDGFKNEAKKMVVALVDMERAFVPPQHFIRLVQRRMERQRREEELKGRSSKKGQDAEQSLLSRATSPQPDGPTAGGSLKSMKDKPSPQDKETPEVSGLKTAGPEGEITAGYLMKKSAKTNGWSRRWFVLNEKTGKLGYTKKQEERNFRGTITLEECTIEEIPEDEVEKSKSSKDKKANGPDSKGPGLVFKITCKVPYKTVLKAHNALVLKAESVVDKNEWINKLQKVIQARGGQVGSVSMRQSLSEGSLDKMVRKPIDPEEELRWMSQEVRGYVEAVLNSLAANVPKAVVLCQVEKAKEDMLNQLYSSISAIGNERIESLIQEDQNVKRRRERYQKQSSLLSKLTRQLSIHDNRAAAASSYSDNSGTESSPRASGGSSGDDWMNAFNSAANGPSDSLSKYGSGGHSRRYSDPAQNGDAASPGSGSNRRTTPNRLPPAPPPTGSAYRY
Protein: NADPH dehydrogenase (EC 1.6.99.1) (Q928C2)
Organism: Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Function: Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes.
Interaction partners:
- Gluconeogenesis factor
- Probable cell division protein WhiA
- Nucleotide-binding protein lin2617
Sequence:
MSKLFSEYKLKDVTLKNRIVMSPMCMYSVENKDGIATDFHFAHYVSRAAGGTGLVILEATAVQEVGRISEFDLGLWNDEQVPALKRLVDGLHYHGAKAGIQLAHAGRKAVLPGEIVAPSAIPFDEKSAKPVELTKEAIKEVVADFKRAAYRAKEAGFDVIEIHAAHGYLIHQFLSPISNRREDNYGGPAGNRYKILSDIIKAVKEVWDGPIIVRVSATDYAHGGLQLEDHIPFAKWMKADGVELIDVSTGGLVNVEPPVFPGYQVPFADEIRRGAGIATGALGLITRGEQAEEILCNERADLIIIGRELLRNPYFAKEAAETLGETIEAPKQYSRAWK
Protein: Gustatory and pheromone receptor 39a, isoform B (P58956)
Organism: Drosophila melanogaster (Fruit fly)
Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. Plays a role in sustaining courtship behavior in males, possibly through the reception of a stimulating arrestant pheromone.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MGTRNRKLLFFLHYQRYLGLTNLDFSKSLHIYWLHGTWSSTAIQIVVVGVFMAALLGALAESLYYMETKSQTGNTFDNAVILTTSVTQLLANLWLRSQQKSQVNLLQRLSQVVELLQFEPYAVPQFRWLYRIWLLVCLIYGAMVTHFGINWLTTMQISRVLTLIGFVYRCVLANFQFTCYTGMVVILKKLLQVQVKQLEHLVSTTTISMAGVAGCLRTHDEILLLGQRELIAVYGGVILFLFIYQVMQCILIFYISNLEGFHSSNDLVLIFCWLAPMLFYLILPLVVNDIHNQANKTAKMLTKVPRTGTGLDRMIEKFLLKNLRQKPILTAYGFFALDKSTLFKLFTAIFTYMVILVQFKEMENSTKSINKF
Protein: Prohibitin (Q57UX1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU366048}.
Interaction partners:
- Prohibitin
- Mitochondrial processing peptidase alpha subunit, putative
- tetrahydrofolate synthase
- Stomatin-like protein, putative
- Zinc metallopeptidase, putative
- Metalloprotease, putative
- ATP-dependent zinc metallopeptidase, putative
- Mitochondrial ATP-dependent zinc metallopeptidase, putative
- ATP-dependent zinc metallopeptidase, putative
- Mitochondrial ATP-dependent zinc metallopeptidase, putative
Sequence:
MSFRFVQRFMLGVTAASAGFYSCCFVVYPGEAAILYNRITGLKDSVYGEGLQCRILGLDEIKVFNIRIRPRVLKTMTGTKDLQMVNISLRVLFRPQTDRLPQIYREFGMDYDERILPSISNEILKAVVAEYKAEELIQKRDVVSARIYQLMQSKVSQFGLVLEDLSLVDIQFGKEFMVAVEQKQVAQQEAERFRYVVLENEQKRRAAVVRAEGEAESARLISEAIQRSGGGLLELRRIEAAVDIASKLIPMRNVTFLPGGSNMLLHMKSHQASEQAH