wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein, isoform A (Q86B80)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD21953p
- Diphosphomevalonate decarboxylase
- Hydroxymethylglutaryl-CoA synthase
- [F-actin]-monooxygenase Mical
Sequence:
MLLLLLAFIMRFVDISKRCAACSRAGIDCTHHSGQSNPQASDANGNHTACWQHVAGGTSNSNSNSSSTSSGCDSNSSSKENYYVPQQLQHQRQRVAKHSKPGNIGVSPQQLEQIRFYQRMQQQQLQLLQQQLLQRRRLQQQLLQQGVPSPPANATTTTAGLTCNQQYLRQQRMQQQQLQQQQQQQQQYVDNNSNNDNNNYLNNYLNNSINQRNNGRVLGQGTKIRRGMTEFSTNNDHSKPHFTASQQKPHQNSPIHQQAFTPSNPNTHPHLLQRLAQQQQQQQQQQHQRPHKFQQSLPFSQLNNGNNTAAHILPGSSPHSPLSYRNPLNSPSNSPFSNTAQTTIGKRYQQQQLTDRLLQQQHLQQCQQQQLQSLGSSDVEEDLAAEELSEESLKQNVAIVLSNLDRYNNALRSIILNEQVSSSIITPSDSLLFGEDSSGLLYCDNDNSRKHKGNNNFVLGKMAATPESDYNSNATTPGGRSSEQQLQQQQQQQQLGVGGMLCGGGGGGGVGMRETTNGGGNNLNCSLASSHDFTHDNSDYQWFLDYGYRDGCGGMQRSVLSSLSASYNAMGDLIYYEDLAKNLDANLAEVDMESFRAEDIHSLLSHLPAYCKSLGGTNSRLQQSLLLQQQQQQQQQLQQQQVLQHNSMLQHMSQTSTTSTNELIDNSFCKSELLFSPVRESHISVDSLDMDAYPDDGEIILTCNKDNYTIAFEGSVLYSDDSFYADPSDIAARNKQNCINLHSNLEDIVKRNKALEVSMSRSAQAFQPLCPMSPKGQAATTSAAKLQRRSLFLVSPARRYPSGNNNTETITITRHLPQCTVRKSSSLPNLQNEEAMAGSCHKEQGPEESGPQAVPLNVSQAISTSTMEAGKSRSRNLLPMCQMPISISVSISERLQQQADQQLPSEQITPTSQQPQQQHHHSHHHRHKHRCSCSQESHISGSASSGNSSNPPAFNLVKLFIKQKSSNSSGGQEDLGAQASAHTCMDVSSGCWPSSDAASSSSGSLEQRLRKKSMNDSGKGSAVSRHDEEEHYPDTETPRRQLRARSEAVFYDDVASSSSTGSLTATNSPAHRRRSMPLRNPQLYQLAAQVSTGSQMSSEASSEQLTQVPRRAEAGCGTSTRPLSCASSSEMITRSMQTSCGSLSTTRSSLSDRYRCVPPSFLEKLNNLGEERQAPIYVIYPNYALPDLGFVKTNASTDVIFSPFNYKMTMDGATGSTSSSGSLRKQRNSSQSVSEDEILKTLDYKHVADWQSLATLLPSEYRRRLQHIPEVKHLVRQLDAELSQRPLFCMSPPLRRNRTHICDCAKYFQGQQTQTDEASSSGSSQQPSSGYRGSSTLLTDSELDVDPLKQMYVYQYDQQRMDSGVETSPGSQLTQTPPQPMPRSILRKAHSAQSRSKRNSMIEAQQTQKLTKLEKRRSLQEPPNNYGLGSTDELADVFEEEEHSQPAPPVKQRLSRKDLDARARAESFLASLPRSELKYYAEIASILESSGEHVTYDAAALKKEVSRVLSQQKKVSFNDEGVAAGLQQHAKRFATPPNSPNISMGALKRDTVDVLEQRKIESNRFKRLQIQWELMSKDSSMLKELASEAATKSGGSTPTSGNSTGSNSAPRSRIPRPVSYPAGRSSTPTSSRTAPVLATPSPARPATPKTVTKSHNKPGLFTSPRPSRLTSAQEAAGGNKVSTRSPSRIVQPKRYSLAGATTPTSTTPTSARARTPTNRVAVTAPNTPKRQAVAQSPRPTSRVR
Protein: SNARE protein, putative (Q8IB99)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MFILSDDDVAYSNSINSEEIEESDYENSEAHSRYYEETDEEESNNNDIDDEDLCLFKYVCIGSLDDVDILLKYSLFNRDIDKSANFIVKKILIASKKKLNYCNKKILNWDNHIIYFIICTDKKLALFLIGLDLKASFKNYAFEFLRKLEIYAKSNLFYDKNYVSSHVNPSKVHTIECFMKTTIKNLNKCCKNEKLFAVKQKLNKINSVMNNHIDTLYKSRGNIKALQYKTEDMSKNTLNFVQNTKKLKRIMFLKYWKTYFLCACFLIIGFKVYRSI
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 8 (ADAM-TS 8) (ADAM-TS8) (ADAMTS-8) (EC 3.4.24.-) (METH-2) (METH-8) (Q9UP79)
Organism: Homo sapiens (Human)
Function: Has anti-angiogenic properties.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen alpha-1
Sequence:
MLPAPAAPRWPPLLLLLLLLLPLARGAPARPAAGGQASELVVPTRLPGSAGELALHLSAFGKGFVLRLAPDDSFLAPEFKIERLGGSGRATGGERGLRGCFFSGTVNGEPESLAAVSLCRGLSGSFLLDGEEFTIQPQGAGGSLAQPHRLQRWGPAGARPLPRGPEWEVETGEGQRQERGDHQEDSEEESQEEEAEGASEPPPPLGATSRTKRFVSEARFVETLLVADASMAAFYGADLQNHILTLMSVAARIYKHPSIKNSINLMVVKVLIVEDEKWGPEVSDNGGLTLRNFCNWQRRFNQPSDRHPEHYDTAILLTRQNFCGQEGLCDTLGVADIGTICDPNKSCSVIEDEGLQAAHTLAHELGHVLSMPHDDSKPCTRLFGPMGKHHVMAPLFVHLNQTLPWSPCSAMYLTELLDGGHGDCLLDAPAAALPLPTGLPGRMALYQLDQQCRQIFGPDFRHCPNTSAQDVCAQLWCHTDGAEPLCHTKNGSLPWADGTPCGPGHLCSEGSCLPEEEVERPKPVADGGWAPWGPWGECSRTCGGGVQFSHRECKDPEPQNGGRYCLGRRAKYQSCHTEECPPDGKSFREQQCEKYNAYNYTDMDGNLLQWVPKYAGVSPRDRCKLFCRARGRSEFKVFEAKVIDGTLCGPETLAICVRGQCVKAGCDHVVDSPRKLDKCGVCGGKGNSCRKVSGSLTPTNYGYNDIVTIPAGATNIDVKQRSHPGVQNDGNYLALKTADGQYLLNGNLAISAIEQDILVKGTILKYSGSIATLERLQSFRPLPEPLTVQLLTVPGEVFPPKVKYTFFVPNDVDFSMQSSKERATTNIIQPLLHAQWVLGDWSECSSTCGAGWQRRTVECRDPSGQASATCNKALKPEDAKPCESQLCPL
Protein: Uncharacterized protein C3orf20 (Q8ND61)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSYIKSNLELYQQYTAMAPKLLARISKLLMICQNAGISVPKGIRNIFEFTWEELISDPSVPTPSDILGLEVSFGAPLVVLMEPTFVQVPTLKKPLPPPPPAPPRPVLLATTGAAKRSTLSPTMARQVRTHQETLNRFQQQSIHLLTELLRLKMKAMVESMSVGANPLDITRRFVEASQLLHLNAKEMAFNCLISTAGRSGYSSGQLWKESLANMSAIGVNSPYQLIYHSSTACLSFSLSAGKEAKKKIGKSRTTEDVSMPPLHRGVGTPANSLEFSDPCPEAREKLQELCRHIEAERATWKGRNISYPMILRNYKAKMPSHLMLARKGDSQTPGLHYPPTAGAQTLSPTSHPSSANHHFSQHCQEGKAPKKAFKFHYTFYDGSSFVYYPSGNVAVCQIPTCCRGRTITCLFNDIPGFSLLALFNTEGQGCVHYNLKTSCPYVLILDEEGGTTNDQQGYVVHKWSWTSRTETLLSLEYKVNEEMKLKVLGQDSITVTFTSLNETVTLTVSANNCPHGMAYDKRLNRRISNMDDKVYKMSRALAEIKKRFQKTVTQFINSILLAAGLFTIEYPTKKEEEEFVRFKMRSRTHPERLPKLSLYSGESLLRSQSGHLESSIAETLKDEPESAPVSPVRKTTKIHTKAKVTSRGKAREGRSPTRWAALPSDCPLVLRKLMLKEDTRAGCKCLVKAPLVSDVELERFLLAPRDPSQVLVFGIISSQNYTSTGQLQWLLNTLYNHQQRGRGSPCIQCRYDSYRLLQYDLDSPLQEDPPLMVKKNSVVQGMILMFAGGKLIFGGRVLNGYGLSKQNLLKQIFRSQQDYKMGYFLPDDYKFSVPNSVLSLEDSESVKKAESEDIQGSSSSLALEDYVEKELSLEAEKTREPEVELHPLSRDSKITSWKKQASKK
Protein: RNA binding motif protein 22 (E5RJW4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATSLGSNTYNRQNWEDATCLGENPYIRMTKEKYGKECKICARPFTVFRWCPGVRMRFKKTEVCQTCSKLKNVCQTCLLDLEYGLPIQVRDAGLSFKDDMPKSDVNKEYYTQNMEREISNSDGTRPVGMLGKATSTSDMLLKLARTTPYYKRNRPHICSFWVKGECKRGEECPYRHEKP
Protein: Meiotically up-regulated gene 72 protein (Q9Y7P6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. Note=Localizes at the cell tip and barrier septum.
Interaction partners:
- Uncharacterized pyrophosphatase/phosphodiesterase C725.05c
- Probable 2-dehydropantoate 2-reductase
Sequence:
MSEEDTSKLRILSVGSNAISAFISWRLSESKACHTTLIWRNRCESVLSEGIRIRSSVFGSTKWKPDVVAPTVEQLAMNSEPFDYIFVCLKILPSVYNLDTAIKEVVTPGHTCIVLNTTGIVGAEKELQHAFPNNPVLSFVLPDQFAQRGPLQFEHTTFAADSAKSVIYVGLTEEEDDVPDSVQDAMIETLTLTLEAGGVSCDFLSKIQKKQWETGVGHMCFYPLSIINDEPNLALMYRLKSFAKVIDGLMDEAFSIAQAQGCEFEPEKLDVLKRHIVNRMLATPRPSYPYQDYIAHRPLEVAVLLGYPVEIAKELGVSVPRMETLLALFDAKNKRNLTVRAGTPQSSPNFNPAMRRSPVGAASRSPSRSTIGISNRIGSVDDLLNTRQFTSSPIGGSMPKGPNSIYKIPSASMVNLSSPLVTSPSGLNPTGRPSRFGGRVRGNPLTMNKAGSVSDLLSTSTNMASSDALETASMIGVPSAMPPNSFDMLTLTQRRNRRNNQSSSPPAPSDRRYTMGARRPVQTRGMTDSVIPILEDPMSTLYDTSRYPTRNSKPATPKASRPPSIASTVHRRMD
Protein: Hemomucin (Q58SM8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VTPPKDLKGALESNFHLEGAERLLEGRVYGPECLIARNNEIYTGIHGGEVIKLTSNHVTHVTKIGQPCEDIYEESRCGRPLGLAFDTQGNNLIIADAYYGLWQVDLGTNKKTLLVSPAQELAGKSINRPAKIFNGVTVSKEGDVYWTDSSSDFTIEDLVFASFANPSGRLFKYNRSKNVSEVLLDELAFANGLALSPNEDFIVVAETGAMRLTKYHLKGAKAGQSEVFVDGLPGLPDNLTPDAEGIWVPLVQSADSEHPNGFTLFTRFPSVRLFLARMLALFELPFRYLNSVYPNKFSQRFIHFVGHMESITVLAPKRTTVVRVDWNGNIVGSLHGFDKSAATISHVLEFQDFLFLGSPTNQYLARVKSPKAKQPTLKVRNVRVEGEGLEASIGVPPSKATPKPKAAPSTTTPKPTTTTTTTTPKPTTKTTTTTTTPKPTTTTTTKKPTTTTTTTTTTPKPTTTKPPTAKPSTTTTTTTTPKPTTTTTPTTPTTPTPEPSKPKVKRTVPEKPAPVEEEIPSD
Protein: DnaJ homolog subfamily C member 7 homolog (Q54IP0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Phosphatidylethanolamine-binding protein PEBP
- Phosphatidylethanolamine-binding protein PEBP
- Luminal-binding protein 1
- Small GTPase
- Small ribosomal subunit protein uS10
- Immunoglobulin E-set domain-containing protein
- Heat shock protein 88
Sequence:
MDHEECKTQGNNYFKQSQYMDAIRCYTQAIELSNGTIAAYYGNRAAAYLAICTKSSLQDSIKDSLKAIELERSFIKGYTRASKAYIHLAQYDQAASIIVRGLVFDPRNNELLQEKNQIDSIQRTISSLTKEKALSNPSSSLNQIENVLSQSKYNTQLQVLKARVLIELKQYPQASNLMTTLLQEDSRNPEYLYVRGLSLYYQNNFPLALQHFQNSLTYDPDYSESRVALKRLRSIESKKKEGNEYFQSKNYQAAYDSFTEALSIDPKLETMNSQLYSNRAAALVHLNRISEAINDCTSAVTIDPNYGKAYIRRAQCQMKQENYEDAVRDYEKAQSLDPENGELQRNIKEAKIAHKKSLRKDYYKILGVSKEAGETEIKKAYRKLALQYHPDKNNQLPEEEKAQAEKMFKDIGEAYSVLSDEKKKRQYDMGQDENGMPFDADMGGVDINSVFSQFFNQGGMGGGMGGGGFGGMGGGGFGGMGGGGFSGMGGGGGFGGMPFGFDMGGGGGYGGMGGGFGGHSGHSHGGSRSRSSRGGNEYR
Protein: 3-ketoacyl-CoA synthase 3 (KCS-3) (EC 2.3.1.199) (Very long-chain fatty acid condensing enzyme 3) (VLCFA condensing enzyme 3) (Q9LQP8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:18465198}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase-like protein At1g24470
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Protein ECERIFERUM 2
- Lysophospholipid acyltransferase 1
- Wax ester synthase/diacylglycerol acyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- Peroxisomal adenine nucleotide carrier 1
Sequence:
MDLLVMLLSLLVSYLIFKIWKRIDSKRDQNCYILDYQCHKPSDDRMVNTQFSGDIILRNKHLRLNEYKFLLKAIVSSGIGEQTYAPRLFFEGREQRPTLQDGLSEMEEFYIDTIEKVLKRNKISPSEIDILVVNVSMLNSTPSLSARIINHYKMREDIKVFNLTAMGCSASVISIDIVKNIFKTYKNKLALVVTSESLSPNWYSGNNRSMILANCLFRSGGCAVLLTNKRSLSRRAMFKLRCLVRTHHGARDDSFNACVQKEDELGHIGVHLDKTLPKAATRAFIDNLKVITPKILPVTELLRFMLCLLLKKLRSSPSKGSTNVTQAAPKAGVKAGINFKTGIDHFCIHTGGKAVIDAIGYSLDLNEYDLEPARMTLHRFGNTSASSLWYVLGYMEAKKRLKRGDRVFMISFGAGFKCNSCVWEVVRDLNVGEAVGNVWNHCINQYPPKSILNPFFEKYGWIHEEEDPDTFKMPEGFM
Protein: Hepatocyte nuclear factor 4 4 alpha variant 1 (F1D8S2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MRLSKTLVDMDMADYSAALDPAYTTLEFENVQVLTMGNDTSPSEGTNLNAPNSLGVSALCAICGDRATGKHYGASSCDGCKGFFRRSVRKNHMYSCRFSRQCVVDKDKRNQCRYCRLKKCFRAGMKKEAVQNERDRISTRRSSYEDSSLPSINALLQAEVLSRQITSPVSGINGDIRAKKIASIADVCESMKEQLLVLVEWAKYIPAFCELPLDDQVALLRAHAGEHLLLGATKRSMVFKDVLLLGNDYIVPRHCPELAEMSRVSIRILDELVLPFQELQIDDNEYAYLKAIIFFDPDAKGLSDPGKIKRLRSQVQVSLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFIKLFGMAKIDNLLQEMLLGGSPSDAPHAHHPLHPHLMQEHMGTNVIVANTMPTHLSNGQMSTPETPQPSPPGGSGSEPYKLLPGAVATIVKPLSAIPQPTITKQEVI
Protein: Complement decay-accelerating factor (CD antigen CD55) (P08174)
Organism: Homo sapiens (Human)
Function: This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Inhibits complement activation by destabilizing and preventing the formation of C3 and C5 convertases, which prevents complement damage.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Lipid-anchor, GPI-anchor.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:16503113}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000269|PubMed:16503113}.; SUBCELLULAR LOCATION: [Isoform 5]: Secreted {ECO:0000269|PubMed:16503113}.; SUBCELLULAR LOCATION: [Isoform 6]: Cell membrane {ECO:0000305|PubMed:16503113}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:16503113}.; SUBCELLULAR LOCATION: [Isoform 7]: Cell membrane {ECO:0000305|PubMed:16503113}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:16503113}.
Interaction partners:
- Complement C3
- Adhesion G protein-coupled receptor E5
- Adhesion G protein-coupled receptor E2
- Complement C4-A
- Complement C4-B
- CD59 glycoprotein
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Complement C2
- Intercellular adhesion molecule 1
- Coxsackievirus and adenovirus receptor
Sequence:
MTVARPSVPAALPLLGELPRLLLLVLLCLPAVWGDCGLPPDVPNAQPALEGRTSFPEDTVITYKCEESFVKIPGEKDSVICLKGSQWSDIEEFCNRSCEVPTRLNSASLKQPYITQNYFPVGTVVEYECRPGYRREPSLSPKLTCLQNLKWSTAVEFCKKKSCPNPGEIRNGQIDVPGGILFGATISFSCNTGYKLFGSTSSFCLISGSSVQWSDPLPECREIYCPAPPQIDNGIIQGERDHYGYRQSVTYACNKGFTMIGEHSIYCTVNNDEGEWSGPPPECRGKSLTSKVPPTVQKPTTVNVPTTEVSPTSQKTTTKTTTPNAQATRSTPVSRTTKHFHETTPNKGSGTTSGTTRLLSGHTCFTLTGLLGTLVTMGLLT
Protein: Defective in cullin neddylation protein AAR3 (Protein ANTIAUXIN-RESISTANT 3) (Q9MBG8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May contribute 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; neddylation of cullins play an essential role in the regulation of SCF-type complexes activity (By similarity). Regulates responses to the synthetic auxin 2,4-dichlorophenoxyacetic acid (2,4-D) in roots, probably by modulating the SCF(TIR1) ubiquitin E3 ligase complex-mediated proteolysis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:17905859}.
Interaction partners:
- Putative cullin-like protein 1
- Putative cullin-like protein 2
- Cullin-like protein 3
- Cullin-2
- Cullin-1
- NEDD8-conjugating enzyme Ubc12
- NEDD8-activating enzyme E1 catalytic subunit
- Probable NEDD8-conjugating enzyme Ubc12-like
- Cullin-associated NEDD8-dissociated protein 1
- RING-box protein 1a
Sequence:
MDSSPVSARFDIFEIYRRFCAIRSGQQLCNKKPCDGEESQRFNLSKEAITQLLYLVENKFQARNSIFDELFKLMSRLDLMVDFTEFTCFYDFVFFMCRENGQKNITISRAITAWKLVLAGRFRLLNRWCDFIEKNQRHNISEDTWQQVLAFSRCVHENLEGYDSEGAWPVLIDDFVEHMYSILGPNKDTSLFCKCGDTESESCLYQEDEHHKDYRRPHTGLRNIPGLKRKTSKKNDEEEEDEDEEVLETQNSSSLLNFKRIKTSNSPRCSSKSPCSIERSLSQGFASLLSTGDKP
Protein: 2-aminoethanethiol dioxygenase (EC 1.13.11.19) (Cysteamine dioxygenase) (Q6PDY2)
Organism: Mus musculus (Mouse)
Function: Plays a vital role in regulating thiol metabolism and preserving oxygen homeostasis by oxidizing the sulfur of cysteamine and N-terminal cysteine-containing proteins to their corresponding sulfinic acids using O2 as a cosubstrate. Catalyzes the oxidation of cysteamine (2-aminoethanethiol) to hypotaurine. Catalyzes the oxidation of the regulator of G-protein signaling 5 (RGS5). Also oxidizes proteins RGS4 and interleukin-32 (IL32) (By similarity).
Interaction partners:
- Cysteine sulfinic acid decarboxylase
- Acidic amino acid decarboxylase GADL1
- Glutamate decarboxylase 2
- Glutamate decarboxylase 1
- Cysteine dioxygenase type 1
Sequence:
MPRDNMASLIQRIARQACLTFRGSSTGSEGPAPGFPENLSLLKSLLTQVRAEDLNIAPRKALPQPLPRNLPPVTYMHIYETEGFSLGVFLLKSGTCIPLHDHPGMHGMLKVLYGTVRISCMDKLDTGAGHRRPPPEQQFEPPLQPLEREAVRPGVLRSRAEYTEASGPCVLTPHRDNLHQIDAVDGPAAFLDILAPPYDPEDGRDCHYYRVVEPIRPKEASGSACDLPREVWLLETPQADDFWCEGEPYPGPKVLP
Protein: Probable NAD(P)H dehydrogenase (quinone) FQR1-like 2 (EC 1.6.5.2) (O23207)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of electrons from NADH and NADPH to reduce quinone to the hydroquinone state.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}.
Interaction partners:
- 2-phytyl-1,4-beta-naphthoquinone methyltransferase, chloroplastic
- Nitroreductase family protein
- Class I glutamine amidotransferase-like superfamily protein
Sequence:
MGKGGGCVPSKKKKPATTGDGPGIDDDNDATNAPIQIDDDQTTIDGDRTTATNTGGTTTPAITTTAAKISSPLKIFVVFYSMYGHVESLAKRMKKGVDSVEGVEATLYRVPETLSQEVVEQMKAPVKDLEIPEITAAELTAADGFLFGFPTRYGCMAAQMKAFFDSTGSLWKEQSLAGKPAGFFVSTGTQGGGQETTAWTAITQLVHHGMLFVPIGYTFGAGMFKMDSIRGGSPYGAGVFAGDGSREATETELALAEHQGNYMAAIVKRLAQP
Protein: Enteropeptidase (EC 3.4.21.9) (Enterokinase) (Serine protease 7) (Transmembrane protease serine 15) [Cleaved into: Enteropeptidase non-catalytic heavy chain; Enteropeptidase catalytic light chain] (P98072)
Organism: Bos taurus (Bovine)
Function: Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Agrin
- Mucin-1
- Thioredoxin
Sequence:
MGSKRSVPSRHRSLTTYEVMFAVLFVILVALCAGLIAVSWLSIQGSVKDAAFGKSHEARGTLKIISGATYNPHLQDKLSVDFKVLAFDIQQMIDDIFQSSNLKNEYKNSRVLQFENGSIIVIFDLLFDQWVSDKNVKEELIQGIEANKSSQLVTFHIDLNSIDITASLENFSTISPATTSEKLTTSIPLATPGNVSIECPPDSRLCADALKCIAIDLFCDGELNCPDGSDEDNKTCATACDGRFLLTGSSGSFEALHYPKPSNNTSAVCRWIIRVNQGLSIQLNFDYFNTYYADVLNIYEGMGSSKILRASLWSNNPGIIRIFSNQVTATFLIQSDESDYIGFKVTYTAFNSKELNNYEKINCNFEDGFCFWIQDLNDDNEWERTQGSTFPPSTGPTFDHTFGNESGFYISTPTGPGGRRERVGLLTLPLDPTPEQACLSFWYYMYGENVYKLSINISSDQNMEKTIFQKEGNYGQNWNYGQVTLNETVEFKVSFYGFKNQILSDIALDDISLTYGICNVSVYPEPTLVPTPPPELPTDCGGPHDLWEPNTTFTSINFPNSYPNQAFCIWNLNAQKGKNIQLHFQEFDLENIADVVEIRDGEGDDSLFLAVYTGPGPVNDVFSTTNRMTVLFITDNMLAKQGFKANFTTGYGLGIPEPCKEDNFQCKDGECIPLVNLCDGFPHCKDGSDEAHCVRLFNGTTDSSGLVQFRIQSIWHVACAENWTTQISDDVCQLLGLGTGNSSVPTFSTGGGPYVNLNTAPNGSLILTPSQQCLEDSLILLQCNYKSCGKKLVTQEVSPKIVGGSDSREGAWPWVVALYFDDQQVCGASLVSRDWLVSAAHCVYGRNMEPSKWKAVLGLHMASNLTSPQIETRLIDQIVINPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGALIYQGSTADVLQEADVPLLSNEKCQQQMPEYNITENMVCAGYEAGGVDSCQGDSGGPLMCQENNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWIQSFLH
Protein: Kinesin-like protein Klp10A (Kinesin-like protein at cytological position 10A) (Q960Z0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required during anaphase to drive sister chromatid separation to promote flux by actively depolymerizing kinetochore microtubules at their pole-associated minus ends, thereby moving chromatids through a 'poleward flux'. Involved in asymmetric cell division of sensory organ precursor (SOP) cells by playing a role in the asymmetric localization of Sara-expressing endosomes to the pIIa daughter cell but not to the pIIb cell. Klp98A targets Sara-expressing endosomes to the central spindle which is symmetrically arranged in early cell division. During late cytokinesis, central spindle asymmetry is generated by enrichment of Patronin on the pIIb side which protects microtubules from depolymerization by Klp10A while unprotected microtubules on the pIIa side are disassembled by Klp10A, leading to the asymmetric delivery of Sara-expressing endosomes to the pIIa daughter cell.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14681690, ECO:0000269|PubMed:20946984, ECO:0000269|PubMed:32965218}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:14681690, ECO:0000269|PubMed:24100293}. Chromosome, centromere {ECO:0000269|PubMed:24100293}. Note=Localizes to mitotic centrosomes, spindle poles and centromeres through metaphase (PubMed:14681690). However, the centromeric localization diminishes markedly at the onset of anaphase, leaving the majority of the protein on the spindle poles (PubMed:14681690). Concentrated around the minus ends focused at the poles (PubMed:14681690, PubMed:24100293). {ECO:0000269|PubMed:14681690, ECO:0000269|PubMed:24100293}.
Interaction partners:
- Patronin
- Centriolar coiled coil protein 110kDa, isoform B
- Kinesin-like protein Klp61F
- CLIP-associating protein
- RT07324p
- Kinesin-like protein
- Kinesin-like protein at 67A, isoform A
- Protein abnormal spindle
- Protein claret segregational
- FI21273p1
Sequence:
MDMITVGQSVKIKRTDGRVHMAVVAVINQSGKCITVEWYERGETKGKEVELDAILTLNPELMQDTVEQHAAPEPKKQATAPMNLSRNPTQSAIGGNLTSRMTMAGNMLNKIQESQSIPNPIVSSNSVNTNSNSNTTAGGGGGTTTSTTTGLQRPRYSQAATGQQQTRIASAVPNNTLPNPSAAASAGPAAQGVATAATTQGAGGASTRRSHALKEVERLKENREKRRARQAEMKEEKVALMNQDPGNPNWETAQMIREYQSTLEFVPLLDGQAVDDHQITVCVRKRPISRKEVNRKEIDVISVPRKDMLIVHEPRSKVDLTKFLENHKFRFDYAFNDTCDNAMVYKYTAKPLVKTIFEGGMATCFAYGQTGSGKTHTMGGEFNGKVQDCKNGIYAMAAKDVFVTLNMPRYRAMNLVVSASFFEIYSGKVFDLLSDKQKLRVLEDGKQQVQVVGLTEKVVDGVEEVLKLIQHGNAARTSGQTSANSNSSRSHAVFQIVLRPQGSTKIHGKFSFIDLAGNERGVDTSSADRQTRMEGAEINKSLLALKECIRALGKQSAHLPFRVSKLTQVLRDSFIGEKSKTCMIAMISPGLSSCEHTLNTLRYADRVKELVVKDIVEVCPGGDTEPIEITDDEEEEELNMVHPHSHQLHPNSHAPASQSNNQRAPASHHSGAVIHNNNNNNNKNGNAGNMDLAMLSSLSEHEMSDELIVQHQAIDDLQQTEEMVVEYHRTVNATLETFLAESKALYNLTNYVDYDQDSYCKRGESMFSQLLDIAIQCRDMMAEYRAKLAKEEMLSCSFNSPNGKR
Protein: Lysine-tRNA ligase (Q8RWI4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Retinal-binding protein
- Transmembrane protein, putative
- Uncharacterized protein
- T10F20.8 protein
- Uncharacterized protein
- At3g02555
- Protein RALF-like 28
- Putative F-box/LRR-repeat protein 9
- Uncharacterized protein
Sequence:
MAAAAMAVHLPKHSSFLPKPKLPLDKKTNFLGGSFNLGRPMSVNREFNSPVMVSASSTSKTVLTDDVDGDQSKRFYINFTGFPFPLGPFLNRRTIRTEAVKGCIWMFEQEQALGFSSVSTNIRMTVIKLKSGGLWVHAPIAPTKECVQLIKELGAPVEYIVLPTFAYEHKIFVGPFSRKFPKAQVWVAPRQWSWPLNLPLEFFGIFRAKIIKDRDLSTPWAEEIEQKVLSSPEVGIGPYVEVAFYHKRSRTLLVTDAVIFVPRKPPSSISNESLLASAKNGLAVKILSKGKDIPNDPVVDNPNTRQKGWERMVLQILFLGPSNLLEPNASFARMSQKLIVSPIVKTLVFSKVPEKVRDWIDEIARDWRFKRIIPAHFEAPINAGRSDFLAAFGFLEDLLGERYVTRPSLSLLFTSLMGKAASYFPPDDMRTLSSLDQFLVSVGAVKKTVSGRKRR
Protein: Serpin B3 (Protein T4-A) (Squamous cell carcinoma antigen 1) (SCCA-1) (P29508)
Organism: Homo sapiens (Human)
Function: May act as a papain-like cysteine protease inhibitor to modulate the host immune response against tumor cells. Also functions as an inhibitor of UV-induced apoptosis via suppression of the activity of c-Jun NH(2)-terminal kinase (JNK1).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10956412, ECO:0000269|PubMed:14970861}. Note=Seems to also be secreted in plasma by cancerous cells but at a low level.
Interaction partners:
- Serpin B4
- Cathepsin G
- Serpin B13
- Sorting nexin-27
- Protein S100-A7
- Cytohesin-interacting protein
Sequence:
MNSLSEANTKFMFDLFQQFRKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGKAATYHVDRSGNVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKIKNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKDLSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP
Protein: SWI/SNF and RSC complexes subunit ssr4 (Q9P7Y0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Chromatin structure-remodeling complex subunit rsc7
- Chromatin structure-remodeling complex subunit snf21
- Chromatin structure-remodeling complex subunit sfh1
- SWI/SNF and RSC complexes subunit ssr3
- SWI/SNF and RSC complexes subunit arp9
- Chromatin structure-remodeling complex subunit rsc9
- SWI/SNF and RSC complexes subunit ssr2
- SWI/SNF chromatin-remodeling complex subunit snf30
- Chromatin structure-remodeling complex subunit rsc58
- SWI/SNF and RSC complexes subunit ssr1
Sequence:
MAATMAAQSLLSIPVEYRSQVWCRANLPYPPAPQLPIPAVVDILTKASQALPQISFSWTLIDQPPDGSLFLVWQAPTLPSPPDGMHFMSNERFFNMDVAGKVLEIHEAKHGFYPLSETRTMHVRCRYRLLGVGFDNFWLVHYFQGSETDSIPANISVAKPPHLRRYPLPDVKTSPFLLQEPKKHIPEGTALSQRETLPNMGSAQMKSQSRTPSFSNVTTSPVPPINSNATAQTAEGHMGATNMTVDNMNKPSIPPNGNTSILMQEDLEIEKGDVMDKLSPQQICTARFIKHAEWMSQVLLTLQSVKDIEPPALWQEPNSMEELGKELKDNKEQLVKQDQKYQSLQGDLSYTDSMSNLLKEFSNIKSAEECDVLQKKIEEFAEAKIVPLSHVTERS
Protein: Secreted Ly-6/uPAR domain-containing protein 2 (SLURP-2) (P0DP59)
Organism: Mus musculus (Mouse)
Function: Binds and may modulate the functional properties of nicotinic and muscarinic acetylcholine receptors. May regulate keratinocytes proliferation, differentiation and apoptosis. In vitro moderately inhibits ACh-evoked currents of alpha-3:beta-2-containing nAChRs, strongly these of alpha-4:beta-2-containing nAChRs, modulates alpha-7-containing nAChRs, and inhibits nicotine-induced signaling probably implicating alpha-3:beta-4-containing nAChRs. Proposed to act on alpha-3:beta-2 and alpha-7 nAChRs in an orthosteric, and on mAChRs, such as CHRM1 and CHRM3, in an allosteric manner.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0DP57}.
Interaction partners:
- Secreted Ly-6/uPAR-related protein 1
- Neuronal acetylcholine receptor subunit alpha-9
- Neuronal acetylcholine receptor subunit alpha-3
Sequence:
MRLPFWFLLAVVLSMELAVTQGLQCHLCKGFGGCSRPSSCPWSSTHCVIIATRSPISFTDLPLVTKMCYSGCPDVSSLGLGPHVSIACCQSNLCNRD