wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase substrate receptor MMS22 (Methyl methanesulfonate-sensitivity protein 22) (Synthetically lethal with MCM10 protein 2) (Q06164)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-MMS22). RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition.
Subcellular location: Nucleus {ECO:0000269|PubMed:15718301}. Note=Nuclear punctate foci structures.
Interaction partners:
- E3 ubiquitin-protein ligase linker protein MMS1
- Regulator of Ty1 transposition protein 107
- Cullin-8
- DNA polymerase alpha-binding protein
- RING-box protein HRT1
- Histone acetyltransferase RTT109
- ATP-dependent DNA helicase RRM3
- Mediator of replication checkpoint protein 1
- ATP-dependent DNA helicase SRS2
- Histone chaperone ASF1
Sequence:
MDVDEPNPIVISDSEATDEEISIIYEPEFNENYLWAEENVQEASRSQKIVTERLSLDSTAGESCTPSVVTDTQVTTGLRWSLRKRKAIQKMPYSLERIKHRQLLEGYDISSFDSISNQLTLPKNASTVIHSNDILLTKRTGKPLDEQKDVTIDSIKPENSSVQSQRYDSDEEIPKKRHRTFKDLDQDIVFQSGDSTEDEQDLASTNLQNTQNDEVIFRGRVLNVRTGYRGVLPRVAWEKSLQKQQSSKVTKRKTQLLNHKGVAKRKMNRSAHIEDEEQNLLNDLIAPDDELDIEENAPPDIYLGNLPEDREANEKELKELQEYYESKYSEDAQSAGTSGFNLNEEYRNEPVYELEYDGPGSCISHVSYKDQPIIYLNSRHSDSGFSEQYNISAEDNQSVISLDAAEEHNDGIIDKMLVKPKRIKATNDANFLNTKSKRVRRYKYKYRNSCLAPSTKAIKVGKRSAHKSHLAANNPVSFVSKKNHVIDDYFFEELESQSLEQDDSSSLKPQKKRRKKKAPIYSSFSADLESRRKPVFNTVVEVPTNRYAFTKPNVRNRDSINHDMEFEEEDSNQELGPIMVVLDSILLKKPFEPPNFFKIQLSDKSFLLSKLNPADIATSLQKIFRVIIDKGITDTELVHFNESLIAFLVHLDMPELFDLIGEFHREFRSKVNSLRKKAKPIHFFQIAACQLMFLEISRYNKISAAAKFDMDVKLLDHIVSFFKLLSVCYDSVMKNPMQYLYTSYYILSAVVDVIHKKEALWDLFQKHPFSPHISLLLVNIFPTKVCRWQVLRLDSEFQPLSSAFRFINYCIETCNWNVTNSLILSLDRIFKRRRFSDFEEESDLSQNNKIIYPPTNQLTSRLMFNRYLHLLTLCELSSSDTQRVIPMGDISMNDSLSVLKNRLNLLIVLATRFDLNLEKRFQELTRPLYSKEYLNLHTQNTVRTITTLIMQASLSFLEISRIKNHPFSGKFIASLFDKLVLQQPSISGVTENFLKEFTNLVSKMKRKSVSMLKFLYPSLVAMSQENIFESSFFLLLQVYLKSLDVLGPTWVQNYLFQFIKSKAQENERWIECYCQIGKFLVDSGIFTWWTFFTYNGLDAALHFQLAFHSLIIDFCDTDSFELLKKPLYSIASDLLLISKDDAFYHFLSNLLKRAHIIVADLKPVSDENELLRLAYIFSKALKKNAYQDLLAVFLSLAKKHYDEGDISRNFLAKYLEFLNKNCLTELRNNQLFISLRRELGISSDEDEKCAFWDSFNEAGDILSKAAFVETGIVQACCTGNEIDGYLDNLSTLFTSTMLESPFAFFSDLVIAHIFENRPFFDVNIKNFLLSHFIDLFNKVLKMKFEQVSPDEFAELCKVYRALCIECATDDTFNSNSDLIAAKDAFLVSVLRIADGFWEHDKLLQLRMLDSNMNIPNQIPHTTLQSSLSAIVIKIIESNIGKIEASEPFKTFKNT
Protein: Microtubule-associated protein 9 (D3ZAG3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSDEIFSTTLAYTKSPKATKRTSFQDELIRAITARSARQRSSEYSDDFDSDEIVSLGEFSDTSTDESLIRKKMNDFHMSDDEEKNSPRLSFLKTKKVNSEISKDDLDSVILDSEGTSPDAQEDMTGNSTPKSQNDDQDVGREVITMKPTPRMLPGKRSTSSGENSSSLDTDGHFKPSPRPRSMLKKSWHPEEGVRSGVDKEYSTTEDSAPTPSLPRQNGTELQTEEKVCSENLDLEDSLLQSLTSSSLKESPGGCISPGSQEKTPIKDHDGEPTEIWDSLISNENEGSSILVNCVTPELEQPKEGQVAADNLEEEREKGGFTEDDLTTDPLLSTSPSVITPTEPAEPAKKTNEVKTTKNKKTTNNRVSSASGRLMTSEFLKRSGPTKRSPSAATSSHYLGSLKVLDQKPPRKQSLEPDKADHIRAAVYQEWLEKKNVYLHEMHRIKRIESENLRIQNEQKKAAKREEALASFEAWKAMKEKEAKKIAAKKRLEEKNKKKTEEENAVRKGEALQAFEKWKEKKLEYLKEKTRREKESERAKKQKEEEAVAEKKKDSVTAFERWSEKKEALLKQKEKEKINERRKEELKRAEKKDKDKQAISEYEKWLEKKERQERIDRKQKKRHSFLESETHPPWSPPSRTAPSKVF
Protein: Peroxisomal membrane protein 13 (ABSTINENCE BY MUTUAL CONSENT) (Peroxin-13) (AtPEX13) (Peroxisome biogenesis protein 13) (Pex13p) (Protein ABERRANT PEROXISOME MORPHOLOGY 2) (Protein AMC) (Q9SRR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (By similarity). Essential for pollen-tube discharge that take place only in the presence of functional peroxisomes in either the male or the female gametophyte.
Subcellular location: Peroxisome membrane {ECO:0000305|PubMed:16813573, ECO:0000305|PubMed:18160292}; Peripheral membrane protein {ECO:0000305|PubMed:16813573}.
Interaction partners:
- Peroxisomal membrane protein PEX14
- Probable purine permease 7
- Peroxisome biogenesis protein 7
- Peroxisome biogenesis protein 5
- Peroxisomal ATPase PEX6
- Pollen-specific leucine-rich repeat extensin-like protein 1
- Protein APEM9
- Peroxisome biogenesis factor 10
- Pollen-specific leucine-rich repeat extensin-like protein 2
- Peroxisome biogenesis protein 12
Sequence:
MASQPAGGSPPKPWEKEGNTSGPNPFRPPSNTSTAGSVEASGTANPGEVVPPPVNRPNTAANMNSLSRPVPARPWEQQNYGSTMGGGYGSNLGMTSGYGSGTYGSALGGYGSSYGGGMYGGSSMYRGGYGGGGLYGSSGMYGGGAMGGYGGTMGGYGMGMGTGMGMGMGMGMGGPYGSQDPNDPFNQPPSPPGFWISFLRVMQGAVNFFGRVAMLIDQNTQAFHMFMSALLQLFDRGGMLYGELARFVLRMLGVRTRPRKMQQPPQGPNGLPLPHQPHGNQNYLEGPKTAAPGGGGGWDNVWGN
Protein: Abnormal cell migration protein 21 (G1FC92)
Organism: Caenorhabditis elegans
Function: Required for determination of left/right asymmetry in nervous system. Acts together with unc-40 to control an initial left-right asymmetric polarization of the Q neuroblasts. Mig-21 and unc-40 may control the asymmetry in Wnt signaling response by restricting posterior polarization to one of the 2 Q neuroblasts. Involved in left-side QL posterior migration. In right-side QR, unc-40 and mig-21 pathways mutually inhibit each other in posterior migration, allowing anterior QR migration.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Tyrosine-protein phosphatase Lar-like
- C-mannosyltransferase dpy-19
- Cadherin-4
- Netrin receptor unc-40
Sequence:
MERDSNTAKSEIFYSNPAIWRHLKDGKGEGMSKSEKRNKHGCRNFTYSIWNCIRPGGWSTWSKWSKCREGIRKRRRTCNNPLPIGTTCSGQKVEKQSCAISSNVPEYLFGSWTSWNPWSRCDCDRSLRIRTRHCKGNSCEGCDKDYEDCRPDECPISKKWSEWTDWVNYGIEQVRFSAWCSSSNVANTEVGIRKETQDSMKHANWSEWHMHPGVAYRYRLLHNSSISIEHHLLSRFTSSCLPLHFAIPIFCFCILTGFLLQNIIYCVVNRFKRRFIRLNYSYDSNPRDYPSHLIRSPGSPKDESFW
Protein: Y-box-binding protein 3 (Cold shock domain-containing protein A) (DNA-binding protein A) (Y-box protein 3) (Q9JKB3)
Organism: Mus musculus (Mouse)
Function: Binds to the GM-CSF promoter. Seems to act as a repressor (By similarity). Binds also to full-length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10772793}. Nucleus {ECO:0000250}.
Interaction partners:
- Decorin
- Tight junction protein 1
- G1/S-specific cyclin-D1
- Cyclin-dependent kinase 4
- Symplekin
- Y-box-binding protein 1
Sequence:
MSEAGEATTGGTTLPQAAADAPAAAPPDPAPKSPAASGAPQAPAPAALLAGSPGGDAAPGPAPASSAPAGGEDAEKKVLATKVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKKNNPRKYLRSVGDGETVEFDVVEGEKGAEAANVTGPDGVPVEGSRYAADRRRYRRGYYGRRRGPPRNYAGEEEEEGSGSSEGFEPPAADGQFSGARNQLRRPQYRPPYRQRRFPPYHVGQTFDRRSRVFPHPNRMQAGEIGEMKDGVPEGTQLQAHRNPTYRPRFRRGPARPRPAPAIGEAEDKENQQAANGPNQPSARRGFRRPYNYRRRSRPLNAVSQDGKETKAGEAPTENPAPATEQSSAE
Protein: Acetylcholine receptor subunit delta (P02716)
Organism: Mus musculus (Mouse)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Acetylcholine receptor subunit gamma
- Acetylcholine receptor subunit beta
- Neuronal acetylcholine receptor subunit alpha-4
- Neuronal acetylcholine receptor subunit alpha-6
- Neuronal acetylcholine receptor subunit beta-2
- Syntaxin-binding protein 5
- Acetylcholine receptor subunit alpha
- 43 kDa receptor-associated protein of the synapse
- Neuronal acetylcholine receptor subunit alpha-9
- Muscle, skeletal receptor tyrosine-protein kinase
Sequence:
MAGPVLTLGLLAALVVCALPGSWGLNEEQRLIQHLFNEKGYDKDLRPVARKEDKVDVALSLTLSNLISLKEVEETLTTNVWIDHAWVDSRLQWDANDFGNITVLRLPPDMVWLPEIVLENNNDGSFQISYACNVLVYDSGYVTWLPPAIFRSSCPISVTYFPFDWQNCSLKFSSLKYTAKEITLSLKQEEENNRSYPIEWIIIDPEGFTENGEWEIVHRAAKLNVDPSVPMDSTNHQDVTFYLIIRRKPLFYIINILVPCVLISFMINLVFYLPGDCGEKTSVAISVLLAQSVFLLLISKRLPATSMAIPLVGKFLLFGMVLVTMVVVICVIVLNIHFRTPSTHVLSEGVKKFFLETLPKLLHMSRPAEEDPGPRALIRRSSSLGYICKAEEYFSLKSRSDLMFEKQSERHGLARRLTTARRPPASSEQVQQELFNEMKPAVDGANFIVNHMRDQNSYNEEKDNWNQVARTVDRLCLFVVTPVMVVGTAWIFLQGVYNQPPLQPFPGDPFSYSEQDKRFI
Protein: Ribosomal protein L18 (J3QQ67)
Organism: Homo sapiens (Human)
Subcellular location: Rough endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004427}.
Interaction partners:
Sequence:
XPQGVDIRHNKDRKVRRKEPKSQDIYLRLLVKLYRFLARRTNSTFNQVVLKRLFMSRTNRPPLSLSRMIRKMKLPGRENKTAVVVGTITDDVRVQEVPKLKVCALRVTSRARSRILRAGGKILTFDQLALDSPKGCGTVLLSGPRKGREVYRHFGKAPGTPHSHTKPYVRSKGRKFERARGRRASRGYKN
Protein: Hyperkinetic, isoform E (Q9W2X0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSMALCNLNGDGSAAQSTSQSQSQSPAATAAAAPLLPHSHSHTLQPESTPLLLGHEQSGSAAPEGSGGGDVTDGAVTSIEMPTVVADDAGVPPLPLPLPQSTPQPLLMALPANLNFITGPTTQQLMIGNGAMGVIPSTNDSNNNNNNNNNVDNTSDESNPVTIYRCRAPIASLDCMEEFSRSISLGSNPALPLRHGSTPTPGLRYKNLGKSGLRISNVGLGTWPVFSPGVSDDQAEAILKLAIESGINLFDISEAHSETEIGKILQRAGWKRTAYVITTKVYWSTKSEERGLSRKHIIECVRASLQRLQLQYIDIVIIHKADPMCPMEVVRAMSYVIQQGWAMYWGTARWSQVEIMEAYTNCRQFNCITPIVEQSEYHMFCREKCELYLPEMYNKIGVGLMAWGPLSMALSDTQNGDKLFLPKGSFKTKSFSWTEDEINRNAALSPQGSWGKDRIDEGRRHCDRLRDLAALAEKLGCSPTQLSIAWSLKHEPVQCLLLGATSAEQLHQSLQSLQLLPRLSSSVMLELERILENKPVRPPMISTLALR
Protein: ABC-type glutathione-S-conjugate transporter (EC 7.6.2.3) (Q7KTB9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Vacuole membrane {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128}.
Interaction partners:
Sequence:
MADDTSSPMDRFCGSTFWNATETWYTNDPDFTPCFEQTALVWTPCAFYWAFVIFDFYYLKASLDRNIPWNKLNVSKALVNLGLLVITALDLIMALVKKGGDSELPLYDLDVWGPIIKFATFLLLFIFIPLNRKYGVQTTGCQFIFWFLLTVLSIPRCRTEVRLDAERQKILNSQQPSEQDFSWEEYQFVSFFIFFTFTSIMLILNCFADGMPRQTKYQRGENEIPELSASFLSRITYQWFDKMALKGYRNPLEEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKNYKNKARVEPKAQFSNGNVTFENPHGEKNGRKKGMASIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLIDENNVLDATKTFVSLSLFNILRFPLTMLPMLITNLVQTQVSVNRINKFLNSEELDPNSVLHDSSKPHPMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFIIQHLQEGNEEEEELNQIKRQISSTADVPELLGTVEKAIKLARTESLSDSISVTSADSLMGGGGSLRRRTKRQDSHDSVASAASLKKKQEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRDMYLGVYGAFGFGQGLCNYGAAISLFTATLHASSRVFHRLFNNIMHCPSEFFDTTPKGRILDRCSSDVNCLDLVMPLNIRMVMSTAFQVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPWELEQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAFYSMAKDANLV
Protein: Inactive N-acetylated-alpha-linked acidic dipeptidase-like protein 2 (NAALADase L2) (Q58DX5)
Organism: Homo sapiens (Human)
Function: May be catalytically inactive.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Nipped-B-like protein
Sequence:
MGENEASLPNTSLQGKKMAYQKVHADQRAPGHSQYLDNDDLQATALDLEWDMEKELEESGFDQFQLDGAENQNLGHSETIDLNLDSIQPATSPKGRFQRLQEESDYITHYTRSAPKSNRCNFCHVLKILCTATILFIFGILIGYYVHTNCPSDAPSSGTVDPQLYQEILKTIQAEDIKKSFRNLVQLYKNEDDMEISKKIKTQWTSLGLEDVQFVNYSVLLDLPGPSPSTVTLSSSGQCFHPNGQPCSEEARKDSSQDLLYSYAAYSAKGTLKAEVIDVSYGMADDLKRIRKIKNVTNQIALLKLGKLPLLYKLSSLEKAGFGGVLLYIDPCDLPKTVNPSHDTFMVSLNPGGDPSTPGYPSVDESFRQSRSNLTSLLVQPISAPLVAKLISSPKARTKNEACSSLELPNNEIRVVSMQVQTVTKLKTVTNVVGFVMGLTSPDRYIIVGSHHHTAHSYNGQEWASSTAIITAFIRALMSKVKRGWRPDRTIVFCSWGGTAFGNIGSYEWGEDFKKVLQKNVVAYISLHSPIRGNSSLYPVASPSLQQLVVEKNNFNCTRRAQCPETNISSIQIQGDADYFINHLGVPIVQFAYEDIKTLEGPSFLSEARFSTRATKIEEMDPSFNLHETITKLSGEVILQIANEPVLPFNALDIALEVQNNLKGDQPNTHQLLAMALRLRESAELFQSDEMRPANDPKERAPIRIRMLNDILQDMEKSFLVKQAPPGFYRNILYHLDEKTSRFSILIEAWEHCKPLASNETLQEALSEVLNSINSAQVYFKAGLDVFKSVLDGKN
Protein: TAR DNA binding protein, like (TAR DNA binding protein, like isoform X2) (Tardbpl protein) (Q803N5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTECYIRVAEDENEEPMEIPSEEDGTVLLSTVAAQFPGACGLRYRSPVSQCMRGVRLVEGVLHAPEADWGNLVYVVNYPKDNKRKMDEMDAASAVKIKRGIQKTSDLIVLGLPWKTTEQDLKDYFGTFGEVIMVQVKRDAKSGNSKGFGFVRFTDYETQIKVMSQRHMIDGRWCDCKLPNSKYFLEQAGPDEPMRSRKVFVGRCTEDMTADELRQFFMQYGEVTDVFIPKPFRAFAFVTFADDQVAQSLCGEDLIIKGTSVHISNAEPKHNNIHHLFSNFPGRSPSLAAMFERSQYQFPSSHV
Protein: Spliceosome RNA helicase DDX39B homolog (EC 3.6.4.13) (DEAD box protein UAP56) (Q18212)
Organism: Caenorhabditis elegans
Function: Required for spliced RNA export out of the nucleus. May play a role in spliceosome assembly.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- THO complex subunit 2
- RRM domain-containing protein
- Chromatin target of PRMT1 protein C-terminal domain-containing protein
- Chromatin target of PRMT1 protein C-terminal domain-containing protein
- Chromatin target of PRMT1 protein C-terminal domain-containing protein
- RNA-binding protein rnp-4
- Death domain-containing protein
- SAP domain-containing protein
- THO complex subunit 5
- THO complex subunit 7 homolog
Sequence:
MEEEQLLDYEEEQEEIQDKQPEVGGGDARKTKGTYASIHSSGFRDFLLKPEILRAIGDCGFEHPSEVQHECIPQAILGMDVVCQAKSGMGKTAVFVITTLQQLEPVDGEVSVVCMCHTRELAFQISKEYERFSKYLPGVKVAVFFGGMAIKKDEERLANDCPHIVVGTPGRMLALARSGKLKLDKVKYFVLDECDKMIGDADMRRDVQEIVKMTPQQKQVMMFSATLPKELRTVCKRFMQDPMEVYVDDEAKLTLHGLQQHYVKLKEAEKNRRLLNLLDALEFNQVVIFVKAVKRCEALHQLLTEQNFPSIAIHRQMAQEERLSRYQAFKDFQKRILVATDLFGRGMDIERVNIVFNYDMPEDSDSYLHRVARAGRFGTKGLAITFVSDENDAKTLNSVQDRFDISITELPEKIDVSTYIEGRTN
Protein: Advillin (p92) (O75366)
Organism: Homo sapiens (Human)
Function: Ca(2+)-regulated actin-binding protein which plays an important role in actin bundling. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis. In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:29058690}. Cell projection, lamellipodium {ECO:0000269|PubMed:29058690}. Cell junction, focal adhesion {ECO:0000269|PubMed:29058690}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9WU06}. Cell projection, axon {ECO:0000250|UniProtKB:Q9WU06}. Note=In podocytes, present in the F-actin-enriched cell periphery that generates lamellipodia and focal adhesions. {ECO:0000269|PubMed:29058690}.
Interaction partners:
- Actin-related protein 3
Sequence:
MPLTSAFRAVDNDPGIIVWRIEKMELALVPVSAHGNFYEGDCYVILSTRRVASLLSQDIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQYHESDTFRGYFKQGIIYKQGGVASGMKHVETNTYDVKRLLHVKGKRNIRATEVEMSWDSFNRGDVFLLDLGKVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAKIGVIEGDKEAASPELMKVLQDTLGRRSIIKPTVPDEIIDQKQKSTIMLYHISDSAGQLAVTEVATRPLVQDLLNHDDCYILDQSGTKIYVWKGKGATKAEKQAAMSKALGFIKMKSYPSSTNVETVNDGAESAMFKQLFQKWSVKDQTMGLGKTFSIGKIAKVFQDKFDVTLLHTKPEVAAQERMVDDGNGKVEVWRIENLELVPVEYQWYGFFYGGDCYLVLYTYEVNGKPHHILYIWQGRHASQDELAASAYQAVEVDRQFDGAAVQVRVRMGTEPRHFMAIFKGKLVIFEGGTSRKGNAEPDPPVRLFQIHGNDKSNTKAVEVPAFASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELASLLCDGSENTVAEGQEPAEFWDLLGGKTPYANDKRLQQEILDVQSRLFECSNKTGQFVVTEITDFTQDDLNPTDVMLLDTWDQVFLWIGAEANATEKESALATAQQYLHTHPSGRDPDTPILIIKQGFEPPIFTGWFLAWDPNIWSAGKTYEQLKEELGDAAAIMRITADMKNATLSLNSNDSEPKYYPIAVLLKNQNQELPEDVNPAKKENYLSEQDFVSVFGITRGQFAALPGWKQLQMKKEKGLF
Protein: Uncharacterized protein C14F5.01 (O60098)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MKRSYKDIIRFLKLIGISHSTAIKLVDGILPVMIGLKTSYLVDCVFLEISELREIIEFVGPDCLRGIYFTEPISQCFVLHVANWEEWSSIDSLVPIVVDLPSKKQNRLLQSCITKHVDRLLDLCKRNLSTFTIDISSSWRQNIIENNEQKEFECTSTAITGCLLNYGATYNYDHTLFKDNGLSCETLKLYTLEVHSKKKDVSDTLIQFSCVNQFEEPVTSNIQRLTSLYQTRWKRINSEEKRNWEEWIKHKYKIPNDTNIELEFCFSVTDRKEQSVIL
Protein: Beta-2 adrenergic receptor (Beta-2 adrenoreceptor) (A0A060Y644)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- GNAS complex locus
- Endothelin-3
- Neuropeptide Y
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Uncharacterized protein
Sequence:
MENVSTSALFNLSDLPVEMNLSSHHWSYSEYSEAEAVLLGIIMALLVLGIVFGNVLVITAIVRFQRLQTVTNMFITSLACADLVMGLLVVPFGACYILLNTWHFGSFLCEFWTAADVLCVTASIETLCVIALDRYLAITSPLRYPSLLTKHKACVVVVTVWGVAALISFLPIHMKWWVSDEPEALSCLENAHCCDFNTNAAYAVASSVVSFYIPLAVMAFVYGRVFQEARKQLQKIRGSEGRFHAQIINNNKGQDGGGGGGGNGKRPKFCLKEHKALKTLGIIMGTFTLCWLPFFVLNVAVTIWKVDNIKMPFRILNWIGYANSAFNPLIYCRSPEFRYAFQEILCLRGTAFPTNEYIYRGHSLQVSPKDKPGCSIHDTGTMELSTGSRSSVPNTNRNCNKPSLASIV
Protein: Stress enhanced protein 2, chloroplastic (Q9SJ02)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in non-photochemical quenching, a process that maintains the balance between dissipation and utilization of light energy to minimize generation of oxidizing molecules, thereby protecting the plant against photo-oxidative damage (By similarity). May play a photoprotective role in the thylakoid membrane in response to light stress (Probable).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:10725357}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Stress enhanced protein 1
- Cytochrome P450 71B9
- Early light-induced protein 1
- Light-harvesting complex-like protein OHP1, chloroplastic
Sequence:
MAMATRAIRYQLPSPRFRAPRCESSEPIKQIQIQQRPRGGDLAENGKIVLQPRLCTLRSYGSDMVIAKKDGGDGGGGGSDVELASPFFETLTDYIESSKKSQDFETISGRLAMIVFAVTVTEEIVTGNSLFKKLDVEGLSEAIGAGLAAMGCAAMFAWLTISRNRVGRIFTVSCNSFIDSLVDQIVDGLFYDTKPSDWSDDL
Protein: At1g66080 (Hikeshi-like protein) (Q9C8D7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Nuclear pore complex protein NUP35
- Nuclear pore complex protein NUP155
- Nuclear pore complex protein NUP107
- At4g27652
- At4g27654
- Probable LRR receptor-like serine/threonine-protein kinase At4g37250
- AT5g23340/MKD15_20
- GEM-like protein 6
- FCS-Like Zinc finger 13
- Expressed protein
Sequence:
MFGVVFPNRSFPIDISTFTQIDTFHWVLDMNHFVGEAYDQISEMCIFLLNNFNLPPDKALAVYVQSPGSAFVFCGAVTLARPSAVLSLQWPEPGSAAKMQLTAGDSSSLSAKIGVSVEDVAALRSLDVVAERRIEKLAMKVGENLFNFMQSFCGVDGSKLVVPMDILDRWFKKFQEKAKRDPDFLKSFAL
Protein: Serine protease (O06316)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MTTSRTLRLLVVSALATLSGLGTPVAHAVSPPPIDERWLPESALPAPPRPTVQREVCTEVTAESGRAFGRAERSAQLADLDQVWRLTRGAGQRVAVIDTGVARHRRLPKVVAGGDYVFTGDGTADCDAHGTLVAGIIAAAPDAQSDNFSGVAPDVTLISIRQSSSKFAPVGDPSSTGVGDVDTMAKAVRTAADLGASVINISSIACVPAAAAPDDRALGAALAYAVDVKNAVIVAAAGNTGGAAQCPPQAPGVTRDSVTVAVSPAWYDDYVLTVGSVNAQGEPSAFTLAGPWVDVAATGEAVTSLSPFGDGTVNRLGGQHGSIPISGTSYAAPVVSGLAALIRARFPTLTARQVMQRIESTAHHPPAGWDPLVGNGTVDALAAVSSDSIPQAGTATSDPAPVAVPVPRRSTPGPSDRRALHTAFAGAAICLLALMATLATASRRLRPGRNGIAGD
Protein: Uncharacterized protein At5g42070 (Q8RWR9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein cL37
Sequence:
MANSISSISLPRCFIFNNGSHKSRPWPSSSSFFLNKSSKHHPHPLLSLSSSPSSVVETDNDDDNDLTFSGCRACGKEEKESGCNGDGRIQGGIATVPGFGWWPIKAYRPCPAFVEAGGRYRRIGQSMDEVAFGRGDSKSSTSVDTSDSLLRQTKPTSSSKSSNK
Protein: Septin-14 (Q9DA97)
Organism: Mus musculus (Mouse)
Function: Filament-forming cytoskeletal GTPase (Probable). Involved in the migration of cortical neurons and the formation of neuron leading processes during embryonic development. Plays a role in sperm head formation during spermiogenesis, potentially via facilitating localization of ACTN4 to cell filaments (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20181826}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33228246}. Cell projection, axon {ECO:0000269|PubMed:20181826}. Cell projection, dendrite {ECO:0000269|PubMed:20181826}. Perikaryon {ECO:0000269|PubMed:20181826}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:33228246}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q6ZU15}. Note=Colocalizes with actin stress fibers (By similarity). Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (PubMed:33228246). {ECO:0000250|UniProtKB:Q6ZU15, ECO:0000269|PubMed:33228246}.
Interaction partners:
- Septin-4
- Septin-10
- Septin-7
- Septin-9
- Septin-8
- Neuronal-specific septin-3
- Septin-6
- Septin-1
- Septin-5
- Septin-11
Sequence:
MAEKPTNTSVPIPGSEDPQKENIRCLSTLGHFGFECLPTQLVNKSIQKGFSFNILCVGETGIGKTTLINTLFNTNLKETKSSHFYSKVGLTVKTYELLERNIPLRLTVVKTVGYGDQINKEASYQPVVDYLDAQFEAYLQEELKIKRSLADYHDSRIHVCLYFITPTGHSLKSLDLLTMKSIDRRVNIIPLIAKADSLSKNDLQRFKNNIMSELNSNGIQIYQFQVDDEASAQVNSSGLLPFAVVGSMEEVKVGKRMVRGRHYPWGVLQEVENENHCDFVKLRDLLLSTNMEDLKDQTHTQHYECYRSNRLQKLGFSDTGPDNRPVSFQEMYEAKRREFHNQCQKEEEELKQTFMQRVKEKELTFKDAEKELQDKFEHLKRIQQEEILKLEEERRKLEEQIIDFYKMKAASESAQAQVCTNIKKDKDRKK
Protein: Ribulose bisphosphate carboxylase (RuBisCO) (EC 4.1.1.39) (P04718)
Organism: Rhodospirillum rubrum
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.
Interaction partners:
Sequence:
MDQSSRYVNLALKEEDLIAGGEHVLCAYIMKPKAGYGYVATAAHFAAESSTGTNVEVCTTDDFTRGVDALVYEVDEARELTKIAYPVALFHRNITDGKAMIASFLTLTMGNNQGMGDVEYAKMHDFYVPEAYRALFDGPSVNISALWKVLGRPEVDGGLVVGTIIKPKLGLRPKPFAEACHAFWLGGDFIKNDEPQGNQPFAPLRDTIALVADAMRRAQDETGEAKLFSANITADDPFEIIARGEYVLETFGENASHVALLVDGYVAGAAAITTARRRFPDNFLHYHRAGHGAVTSPQSKRGYTAFVHCKMARLQGASGIHTGTMGFGKMEGESSDRAIAYMLTQDEAQGPFYRQSWGGMKACTPIISGGMNALRMPGFFENLGNANVILTAGGGAFGHIDGPVAGARSLRQAWQAWRDGVPVLDYAREHKELARAFESFPGDADQIYPGWRKALGVEDTRSALPA