wanglab/gogpt-training-data huggingface dataset:
Protein: Kinesin associated protein 3, isoform F (B7Z139)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQRQQQTNKQRRRWKGGSIEPHPTDKALIVNYQLEATVFGEPNNPMIEEKKHCQKIIRLRSLNAKTDPAALAREVVEKCDLIHKSQLNDVEQIIFYLKNRKDNASNDIPDNNTHSRRSAALHTSHTRSSARSHSSVAAMTSSTGSGGGSTGASNGVSNALSAATPTADVSINNIDEYVELLYEELGERIRGSAMILQMARNPDNLEELEKNEACLSALSRVLREDWRKSLDLSTNIIYIFFCFSTYTKFHPLIVQYKIGSLCMDVIDYELRRYETMRNELDVRKQPNGSSTPHSAKASKEKLNRSTDDFLDIMNEEKPKEMEPPRRRIPELKQRPKSGNWSSFHGSMSSSLIKSQILNSSYHESLCAGGSPGGDTPAVPAEQKAQSNESLDRNDPKVKKEEIDRLNKQLKIFAKKQEQLLRVAFYLLLNMAENVKLEEKMRRKHIVKMLVKALDRQNIDLLMLVSTFLKKLSIVGDNKDEMGALNIVAKLPRLFQSTHTDLVQVTLKLVFNLSFDGGLRRKMIAAGYLPMLVMFINDEKHHGIAVKILYHMSLDDKVKGMFTQTECVQMATDAIILNLNVKVDLDLIALCINLSLNRRNAQIMVEGQRLHSLMDRAFKYQDALLMKLLRNLSQHESLQLQFIDYVGDLARILTICDDEAFIVECLGILGNLALTDLDYSQILQNFQLIPWIRQILLPCARMDDLVLDTIVYLGTCACDELCALLFCRAKVVISLIELLKAKQEDDEIVLQIIFVFQQILRHESTREYMIKETESAAYLIDLMHDKNEEIRKVCDYCLDIIAISDSEWAKRIKLEKFRNHNSQWLCMVESQQDQDNEQDYADQEDECDNDLDTYLRSEYLDNCDLYNDNADNDSNSNSNHSNNNPASPAMSTYSRPLSTYRRSQDLDDLYNMTSSSKSQGSSDNNYIFKSNKSLDADGLHEELLMA
Protein: Rho guanine nucleotide exchange factor 18 (M0QZS0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
XRMKEKYGVFCSGHNEAVSHYKLLLQQNKKFQNLIKKIGNFSIVRRLGVQECILLVTQRITKYPVLVERIIQNTEAGTEDYEDLTQALNLIKDIISQVDAKVSECEKGQRLREIAGKMDLKSSSKLKNGLTFRKEDMLQRQLHLEGMLCWKTTSGRLKDILAILLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLQGPEMYEIYTSSKEDRNAWMAHIQRAVESCPDEEEGPFSLPEEERKVVEARATRLRDFQERLSMKDQLIAQSLLEKQQIYLEMAEMGGLEDLPQPRGLFRGGDPSETLQGELILKSAMSEIEGIQSLICRQLGSANGQAEDGGSSTGPPRRAETFAGYDCTNSPTKNGSFKKKVSSTDPRPRDWRGPPNSPDLKLSDSDIPGSSEESPQVVEAPGTESDPRLPTVLESELVQRIQTLSQLLLNLQDSYVETQRAAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAALEKLQSQLRHEQQRWERERQWQHQELERAGARLQEREGEARQLRERLEQERAELERQRQAYQHDLERLREAQRAVERERERLELLRRLKKQNTAPGALPPDTLAEAQPPSHPPSFNGEGLEGPRVSMLPSGVGPEYAERPEVARRDSAPTENRLAKSDVPIQLLSATNQFQRQAAVQQQIPTKLAASTKGGKDKGGKSRGSQRWESSASFDLKQQLLLNKLMGKDESTSRNRRSLSPILPGRHSPAPPPDPGFPAPSPPPADSPSEGFSLKAGGTALLPGPPAPSPLPATPLSAKEDASKEDVIFF
Protein: Glutathione S-transferase omega-like 1 (EC 2.5.1.18) (Glutathione-dependent dehydroascorbate reductase) (EC 1.8.5.1) (P48239)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB).
Subcellular location: Peroxisome {ECO:0000269|PubMed:16936141}.
Interaction partners:
- Ubiquitin-activating enzyme E1 1
- Glutathione S-transferase 2
- Glutathione S-transferase 1
- Peroxisomal targeting signal receptor 9
Sequence:
MSVSYKGTISKTHSVFKPEKGRYYIYGALGCPFTHRAILARSLKKLEPVLGLVLSHWQLDSKGARFLPAPHRPEKYKERFFTATGGIASAKLDESEELGDVNNDSARLFVDGAFDPVENISRLSELYYLNDPKYPGTKFTVPVLWDSKTRKIVNNESGDIIRILNSGVFDEFIQSEETNVIDLVPHDLIDEIDKNIKWVHPKINLGVYKVGLAENGKIYETEVKTLFENLQKMECVLKENYKRLEEQFSGNKQKILAKYFVLGQRLTEADIRLYPSIIRFDVVYVQHFKCNLKTIRDGFPYLHLWLINLYWNYAEFRFTTDFNHIKLFYIRMEVSRNKINQFGIVPLGPKPDISRL
Protein: Armadillo repeat-containing X-linked protein 5 (Q6P1M9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVDSGTEARARGKAEAGLQDGISGPATARVNGKTQAEAVAEAELKTESVTQAKAGDGAMTRTHTVTYREAMAVTREVIKVEDTTKTRVMVETKTKPLAERSIVPQTKSKAMPMSRVSTVTKSEVKVVAVIEANIRSYAKSHDKANTGSRPDRREETSIGMKSSDEDEENICSWFWTGEEPSVGSWFWPEEETSLQVYKPLPKIQEKPKPTHKPTLTIKQKVIAWSRARYIVLVPVEGGEQSLPPEGNWTLVETLIETPLGIRPLTKIPPYHGPYYQTLAEIKKQIRQREKYGPNPKACHCKSRGFSLEPKEFDKLVALLKLTKDPFIHEIATMIMGISPAYPFTQDIIHDVGITVMIENLVNNPNVKEHPGALSMVDDSSESSEEPKSGESYIHQVCKGIISCPLNSPVQLAGLKLLGHLSIKFEDHYVITSYIPDFLTLLNKGSVKTKFYVLKVFSCLSKNHANTRELISAKVLSSLVAPFNKNESKANILNIIEIFENINFQFKTKAKLFTKEKFTKSELISIFQEAKQFGQKLQDLAEHSDPEVRDKVIRLILKL
Protein: Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Peptidase M) (P9WK19)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Interaction partners:
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL4
Sequence:
MPSRTALSPGVLSPTRPVPNWIARPEYVGKPAAQEGSEPWVQTPEVIEKMRVAGRIAAGALAEAGKAVAPGVTTDELDRIAHEYLVDNGAYPSTLGYKGFPKSCCTSLNEVICHGIPDSTVITDGDIVNIDVTAYIGGVHGDTNATFPAGDVADEHRLLVDRTREATMRAINTVKPGRALSVIGRVIESYANRFGYNVVRDFTGHGIGTTFHNGLVVLHYDQPAVETIMQPGMTFTIEPMINLGALDYEIWDDGWTVVTKDRKWTAQFEHTLLVTDTGVEILTCL
Protein: U3 small nucleolar ribonucleoprotein protein imp4 (U3 snoRNP protein imp4) (O13823)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the U3 small nucleolar ribonucleoprotein. Required for the early cleavages at sites A0, A1 and A2 during 18S ribosomal pre-RNA processing (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- U3 small nucleolar ribonucleoprotein protein imp3
- Uncharacterized protein C1604.06c
- U3 small nucleolar ribonucleoprotein protein mpp10
- U3 small nucleolar RNA-associated protein 4
- Uncharacterized WD repeat-containing protein C2E1P5.05
- Probable U3 small nucleolar RNA-associated protein 13
- U3 small nucleolar RNA-associated protein 21 homolog
- Uncharacterized protein C3B8.09
- Nucleolar protein 58
- KRR1 small subunit processome component homolog
Sequence:
MLRRAVRERRQFIYKRNQELQEAKLNEKRRALRKALEGNKELNKDLQEDSQLQKDYKYDESRATQEETETNLDDEYHRLGEREPKVLVTTSREPSSRLAQFAKEVRLLIPNSYRLNRGNIVVGSLVEAARANDITDIVILHEHRGIPDGLVISHLPYGPTLSFSLHNVVLRHDIPNTGTMSEAYPHLIFENLTSKLGKRVKTALSALFPPDPKDTTPRVVTFANTDDYISFRHHIYAKTGPKQIILSEAGPRFEMKLFEITLGTVDMVDADVEWKLKPYQRHKRDVLAE
Protein: TBC1 domain family member 1 (D4AC16)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Ras-related protein Rab-8A
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- Ras-related protein Rab-10
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- Ras-related protein Rab-14
- Ras-related protein Rab-2A
- Protein kinase AMP-activated non-catalytic subunit gamma 3
- Ras-related protein Rab-11B
- 5'-AMP-activated protein kinase subunit beta-2
- Protein kinase AMP-activated non-catalytic subunit gamma 2
Sequence:
MSPLFSWVAKVPEIISSIRQAGKIARQEELRCPSEFDDTFAKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSCGRRIDWDAPTGQPSAPGARPMRKSFSQPGLRSLAFRKEFQDASLRSSTFSSFDNDIENHLIGGHNVVQPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGGGAGFHFVCYVFQCTNEALVDEIMMTLKQAFTVAAVQQTAKAPAQLCEGCPLQGLHKLCERIEGMNSSKTKLELQKHLTTLTNQEQAMIFEEVQKLRPRNEQRENELIISFLRCLYEEKQKEHSHTGEPKQTLQVAAENIGSELPPSASRFRLDSLKNRAKRSLTESLESILSRGNKARGLQDHSASVDLDSSTSSTLSNTSKELSMGDKEALPISESSFKLLGSSDDLSSDSESHIAEESALLSPQQAFRRRANTLSHFPVECPAPPEPAQTSPGVSQRKLMRYHSVSTETPHERKDFESKANHLGDTDGTPVKARRHSWRQQIFLRVATPQKACDSPSRYEDYSELGELPPRSPLEPVCEDGPFGPVQEEKKKTSRELRELWKKAILQQILLLRMEKENQKLQASENDLLNKRLKLDYEEITPCLKEVTTVWEKMLSTPGRSKIKFDMEKVHSAVGQGVPRHHRGEIWKFLAEQFHLKHPFPSKQQPKDVPYKELLKKLTSQQHAILIDLGRTFPTHPYFSAQLGAGQLSLYNILKAYSLLDQEVGYCQGLSFVAGILLLHMSEEEAFKMLKFLMFDMGLRKQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEYEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLILQHENLETIVDFIKNTLPNLGLVQMEKTISQVFEMDIAKQLQAYEVEYHVLQEELIDSSPLSDNQRMDKLEKTNSSLRKQNLDLLEQLQVANARIQSLEVTVEKLLTSESKLKQAVLTLEMERSALLQMVEELRRQMAQPSTAEPDCTRLEPTGD
Protein: MACPF domain-containing protein CAD1 (Protein CONSTITUTIVELY ACTIVATED CELL DEATH 1) (Protein CAD1) (Q9C7N2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negatively controls the salicylic acid (SA)-mediated pathway of programmed cell death in plant immunity.
Interaction partners:
- Expressed protein
- Berberine bridge enzyme-like 16
- Vesicle-associated protein 1-4
- Similarity to disease resistance protein domain family protein)
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- FCS-Like Zinc finger 3
- Eukaryotic translation initiation factor 4E-3
- Brefeldin A-inhibited guanine nucleotide-exchange protein 2
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Probable protein phosphatase 2C 67
Sequence:
MENRKGGNFSVPSSEALTTTLRNAIQALGRGFDVTSDVRLLYCKGAPGSRLVRIEEGQNRDLELSHGFLLPNVPADIDCSRGNSGTQRISVCSFHEMAEEFNVRSGVKGNIPLGCFNAMFNYTGSWQVDAASTKSLALVGYFIPLYDVKLAKLTLVLHNEIRRAVPSSWDPASLASFIENYGTHIVTSVTIGGRDVVYIRQHQSSPLPVSEIENYVNDMIKHRFHEAESQSITGPLKYKDKDITVIFRRRGGDDLEQSHARWAETVPAAPDIINMTFTPIVSLLEGVPGLRHLTRAIELYLEYKPPIEDLQYFLDYQIARAWAPEQSNLQRKEPVCSSLQFSLMGPKLFISADQVTVGRKPVTGLRLSLEGSKQNRLSIHLQHLVSLPKILQPHWDSHVPIGAPKWQGPEEQDSRWFEPIKWKNFSHVSTSPIEHTETHIGDLSGVHIVTGAQLGVWDFGSKNVLHLKLLFSKVPGCTIRRSVWDHTPVASSGRLEPGGPSTSSSTEEVSGQSGKLAKIVDSSEMLKGPQDLPGHWLVTGAKLGVEKGKIVLRVKYSLLNY
Protein: rRNA processing protein (Q381W4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVKKMGRDEARAGVERRPPPMLKAERQAAFRRKVRNELLLSGRERKDAERQRMEEFRRLCKAEGIQSKRLQEYDAMREEAANKLGEKLNHIEYDQSLTNAEKRKRRYNLKRNYAGQTVMDLVQKQEKHHNALTKVEKIRKKRQEEIEAARVAKRERDEMKVKRIKERMAQNALYAQRTRKGQPVMSGRVEALLNKIQRNQQQ
Protein: AP-2 complex subunit alpha (Q66HM2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane, coated pit {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004277}.
Interaction partners:
Sequence:
MPAVSKGEGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSPDLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLETILNKAQEPPKSKKVQHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSIREEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAAKTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRALLLSTYIKFVNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLEEMPPFPERESSILAKLKKKKGPSTVTDLEETKRERSIDVNGGPEPVPASTSAASTPSPSADLLGLGAVPPAPTGPPPTSGGGLLVDVFSDSASAVAPLAPGSEDNFARFVCKNNGVLFENQLLQIGLKSEFRQNLGRMFIFYGNKTSTQFLNFTPTLICADDLQTNLNLQTKPVDPTVDGGAQVQQVVNIECISDFTEAPVLNIQFRYGGTFQNVSVKLPITLNKFFQPTEMASQDFFQRWKQLSNPQQEVQNIFKAKHPMDTEITKAKIIGFGSALLEEVDPNPANFVGAGIIHTKTTQIGCLLRLEPNLQAQMYRLTLRTSKDTVSQRLCELLSEQF
Protein: Tetratricopeptide repeat (TPR)-containing protein (F4HS68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGASLPPKEANLFKLIVKSYETKQYKKGLKAADAILKKFPDHGETLSMKGLTLNCMDRKTEAYELVRLGVKNDIKSHVCWHVLGLLYRSDREYREAIKCYRNALRIDPDNLEILRDLSLLQAQMRDLSGFVETRQQLLTLKPNHRMNWIGFAVSQHLNANASKAVEILEAYEGTLEDDYPPENELIEHTEMILYKVSLLEESGSFDKALEELHKKEPKIVDKLSYKEQEVSLLSKVGRLEEANKLYRVLLSMNPDNYRYHEGLQKCLGLYSESGQYSSDQIEKLNALYQSLSEQYTRSSAVKRIPLDFLQDENFKEAVAKYIKPLLTKGVPSLFSDLSSLYDHPRKPDILEQLVVEMKHSIGTTGSFPGSDVKEPPSTLLWTLFFLAQHYDRRGQYDVALCKIDEAIAHTPTVIDLYSVKSRIMKHAGDLTAAAALADEARGMDLADRYINSECVKRMLQADQVPLAEKTAVLFTKEGDQLNNLHDMQCMWYDLASGDSYFRQGDLGRALKKFLAVEKHYADISEDQFDFHSYCLRKMTLRSYVDMLKFQDRLHSFPYFHKAAIRAIRCYLKLHDSPKSTAGEDEMSKLAPAQKKKIKKQKKAEARAKKEAESKSEESTASGASKSGKRNVKPVDPDPHGQKLIQVEEPMAEASKYLRLLQKHSPNSLETHLLSFEVNMRKQKFLLAFQAVKQLLKLGAENPDSHRSLVKFFLMTESISAPTTEAEKLRWRVLEAERPSISQLQNKSLMEANKEFLGRHEDSLVHRAAYAEMLYILDPSKKTEAIKIIEDSTNKVVQTNEALGQAREWKLKDCIAVHTLLDTVLLDSQAASRWKSRCAEYFPCSTHFEGKHCSLMPDSVYNSSRKSNENGDTPNHPMGQTELSDGQLEAFKSLSKMFWSCNMPNVYNCFSI
Protein: Phosphoethanolamine/phosphocholine phosphatase (EC 3.1.3.75) (Q8R2H9)
Organism: Mus musculus (Mouse)
Function: Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho) (By similarity). Involved in the generation of inorganic phosphate for bone mineralization. Acts in a non-redundant manner with PHOSPHO1 in skeletal mineralization: while PHOSPHO1 mediates the initiation of hydroxyapatite crystallization in the matrix vesicles (MVs), ALPL/TNAP catalyzes the spread of hydroxyapatite crystallization in the extracellular matrix.
Subcellular location: Extracellular vesicle {ECO:0000269|PubMed:17227223}. Note=Localizes to special class of extracellular vesicles, named matrix vesicles (MVs), which are released by osteogenic cells. {ECO:0000269|PubMed:17227223}.
Interaction partners:
- Ethanolamine-phosphate cytidylyltransferase
- Choline-phosphate cytidylyltransferase A
- Choline/ethanolamine kinase
- Ethanolamine-phosphate phospho-lyase
- Choline-phosphate cytidylyltransferase B
- Choline kinase alpha
- Glycerophosphocholine phosphodiesterase GPCPD1
- Choline O-acetyltransferase
- Acetylcholinesterase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Sequence:
MSGCFPAVGLRCLSRDGRMAAPGAPRFLLTFDFDETIVDENSDDSIVRAAPGQQLPESLRATYREGYYNEYMQRVFKYLGEQGVRPRDLRAVYETIPLSPGMGDLLQFIAKQGSCFEVILISDANTFGVESALRAAGHHSLFRRILSNPSGPDARGLLTLRPFHTHSCSRCPANMCKHKVLSEYLRERARDGVHFERLFYVGDGANDFCPMGLLAGGDVAFPRRGYPMHRLIQEAQKAEPSSFRAHVVPWETAADVRQHLQQVLKMC
Protein: DnaJ heat shock protein family (Hsp40) member C7 (A0A6I8PLE7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKDFDPNNIFKAFFGGPGGFSFEASGPGNFFFQFG
Protein: Leishmanolysin (EC 3.4.24.36) (Q4QHH0)
Organism: Leishmania major
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MSVDSSSTHRRRCVAARLVRLAAAGAAVTVAVGTAAAWAHAGALQHRCVHDAMQARVRQSVADHHKAPGAVSAVGLPYVTLDAAHTAAAADPRPGSARSVVRDVNWGALRIAVSTEDLTDPAYHCARVGQRVNNHAGAIVTCTAEDILTNEKRNILVKYLIPQAVQLHKERLKVQQVQGKWKVTDMVGEICGDFKVPQAHITEGFSNTDFVMYVASVPSEEGVLAWATTCQTFSDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHALGFSGPFFEDARIVANVSNVRGKNFDVPVINSSTAVAKAREQYGCDTLEYLEVEDQGGAGSAGSHIKMRNAQDELMAPAAAAGYYTALTMAIFQDLGFYQADFSKAEVMPWGQNAGCAFLTNKCMEQNITQWPAMFCNESEDAIRCPTSRLLLGTCGIREYELPLPRYWQYFTNASLGGYSPFLDYCPFVIDYADGSCNQDASSAEEFFTAFNVFSDAARCIDGAFRPKATNGIVKSYAGLCANVQCDTATRTYSVQVHGSNDYTNCTPGLRVELSTVSKTFEEGGYITCPPYVEVCQGNVQAAKDFDGDSDSSSSSSDAADKAAIERWNERMAGLATAATVLLGVVLSLMALVVVWLLLVSCPRWCCKVGGLPT
Protein: At4g21108/At4g21108 (Cytochrome-c oxidase/ electron carrier) (Q944S8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- At1g31410
- Disease resistance protein
- Subtilisin-like protease SBT2.6
- Protein PECTIC ARABINOGALACTAN SYNTHESIS-RELATED
- Putative clathrin assembly protein At4g40080
- Probable pectate lyase 5
- Probable amino acid permease 7
- Proteasome activator subunit 4
- Copper transport protein ATX1
Sequence:
MLTETPFRPREKLLEKQRLFQSIQRHTYLKGPMDKITSVAIPIALAASSLYMIGTGIYNMSNGIGKKE
Protein: Solute carrier family 12 member 1 (Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 1) (BSC1) (Kidney-specific Na-K-Cl symporter) (Na-K-2Cl cotransporter 2) (mNKCC2) (P55014)
Organism: Mus musculus (Mouse)
Function: Renal sodium, potassium and chloride ion cotransporter that mediates the transepithelial NaCl reabsorption in the thick ascending limb and plays an essential role in the urinary concentration and volume regulation. Electrically silent transporter system.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:29993276}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 1
- STE20/SPS1-related proline-alanine-rich protein kinase
- Aquaporin-2
- Sodium/hydrogen exchanger 3
- Barttin
- Uromodulin
- Chloride channel protein ClC-Kb
- Epithelial sodium channel subunit gamma
- Sodium-dependent phosphate transport protein 2A
- Epithelial sodium channel subunit alpha
Sequence:
MSVSIPSNSVPSSASRFQVHVINEGHGSAAAVGDSADPPHYEETSFGDEAQNRLRISFRPGNQECYDNFLQTGETAKTDTTFHAYDSHTNTYYLQTFGHNTMDAVPKIEYYRNTGSVSGPKVNRPSLLEIHEQLAKNVTVAPGSADRVANGDGMPGDEQAENKEEDMTGVVKFGWVKGVLVRCMLNIWGVMLFIRLSWIVGEAGIGLGVLIILLSTMVTSITGLSTSAIATNGFVRGGGAYYLISRSLGPEFGGSIGLIFAFANAVAVAMYVVGFAETVVDLLKESDSMMVDPTNDIRIIGSITVVILLGISVAGMEWEAKAQVILLVILLIAIANFFIGTVIPSNNEKKSRGFFNYQASIFAENFGPSFTKGEGFFSVFAIFFPAATGILAGANISGDLEDPQDAIPRGTMLAIFITTVAYIGVAICVAACVVRDATGSMNDTIVSGMNCNGSAACGLGYDFSRCQHEPCQYGLMNNFQVMSMVSGFGPLITAGIFSATLSSALASLVSAPKVFQALCKDNIFKGLQFFAKGYGKNNEPLRGYFLTFVIAMAFILIAELNVIAPIISNFFLASYALINFSCFHASYAKSPGWRPAYGIYNMWVSLFGAILCCAVMFVINWWAAVITYVIELFLYIYVTYKKPDVNWGSSTQALSYVSALDNALELTTVEDHVKNFRPQCIVLTGGPMTRPALLDITHAFTKNSGLCICCEVFVGPRKLCVKEMNSGMAKKQAWLIKNKIKAFYAAVAADCFRDGVRSLLQASGLGRMKPNTLVIGYKKNWRKAPLSELENYVGIIHDAFDFEIGVVIVRISQGFDISPVLQVQDELEKLEQERLALEAAIKDNECEEGKGGIRGLFKKAGKLNITKPAPKKDGNISSIQSMHVGEFNQKLVEASAQFKKKQGKGTIDVWWLFDDGGLTLLIPYILTLRKKWKDCKLRIYVGGKITRIEEEKISMASLLSKFRIKFADIHIIGDINIKPNKESWKVFEEMIEPYRLHESHKDLTTAEKLKRESPWKITDAELEAVKEKSYRQVRLNELLQEHSRAANLIVLSLPVARKGSISDLLYMAWLEILTKNLPPVLLVRGNHKNVLTFYS
Protein: Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMN/NaMN adenylyltransferase 1) (EC 2.7.7.1) (EC 2.7.7.18) (NAD(+) diphosphorylase 1) (NAD(+) pyrophosphorylase 1) (Nicotinamide-nucleotide adenylyltransferase 1) (NMN adenylyltransferase 1) (NMNAT 1) (Nicotinate-nucleotide adenylyltransferase 1) (NaMN adenylyltransferase 1) (NaMNAT 1) (Q06178)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate to form deamido-NAD(+) (NaAD). Key enzyme in both de novo and salvage pathways for NAD(+) biosynthesis. Predominantly acts in the salvage pathways via NMN.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Glutamine-dependent NAD
- Nicotinate phosphoribosyltransferase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Uridine nucleosidase
- Purine nucleoside phosphorylase
- NAD-dependent histone deacetylase SIR2
- Nicotinamide riboside kinase
- IMP-specific 5'-nucleotidase 1
- Suppressor of disruption of TFIIS
Sequence:
MDPTRAPDFKPPSADEELIPPPDPESKIPKSIPIIPYVLADANSSIDAPFNIKRKKKHPKHHHHHHHSRKEGNDKKHQHIPLNQDDFQPLSAEVSSEDDDADFRSKERYGSDSTTESETRGVQKYQIADLEEVPHGIVRQARTLEDYEFPSHRLSKKLLDPNKLPLVIVACGSFSPITYLHLRMFEMALDAISEQTRFEVIGGYYSPVSDNYQKQGLAPSYHRVRMCELACERTSSWLMVDAWESLQPSYTRTAKVLDHFNHEINIKRGGVATVTGEKIGVKIMLLAGGDLIESMGEPNVWADADLHHILGNYGCLIVERTGSDVRSFLLSHDIMYEHRRNILIIKQLIYNDISSTKVRLFIRRAMSVQYLLPNSVIRYIQEHRLYVDQTEPVKQVLGNKE
Protein: Photosystem II protein D1 2 (PSII D1 protein 2) (EC 1.10.3.9) (Photosystem II Q(B) protein 2) (P16033)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:9512353}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:9512353}.
Interaction partners:
- Photosystem II D2 protein
- Cytochrome b559 subunit beta
- Cytochrome b559 subunit alpha
- Photosystem II reaction center protein H
- Photosystem II extrinsic protein V
- Photosystem II reaction center protein I
- Photosystem II CP47 reaction center protein
- Photosystem II CP43 reaction center protein
- Photosystem II reaction center protein K
- Photosystem II reaction center protein L
Sequence:
MTTTLQQRESASLWEQFCQWVTSTNNRIYVGWFGTLMIPTLLTATTCFIIAFIAAPPVDIDGIREPVAGSLLYGNNIISGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLVVFHFLIGIFCYMGRQWELSYRLGMRPWICVAYSAPVSAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLVRETTEVESQNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLGAWPVIGIWFTAMGVSTMAFNLNGFNFNQSILDSQGRVIGTWADVLNRANIGFEVMHERNAHNFPLDLASGEQAPVALTAPAVNG
Protein: Chromosome associated protein G, isoform F (A1Z987)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
- Structural maintenance of chromosomes protein
- Condensin complex subunit 1
- Condensin complex subunit 2
- Structural maintenance of chromosomes protein
- Condensin-2 complex subunit
- Chromosome associated protein H2, isoform E
- Protein abnormal spindle
- Monopolar spindle 1, isoform B
- Structural maintenance of chromosomes protein
- Guanylate kinase-associated protein mars
Sequence:
MAKPKAKAGETEKPKTKAAGGKKRLAATKKTKKDGEKENEDQSVATTSDTSAELMYAIMRQAELKESLHKRYSKEMQQLYAKMGHESFRKAFINVLKAVLGAEEGNENANMALNFCATFVTSSDSDGTEPMLAETFHWLLTTYSSNPHIRYRICYFVNLILKELGPNAALDDHQCDDILEAMLDRVKDVSASVRKQAVLAMQRLQNPDNPSDVVVGAYMYHLTSDPSPNVRQCIITCMGRNYITIPHILERLWDVDEKVRRHTYVNMCNYPVRSYKVAQRLTLLEQGLNDTSATVRKTVINFMLKTWIESYQQNYVALIAALKLDSNEEELLRFRRVAKQMLRVIFQQTDIKQLIDQLPLSEDCELHRCIPHDSVTVELLLYWQCLSEYLETEAPEIESLLPELSVFCTYMDKFCQFQKPDMDKFAQVEFQNMLLSLVEILETYDLGDEIGRGNMRLLITNLLKDCLLDHKIVRVLVRCMEQLITDTNDRIQYFIEIIYELCELNTKQNDLIHDRSLINKLLDDLDTPLKMKISSLKVKILELEELEGNYVRQREYIRAQSVNDEKIAVTEEYTELIRPLLEKHGVIEMPTRPKLSKQERVLKGLYISYYMTASPHVHKLTPSLCQLYKDFICRYLPCAEVDIFEWSIKCGTTFSIFYEAYSREVFEVVVVQFCKNNNVRLCEASANCILELLDRYGVDYFNDLNQTGGSLSKTKRRQLYTMQELYDDDDGSQSQNNEQNSDILVVLGHYLERVQHRGVGMAIVRGLCRLVLRGHVDDRTDVLELLLKRYFNPNTEPIINQVLGLFFEELRRLNKHSLLQPCFLPTVWTCNYDSPLHGVQPEHLTKFFLEMTVQEMSTPQTNIHNKIAISFLQYIQNYFTERKDMCRLLAKELTNLSINVLNGPEVKAELLALAENLIQSELDPRMIKCIQNFKLVVNGSFNPPPRRNPDEGESDEEYETATVTTAESETAVPAQSQPPVTEESPNDVTQSAAITAVDATETPKAAAPPAPVPEPIVTTFGKDNIVGIRHLRRSMAISHSDAESLLGPQSPNPEESTESEAVETSKQNLRQPQMRRRLEMAIARSSKTPEKQPSTEEESSDEEISESPNAANKSNDSEVIEASPTAASPSPRAGHEASHLRIRSLRIRKVASTSTSQTTPKPVSKRKVVHLETPLRNGRKRVLRRSPSNSNSRSLRSRDSTALSSPRVSPRRKQQRLDNRSTRRQQMTKNTNSPTDSTSSVKENQIPPVIVIELDSDTESESNAKPESTPPKKPLKKTIPLIRSRPSSSTPKVTTRNEARAQRMNSKVMTRKRMSLEMNLSGGQLQVSTPKRVTRAVALSMSTDGKRSRRK
Protein: At5g59610 (Chaperone DnaJ-domain superfamily protein) (Q9FNA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MYATSSILSPTPQSFFLSHHLPPISFLYRINFLGFPVTSCCYGGDIGLASLYKRRSSIQRRRNRIFVTRARSSPYEILGVSPSATPQDIKRAYRKLALKYHPDVNKEANAQEKFLKIKHAYTTLINSDSRRKYGSDSRATGSSTGQTSRKGNSQVEEDFYGLGDFFKDLQEEYKNWEASASSQGKPKSLWEELSEIGEEFVEFLEKELNISDEDNEGSSKNGERFDFEEGSTEKSSGKNNSSTKNSIEDNIDEIEATLAQLKKDLGLQ
Protein: Conidiation-specific protein 10 (Eurofung) (Q5B365)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- SpoC1-C1C protein
Sequence:
MADNQNPGNFANRPHEEVENIARKGGQSSHSGGFASMDSEKQRNIASQGGHASSGSFQPGDERAREAGRKGGKATGHHEPEE
Protein: Kinesin-like protein (Q38E15)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Kinesin-like protein, putative
- Kinesin, putative
- Kinesin-like protein
- Kinesin-like protein
- Kinesin-like protein
- Kinesin-like protein
Sequence:
MPNIPLVAELGTKCAEFQRLLNTSEVPEVVKKKLRPSMDPKELFTSQDSRIFVRCRPIIPFDQEDMNSKSIIRKVDGYRDPVVMSPKISLAGQCTIEPHSVTLDGVFCGGDDTERVYMESCAPLVHLSVEGASTCVLCYGQTGSGKTHTTLGIVGLMSRDLAPYFASHNIFITVIEIQANKNIDLLTGSEVQVVEDISGELKIRGTDGFECSNDEMLLAVFQEAASQRMTKATGRNEVSSRSHMVTCIQIICKNSTWVKPGELFIVDLAGSENTADSATHDKERQMEAKFINTSLMTLKECIRARAMAATSTSHLHIPFRRSPLTLLLRDCFEIAVKRPTKTVVIACVSPLLRDSRHTINTLRYASLLAVTVPARIVADDPDDPNGFDREQALAFICRCSRGRITNPEYILPEGDGRTLVHIPEAEFIRRIMESHAKISEKGAKQIYTSVWQKIVDARTKGRKVMTSSKKAPIAPRCATQRR