wanglab/gogpt-training-data huggingface dataset:
Protein: Non-specific lipid-transfer protein-like 2 (NSL-TP2) (EC 2.3.1.176) (3-keto-acyl-CoA thiolase) (Abnormal dauer formation protein 22) (Propanoyl-CoA C-acyltransferase) (Protein P-44) (G5EDP2)
Organism: Caenorhabditis elegans
Function: Catalyzes the thiolytic cleavage of 3-ketoacyl-CoA with 8-16 carbon residues in the acyl group using a ping-pong mechanism whereby binding to 3-ketooctanoyl-CoA results in the release of acetyl-CoA and the subsequent addition of CoA produces 3-ketohexanohyl-CoA. Involved in the biosynthesis of the dauer pheromone by providing short chains of fatty acid that are attached to the ascarylose sugars of the pheromone.
Subcellular location: Peroxisome {ECO:0000269|PubMed:19174521, ECO:0000269|PubMed:19496754}. Note=Punctate localization in the cytoplasm. {ECO:0000269|PubMed:19174521, ECO:0000269|PubMed:19496754}.
Interaction partners:
- SCP2 domain-containing protein
- MaoC-like domain-containing protein
- Acyl-coenzyme A oxidase acox-1.1
- Acyl-coenzyme A oxidase acox-3
- Acyl-coenzyme A oxidase acox-1.3
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase acox-1.2
- Acyl-coenzyme A oxidase acox-1.4
- Probable acyl-coenzyme A oxidase acox-1.5
- Non-specific lipid-transfer protein-like 1
Sequence:
MTPTKPKVYIVGVGMTKFCKPGSVPGWDYPDMVKEAVTTALDDCKMKYSDIQQATVGYLFGGTCCGQRALYEVGLTGIPIFNVNNACASGSSGLFLGKQIIESGNSDVVLCAGFERMAPGSLENLAAPIDDRALSVDKHISVMSETYGLEPAPMTAQMFGNAAKEHMEKYGSKREHYAKIAYKNHLHSVHNPKSQFTKEFSLDQVINARKIYDFMGLLECSPTSDGAAAAVLVSEKFLEKNPRLKAQAVEIVGLKLGTDEPSVFAENSNIKMIGFDMIQKLAKQLWAETKLTPNDVQVIELHDCFAPNELITYEAIGLCPVGQGHHIVDRNDNTYGGKWVINPSGGLISKGHPIGATGVAQAVELSNQLRGKCGKRQVPNCKVAMQHNIGIGGAGVVGLYRLGFPGAAQSKI
Protein: TRPA1 (Transient receptor potential cation channel subfamily A member 1a) (Q5UM15)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTKKMTHISKSEKSRQQSYDNVMDGDESNQISANVFEWTKQGNAAALEKNSRYLDTRDNIGASPLHYASANGHFRIIRHIVQIVGHQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHMAVSLGKNFVLEQLVSHKQTDVNLEGDLGNTPVILSAALDNHEALGILYKHGAKFCRQNNLGHFPIHAAAFSGAKKSMEVILLKGEEAGLSIDAHINYVDKSCSSPLHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVMLSSYPKVCDLINITDGANQTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGADLTKKDKSGCNFLHLAILQPRGLKNLPTEVLQHESVRELLNDEDIEGCTPLHYACRLGIPDSVKNMLGLEVSLDQKSKEKKSALHFAAEFGRINTCHRLLEMVTDTRLLNEGDEKGLTPLHLASREGHVKVVELLLRKGALFHSDYRGWSGLHHAASEGYTQTMDTLLTSNIKLLNKTDGDGNTALHLAARAGHVAAVRLLLYRGAKIILNKNDASFLHEAVHNARREVTNMVIESDRCEEAMTTYKPNSTKRCIVMDMIEFLPESFKHLLDTCIRESEEDVNCTNYYIEYNFRWLQHPLQNLKKTGMEKDMAYKPLSALNAMVNFNRVNLLTHPVCKKYLEMKWSAYGIKAHLLNMTVYALGVFPLTYLIVNLKPTLVTSRNVTSVNMVCTSLYKQSYLTTSSMLLVLAMNMYAVGKEILQMFQQRLNYLRDLSNYMDWAAAICALLFVVPLLMNLKSSWHWQAGALAALTSWLNLLLYLQRFERIGIYVVMFREISRTLLSIIVLFFYLILGFALSFYALMIEQQHFGRMFLSLLQTFVMMVGEMNYQDNFMKPYLQGDLPFPDLTLAIFVWFVLLVPILLMNLLIGLAVGDIAEVQTNACLKRIAMQIELHTNLEERLPYWFMKRVDQVTIREYPNRCFSGKKRWFFGGNEVKSRTRLGPTFHQLTPLERELTKQKYRLKEISETMEKQHNLLKLIVQKMEISSEADEHDGPPVFQELKEKLLTKSKWGPLLRAVTARKKGICSFGKT
Protein: Acetylcholine receptor subunit alpha-type acr-15 (Nicotinic acetylcholine receptor subunit acr-15) (O16926)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P48180}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P48180}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- GLutamate Receptor family
- G-protein coupled receptors family 1 profile domain-containing protein
- Ion transport domain-containing protein
- GLutamate Receptor family
Sequence:
MLLPILLHFLLLITQLNGSPAEVRLINDLMSGYVREERPTLDSSKPVVVSLGVFLQQIINLSEKEEQLEVNAWLKFQWRDENLRWEPTAYENVTDLRHPPDALWTPDILLYNSVDSEFDSSYKVNLVNYHTGNINWMPPGIFKVSCKLDIYWFPFDEQVCYFKFGSWTYTRDKIQLEKGDFDFSEFIPNGEWIIIDYRTNITVKQYECCPEQYEDITFTLHLRRRTLYYSFNLIAPVLLTMILVILGFTVSPETCEKVGLQISVSLAICIFLTIMSELTPQTSEAVPLLGVFFHTCNFISVLATSFTVYVQSFHFRNQHVHERMDFWMRFILLEWSPWLLRMKMPDRENNFQTLTESWKGRNRRESMARTAFEYADGPVTQIHSMGIMLKDNFEELIYQVKQEKIADEKGIERLRVLQKIYDHVKMIREHDDDNDEDSRVALEWRFAAIVVDRLCLLAFSLLIVVVSIIIALRAPYLFA
Protein: Nesprin (Q71JA7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
Sequence:
MQLPKQEKKSKKDKKKKQKNVPEVEQQLPEDQQISVTVEIAPELLSESGIVVSTNQQIEDVPHVTPVVDTPIESEEVETPKAQRVQLQITKTTVYDEYPDLPVHITEQNKVLIASQQSKRSGAGPTSSAVTIEEVGSPTEELVVPITPGPDNLSGEPHNIWFSATTSVDKTPIELSQALIMSESLQHYPGQQKLTQEPILISTKEAIGDRIKQLKQASPQQATPLSNVLHLATLSEQIKELPTEQRILEVNEGLKDLDVAIKNGDKTVIQTTVITVIEKVSTWLETIEYRVYLIRQNSNEGPSEEKLDNYNQLNDELSTIKQNVVQLERQLSKAEPEPQLLQCVDSLKEHVDAVEQVTQQNQVQDSNDLDKWHNFEVLLYNVSSVLADLQQSYDLLINQEYPLSAKLAQLDELEQQHEAAQQQLAHLCQNARAFQRDFPGKKMPQDVHNAFETSKNIANNIQAERERVLQLQSLAEEYEQTLKEFTKITVLADKLVESPIVSSSLEQLNNEVQKQRKFFVNLSHCRAMLESLEENIDSETREKHSELHKELYNRATSLLDKASERSSKLVQAASRWTVLEKGMRDELQWLQVAQQRVPDLSAVTSADYDQYTTLYQSLSNDISHHYVKMTQLSGIANKLQLLVQAPNLVEETNEALIVLLKLREEVALYLHRLLVFKEIWVQYEQQTDKLEAFVREAEQELRNIQIPSQPTHQPIEHMRQFWEIKARFELHNNVRTDTGLSFEKSLQVIPLADEMLQRQFHAQLEDRWQAVAQAIELIQHNIVECLSSEDVPADEKLKMVERELQEIYLTMTSMKGVIKNEEELCLYIERVQVLRTRVGFIGNELGRIGLQEPAIEPEKVGELFSLSHKISTQIAEELEGASVLRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEELVISWQEIMRIRQMLHTLPMRLKMSVSPVKLERDISQLQDDHAFLESKCTNIMAILRSRLAVWLRYERQLELVHGSVQETDFMMELIRVHGQVDYERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIESCDVQIVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELWDKYRNASAAVKNSIDQQMDAVKSLEQPLDALQHAKVCQDNLTTQNDRILELRDIVAKIAADVGLDASALMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQNLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISPHDMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELLTLYSEPEVRSQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRAWLFEVESQLDKPLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWRTQVNTSGLAASAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLRQLEQIYAKLAMSAGVEPENIQKLTLPTKVMVSMWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNAIQKALEQLPSAENQQTSKAEPKAVLQRLESLEKKLQDAQQHVQQADNLAQEAKTRTKQQPQLKQLLELVSAYTTLWQTVQTRIVTLKTTWLTRAAQAAASLPVSEAANAAVQVNTLSQRKLRQAQQMQRETSITAKDAYIMELQTAITECQNNLDELQRTVVDKTRKPGPQKIAKLLGNAQSSTELVKHLSHLLLTECKADDQAAEVDTVAELTLRFDTLQSQWKARQQHDQNASEVGRLTCPLCTQRNWQQIDNDLWRLEQWLQFAESTQKAQSAPPSNIELLEDVTQDHREFLLDLESHKSIISSLNVVGDHLATHTLDTEKARQLRSRLEADNERWNNVCINATKWQGLLQTALMGNSEFHQTIGELVEWLQRTEQNIKASEPVDLTEERSVLETKFKKFKDLRAELERCQPRVVSLQDAADQLLRSVEGSEQQSQHTYERTLSRLTDLRLRLQSLRRLSGIYIVKLGAVLGYEGDNLGVPLHMLSSELLDNTTLSTSSMQAAAPNTENANNTDGGDAVDGDVINTTVLARGARFLGRVARASLPIQALMLLLLGVATLVPHGEDYTCMFSNTFARSLEPMLSYPHGPPPT
Protein: tRNA dimethylallyltransferase (EC 2.5.1.75) (Isopentenyl-diphosphate:tRNA isopentenyltransferase) (IPP transferase) (IPPT) (tRNA isopentenyltransferase) (IPTase) (Q80UN9)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 of both cytosolic and mitochondrial tRNAs, leading to the formation of N6-(dimethylallyl)adenosine (i6A37). Mediates modification of a limited subset of tRNAs: tRNA(Ser)(AGA), tRNA(Ser)(CGA), tRNA(Ser)(UGA), as well as partial modification of the selenocysteine tRNA(Ser)(UCA) (By similarity). TRIT1 is therefore required for selenoprotein expression.
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000250|UniProtKB:Q9H3H1}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- Leukotriene A-4 hydrolase
- Mitochondrial tRNA methylthiotransferase CDK5RAP1
- Mitochondrial tRNA-specific 2-thiouridylase 1
- tRNA
- tRNA
- Putative GTP-binding protein 6
- rRNA methyltransferase 2, mitochondrial
- tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
- Methionyl-tRNA formyltransferase, mitochondrial
- Threonylcarbamoyl-AMP synthase
Sequence:
MAAAAAARAVPVSSGFRGLRRTLPLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQKMCQHHMISFVDPLVTSYTVVDFRNKATALIEDIFARDKIPIVVGGTNYYIESLLWKVLITTKPQEMGTGKVVDRKVELEKEDGHELHKRLSQVDPEMAAKLHPHDKRKVARSLQVFEETGISHSEFLHRQHAEEGGGPLGGPLRFPNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELRGFHRRYNLKNISENSQDYQHGIFQSIGFKEFHEYLTTEGKCTPETSNQLLKKGIEALKQVTKRYARKQNRWVKNRFLSRPGPSVPPVYGLEVSDVSKWEESVLEPALNIVQSFIQGHKPTAMPVKMAYNESENKRSYHMCDLCDRIIIGDREWAAHLKSKSHLHQLKKRRRLDLDAVSATGSQSNSPDCDPERIEGESSGQHNQELKASV
Protein: Methylmalonyl-CoA mutase small subunit (EC 5.4.99.2) (A0A045IZR3)
Organism: Mycobacterium tuberculosis
Interaction partners:
Sequence:
MSIDVPERADLEQVRGRWRNAVAGVLSKSNRTDSAQLGDHPERLLDTQTADGFAIRALYTAFDELPEPPLPGQWPFVRGGDPLRDVHSGWKVAEAFPANGATADTNAAVLAALGEGVSALLIRVGESGVAPDRLTALLSGVYLNLAPVILDAGADYRPACDVMLALVAQLDPGQRDTLSIDLGADPLTASLRDRPAPPIEEVVAVASRAAGERGLRAITVDGPAFHNLGATAATELAATVAAAVAYLRVLTESGLVVSDALRQISFRLAADDDQFMTLAKMRALRQLWARVAEVVGDPGGGAAVVHAETSLPMMTQRDPWVNMLRCTLAAFGAGVGGADTVLVHPFDVAIPGGFPGTAAGFARRIARNTQLLLLEESHVGRVLDPAGGSWFVEELTDRLARRAWQRFQAIEARGGFVEAHDFLAGQIAECAARRADDIAHRRLAITGVNEYPNLGEPALPPGDPTSPVRRYAAGFEALRDRSDHHLARTGARPRVLLLPLGPLAEHNIRTTFATNLLASGGIEAIDPGTVDAGTVGNAVADAGSPSVAVICGTDARYRDEVADIVQAARAAGVSRVYLAGPEKALGDAAHRPDEFLTAKINVVQALSNLLTRLGA
Protein: RING finger protein Z (Protein Z) (Zinc-binding protein) (Q6UY77)
Organism: Machupo virus (MACV)
Subcellular location: Virion {ECO:0000256|HAMAP-Rule:MF_04087, ECO:0000256|PIRNR:PIRNR004030}. Host cytoplasm, host perinuclear region {ECO:0000256|HAMAP-Rule:MF_04087, ECO:0000256|PIRNR:PIRNR004030}. Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04087, ECO:0000256|PIRNR:PIRNR004030}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000256|HAMAP-Rule:MF_04087, ECO:0000256|PIRNR:PIRNR004030}.
Interaction partners:
Sequence:
MGNCNKPPKRPPNTQTSSNQPSAEFRRTAPPSLYGRYNCKCCWFADTNLITCNDHYLCLRCHQTMLRNSELCHICWKPLPTSITVPVEPSAPPP
Protein: Pantothenate kinase subunit, putative (EC 2.7.1.33) (Q384T6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA/pantothenate metabolism flavoprotein C-terminal domain-containing protein
- Flavoprotein domain-containing protein
Sequence:
MISSSQGGPKPRGGAKRGVAELRGIAVATATNAQLRVLSYNFNILPRGCGGFQRERISSFLETVDQYDVIMLQEVYAASVLPYFLQNRMCFQKMLVDELVLRGFQHYAISKQPSYTTMLRNNVFSDNGLIIASRFPIGQRGSYTFRSHERAVQSVRRGCLFAEVKVPLTSGGEESIIFFNVHLRQEDSDDVTSEHVKETRQFAASVIRNMCSNPEDVAQIPFVLAGDFDVNGINLHNVGQPTKKYEDLLGELQALGSGVREAVFDAQHRHPPTRPTELFFPTQSKLVRNSFSPQRQDYFFVSHTVAVKNPDIHKFVSDSQQPYTYLSDHFGVSAVLAIPQTSKQRHKRWMPLTESNAPESEETVNEHSNPIFSIIVEIIVLCTVSWAAFCFSWVALLFSLLVGVLVWYCLSPIHELRSERKFTRVGNSNAHGGEGCVSDLPREYESLKHANSVGEMWRRAVSLHSAQRCLGQKNDAGVPEWLTFVSVDARAQELASGLAALGVGPGDVIGVDCDASVDSTVLELACATYGIATLALVGKGSTIRNLIDEYDIKVVFAARNAVGAILTCRSRSLETLVCMHSSHDSTDCMVARDVCITLISYNEVFSKGRSQPVLLRPVCDDTTLYTMVVDPSTSNGNLKVVRVTHADALRAIRTLVGTAVLPNTQHKHLLVHYTPFAMLFNRLFVLGLFAHGSAVATTPVAACARAFATIQPTIVVATPSLFSTSAVQLRRRNERYWPIFSWIFEQIYHLRLFLINTHNRDSLILRTIFFRGTQHLFGGNVEKIVVCSSEESLSDTLAEHIVVCYTPCLREVFFLPSEGVFCVDGVPAPNIHVHLEPFDEPSKEAKIGSLVLSCEGRKERTLPIAAMWTGTRTLRLIGPPDGVLLPVRSEYVLAASLERVFSQSRYVNDVFLYAEPSRPIIAIISPNRDTVDFEWRQSREGEVAGEDNLLSNWAKFASFASDLLTADFQVIAKRNALHESNVPSYVHIHPHAFKKHDSFLTPYGGIRRNSLKSYFKVVIEGFYNDATPTALPTPGQIIESDEEGQAYERDQKPFSLNTPISIDVGGTFAKLVYVQPPGDFKVPHYVVKEAAVLAEGFNVRMLDLLDNAEGMKRLLNDDPFSTVGTLQFAKMSSKCIPDFMSYIVESQMLSYYTKEYRNTLRVTGGGAFKYAALAKKMDLNFSVMREMSAVVHGLGVVIGRAPETIFTVDPATGERHPHRLKSPPGEPFSPYPCLLVNIGSGISIIKCLGPDGSHVRIGGSPMGGATFWGLVRTMTAVTSWEEITETMRLDGPGDNRNVDLLVGDIYGYNAKDLPPMLSVDTVASTFGKLGTERFYESQGNVDRLYASSSEDLSGAVSSSPDSNPTLHDAVAPTLASHGKTSEIDIVRSLLNMISSNVTQLAYLHSRVQDVHNIFFAGGFVRNNPIVWSHISSFMAYWSKGECHAHFLGHDSHLGALGAATNTEEHVS
Protein: Secreted protein A (Protein gp17) (O77257)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Secreted {ECO:0000269|PubMed:27187592, ECO:0000269|PubMed:27340834}. Extracellular vesicle {ECO:0000269|PubMed:27187592}. Note=Most abundant protein present in secreted pycnosomes, which consist of membranous materials that are continuously secreted (PubMed:27187592). Also found in multilamellar bodies, which consist of structures of lysosomal origin composed of multiple concentric membrane layers (PubMed:27340834). {ECO:0000269|PubMed:27187592, ECO:0000269|PubMed:27340834}.
Interaction partners:
- Secreted protein D
- PhoPQ-activated pathogenicity-related protein
- Ponticulin-like protein C1
- Ponticulin-like protein C3
- CMP/dCMP-type deaminase domain-containing protein
- Ponticulin-like protein C4
- Ponticulin-like protein C2
- Ponticulin-like protein C5
- DNA helicase
- SAC domain-containing protein
Sequence:
MRLLITLFAIFALFNCSLANTATNVGEFLIGFAQGVEITLNSNSQACLSGVTSTFDEFQTAFQLIDSGFKSKSINQVKTGITDLGLAIQQVPVDYDACGITQFVEEIEEIASKLSSGVDGIVDVILKEAVEIWEHKNDLSADFKTAIADWKSSNYNGSGVAVGSIIGDLIQGAK
Protein: Uncharacterized protein (Q57WY1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNSEEGRHHTLSSFLASTLESHVRSIRQEALTVCINHAQCELLSRRLQQVYNTLRKLPNGAPTPQLLTVFASADMLVQRMRHGGWLLLLERHLTCRALFAALFERIPCVWQLQMTDSWLGEDLLAVRADEQVDARVYLEKLGGWADVESRMDRARGSFDSSSGEESDTGETRGGAPPDALTEQDVIDMFRRQTLSRWRVPLEDLTPPGEDVPPPPYADSELHVFSLYNGYRYGKTPVLLYQLEQTAKRTIPPTTVTNFVQDMVARARWCHPNLVPFTGAFTEKVPFLCQPDDDNDCDPDVDTSSQFSGENSSRSQSANGCGATEEDVTAADDGGVDPSSAPVLDLGYMIEDMKYLKAELLNEESPYLTSYVVREVDNYIGNETFKTLHEVLFVERRPFTVREAIAITLQVADALQYILMEEGNMPEEVLDAWTVVSPSNIYVCPITVPRRSQHECCHEPGEFGGSAWPTCDDGYGDIQEEYDHDMVAPPFCGSSVQQRRCVELFAPGGWAAMYNPPVYVDGGPYSRWRPHPHASCRPTYAMAQLLLALVNNEPPYRLLTKQEELARHVFEADNMNDDDNVSVSVRVSIPVGSIVPRRLPVALRKLCSHAMHLRDPHRRGEAWDGLSLSDFRNQLWESYISLSNSMDTAGMLPGMDDDAQATVVPVGERVEMGFSRESSVTRERAPGPTLDDYGEFPSRES
Protein: Keratin-associated protein 1-4 (High sulfur keratin-associated protein 1.4) (Keratin-associated protein 1.4) (P0C5Y4)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 27-1
Sequence:
MASCSTSGTCGSSCCQPSCCETSCCQPSCCQTSSCGTGCGIGGGIGYGQEGSGGSVSTRIRWCHPDCHVEGTCLPPCYLVSCTPPSCCQLHHAEASCCRPSYCGQSCCRPACCCHCCEPTC
Protein: Ferredoxin-1 (Ferredoxin I) (P27320)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Interaction partners:
- Photosystem I reaction center subunit II
- Photosystem I reaction center subunit IV
- Ferredoxin-thioredoxin reductase, variable chain
- Ferredoxin-thioredoxin reductase, catalytic chain
- Ferredoxin--NADP reductase
- Photosystem I iron-sulfur center
- Hydrogenase subunit
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I reaction center subunit III
- Photosystem I reaction center subunit XI
Sequence:
MASYTVKLITPDGESSIECSDDTYILDAAEEAGLDLPYSCRAGACSTCAGKITAGSVDQSDQSFLDDDQIEAGYVLTCVAYPTSDCTIETHKEEDLY
Protein: Epsin-2 (Q05785)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein. Note=Localizes in a punctate pattern. Found in the actin cortical patches, although the majority is located at the cell periphery.
Interaction partners:
- Actin cytoskeleton-regulatory complex protein PAN1
- Clathrin heavy chain
- EH domain-containing and endocytosis protein 1
- Protein SLA2
- Clathrin coat assembly protein AP180B
- Actin cytoskeleton-regulatory complex protein END3
- Clathrin coat assembly protein AP180A
- AP-2 complex subunit alpha
- Epsin-1
- Clathrin light chain
Sequence:
MSKQFVRSAKNMMKGYSSTQVLVRDATANDSRTPSIDTLDDLAQRSYDSVDFFEIMDMLDKRLNDKGKYWRHVAKSLTVLDYLVRFGSENCVLWCRENFYVIKTLREFRHENESGFDEGQIIRVKAKELVSLLNDEERLREERSMNTRNRRANRAARPRPRRQRTRSNPHDSSPSYQDDLEKALEESRITAQEDEQRRRELAQYDDEDPDFQAALQLSKEEEELKQLQELQRLQKQQQSLSQFQAPLQQQQPQQQPAYYDIFGNPISQDEYLQYQYQQDQEQAMAQQRWLDQQQEQQQLAEQQYFQQQQQAAAAASALQQQQTAANMQQQQQQPADFQQPLPTGSNNPFSMDNLERQKQEQQHAQLQRQQEEARQQQEQLKLQQLQRQQQEEAQLHQKRQEEAQLQQQQAQLLQQQAQFQQQQPLKQTRTGNQSISDKYSDLNTLLATGTGIDTFGNTGEARIPAQHTKTGTFINSQGTGYKQVTNEPKNNPFLSNQYTGLPSTNIVPTQTGYGFGNQPQSPPTNSPQQNPTGISYSQPQQQQQPQQQPQYMQNFQQQQPQYAQNFQQQPQYTQNYQQQPQYIQPHQQQQQQQQQQQQQQGYTPDQGVSLIDL
Protein: Oxoglutarate dehydrogenase inhibitor (Q8NQJ3)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: An essential component of the PknG signaling pathway. When unphosphorylated, it inhibits the activity of 2-oxoglutarate dehydrogenase. When phosphorylated it does not inhibit 2-oxoglutarate dehydrogenase.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Probable serine/threonine-protein kinase PknB
- 2-oxoglutarate dehydrogenase E1/E2 component
- Serine/threonine-protein kinases PknA
- non-specific serine/threonine protein kinase
- Protein serine/threonine phosphatases
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Predicted transcriptional regulators
- FHA domain-containing protein
- FHA-domain-containing proteins
Sequence:
MSDNNGTPEPQVETTSVFRADLLKEMESSTGTAPASTGAENLPAGSALLVVKRGPNAGARFLLDQPTTTAGRHPESDIFLDDVTVSRRHAEFRINEGEFEVVDVGSLNGTYVNREPRNAQVMQTGDEIQIGKFRLVFLAGPAE
Protein: Chondrolectin (Transmembrane protein MT75) (Q9CXM0)
Organism: Mus musculus (Mouse)
Function: May play a role in the development of the nervous system such as in neurite outgrowth and elongation. May be involved in motor axon growth and guidance (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MIRIASLLLGAALLCAQGAFARRVVSGQKVCFADVKHPCYKMAYFHELSSRVSFQEARLACESEGGVLLSLENEAEQKLIESMLQNLTKPGTGISDGDFWIGLLRSGDGQTSGACPDLYQWSDGSSSQFRNWYTDEPSCGSEKCVVMYHQPTANPGLGGPYLYQWNDDRCNMKHNYICKYEPEIHPTEPAEKPYLTNQPEETHENVVVTEAGIIPNLIYVIIPTIPLLLLILVALGTCCFQMLHKSKGRSKTSPNQSTLWISKSTRKESGMEV
Protein: Myosin regulatory light chain 10 (Myosin light chain 2, lymphocyte-specific) (Precursor lymphocyte-specific regulatory light chain) (Q62082)
Organism: Mus musculus (Mouse)
Interaction partners:
- Rho-associated protein kinase 1
- Rho-associated protein kinase 2
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- Myosin-9
- Myosin-10
- Myosin light chain kinase 3
- Myosin light chain kinase 2, skeletal/cardiac muscle
- Myosin-11
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Sequence:
MGQSSLDHGVQGPVAGTGDFGPLKEATATGFISCAQAPRRARKRVEGTASSNVFSMFDQSQIQEFKEAFTIMDQNRDGFIDKEDLRDTFAALGRINVKNEELEAMVKEAPGPINFTVFLTMFGEKLKGTDPEETILHAFKVFDTEGKGFVKADFIKEKLMTQADRFSEEEVKQMFAAFPPDVCGNLDYRNLCYVITHGEEKD
Protein: Ankyrin repeat domain-containing protein 46 (Ankyrin repeat small protein) (ANK-S) (Q86W74)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Pregnancy-specific beta-1-glycoprotein 3
- E3 ubiquitin-protein ligase MGRN1
- Attractin
Sequence:
MSYVFVNDSSQTNVPLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHLCGHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGVNKDVIRLLESLEEQEVKGFNRGTHSKLETMQTAESESAMESHSLLNPNLQQGEGVLSSFRTTWQEFVEDLGFWRVLLLIFVIALLSLGIAYYVSGVLPFVENQPELVH
Protein: (+)-3-carene synthase 1, chloroplastic (EC 4.2.3.107) (Terpene synthase (+)3car1) (PbTPS-(+)3car1) (Terpinolene synthase (+)3car1, chloroplastic) (EC 4.2.3.113) (R9QMW4)
Organism: Pinus banksiana (Jack pine) (Pinus divaricata)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (+)-3-carene and, to a lower extent, to terpinolene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSLISAVPLASSCVSKSLISSVREHKALRRAIATLQMSRPGKSVAASTRMSSATAGCDDGVKRRIGDYHSNLWDDNFIQSLSSPYGASSYGDHADRLIGEVKEIFNSFSIADGELTSPVSDLLQQLWMVDNVERLGIDRHFQTEIKVALDNVYRYWSEKGIGCGRDSASTDLNTTALGFRIFRLHGYTVSSDAFEHFKDQMGQFTASANDTELQTRSVFNLFRASLIAFPEEKVLEEAEKFAAAYLKAALQTLPVSGLSREIKYVFDYRWHSNLPRLEARSYIDILADNTISGTPDANTKKLLELAKLEFNIFHSLQQKELQCLWRWWKEWGCPELTFIRHRYVEFYTLVSGIDMVPEHATFRLSFVKTCHLITILDDMYDTFGTIDELRLFTAAVKRWDPSATECLPEYMKGVYMVLYETVNEMAKEAQKSQGRDTLGYVRQALEDYIGSYLKEAEWIATGYVPTFQEYFENGKLSSGHRIATLQPILTLSIPFPHHILQEIDFPSKFNDYACSILRLRGDTRCYKADSARGEEASCTSCYMKENLGSTQEDALNHINGMIEDLIKKLNWEFLRPDNNAPISSKKHAFNISRGLHHFYNYRDGYSVASNETKDLVIKTVLEPVLM
Protein: Inositol 3-kinase (EC 2.7.1.64) (Myo-inositol kinase) (AtMIK) (Q93Z01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Kinase that phosphorylates myo-inositol to produce multiple myo-inositol monophosphates. Participates in phytic acid biosynthesis in developing seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds.
Interaction partners:
- Protein MALE DISCOVERER 1
- Inositol-phosphate phosphatase
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- Probable inositol 3-phosphate synthase isozyme 3
- Inositol-3-phosphate synthase isozyme 2
- Bifunctional phosphatase IMPL2, chloroplastic
- Inositol-3-phosphate synthase isozyme 1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Phosphatase IMPL1, chloroplastic
- Inositol oxygenase 5
Sequence:
MTLNPPPSQQTSHSPRRIPNRRVLIVGNYCHDVLIQNGSVVAETLGGAASFISNVLDSSSVSCDLVSKVGHDFRYEVTHSPIVAPEKETTVFEAYFDLGIDGIGHADRVLKRVSACDPILPSDIPDSRFDFGMAVGVGGEILPETLEKMVEICDVVAVDIQALIRVFDPVDGAVKLVDLKESGFYHILHRIGFLKASSDEALFMDVEQMKHLCCVVVTNGEKGCRIYHKDDEMTVPPFLAKQVDPTGAGDSFLGGLIVGLVEGLTVPDAALLGNLFGSITVEHIGQPKFDLMMLQKVKDEVQRRKKQCNISSSHNNDHNEFHERLSPARFSCVDSQLQPKLLVNGHSCDDRSL
Protein: Putative serine/threonine-protein phosphatase C22H10.04 (EC 3.1.3.16) (Q10298)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Factor arrest protein 11
- Uncharacterized WD repeat-containing protein C1773.01
- Uncharacterized protein C3H7.13
- Uncharacterized protein C2C4.10c
- Protein phosphatase PP2A regulatory subunit A
- Uncharacterized protein C216.01c
- Uncharacterized protein C63.05
- Serine/threonine-protein kinase plo1
Sequence:
MIDLDNIIERLYEKQLIAESVIAYLCSLAKEVLMQESNVVRLSTPITVVGDIHGQFDDLLEIFRIGGPCPYTNYLFLGDYVDRGYYSIETITLLICLKLRYPKRITLLRGNHESRGITQTYGFYSECLRKYGNANVWKYFTDIFDFLTLSATIDDTIFCVHGGLSPSIQHIDQILVLDRFREFPHEGPMADLVWSDPDPSVQEFSLSPRGAGFSFGEVIVTKFLEYNNMKHILRAHQLCSEGYQILFEKKLSTVWSAPNYCYRCANLASILQIDTDQSRFFNVFDAAPNQETPFVEPAAKVTAEYFL
Protein: Paxillin (Q9BPQ9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSSKLISSSFHSSPLSDCFKVGEFERRLDALLADLQNSVPGQPQQPQPQYGTVQPKHQALQQQQFVDNTPGYGSLRSKAQPQVYQEHYSVETRSPTAGHDFNGSSTTPGYANQGSLPRQAAGASTGLSELDSLLQDLQKIDVPVNYSTPVSKYNTMNSYATVEERPSVDSLLNELDNAHIYAVPNGSAHKSPTPGRHVTITVRETKTEKLTGPDGPVGTVEEQIVQQKDSYTPNHAVPGQQVHQAYTSQATKELDDLMASLSDFKVSNGTNGIGNGSHPQQHSSTVQHQTVTDYARPNKGSQQAHLTQTIEETTIVEDSREDQLDSMLGNLQANMSRQGVNTVQKGCCNACEKPIVGQVITALGKTWHPEHFTCNHCSQELGTRNFFERDGFPYCEPDYHNLFSPRCAYCNGAILDKCVTALDKTWHTEHFFCAQCGQQFGEEGFHERDGKPYCRNDYFEMFAPKCNGCNRAIMENYISALNSQWHPDCFVCRDCRQPFQGGSFFDHEGLPYCETHYHAKRGSLCAGCSKPITGRCITAMFKKFHPEHFVCAFCLKQLNKGTFKEQKDKPYCHTCFDKIFG