wanglab/gogpt-training-data huggingface dataset:
Protein: Aa1018 (Vitronectin) (Q7TQ11)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Plasminogen activator inhibitor 1
- Urokinase plasminogen activator surface receptor
- Urokinase-type plasminogen activator
- Integrin beta-3
- Integrin beta-1
- Integrin alpha-8
- Plasminogen
- Integrin subunit alpha 2b
- Fibronectin
- Nidogen-1
Sequence:
MASLRPFFILALLALVSLADQESCKGRCTQGFMASKKCQCDELCTYYQSCCVDYMEQCKPQVTRGDVFTMPEDEYWSYDYPEETKNSTSTGVQSENTSLHFNLKPRAEETIKPTTPDPQEQSNTQEPEVGQQGVAPRPDTTDEGTSEFPEEELCSGKPFDAFTDLKNGSLFAFRGDSVDRFDGGEYCYELDETAVRPGYPKLIQDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPDYPRNISEGFSGIPDNVDAALALPAHSYSGRERVYFFKGTQGKQYWEYEFQQQPSQEECEGSSLSAVFEHFALLQRDSWENIFELLFWGRSSDGAKGPQFISRDWHGVPGKVDAAMAGRIYITGSTFRSVQAKKQKSGRRSRKRYRSRRGRGHSRSRSRSMSSRRPSRSVWFSLLSSEESGLGTYNYDYDMNWRIPATCEPIQSVYFFSGDKYYRVNLRTRRVDSVNPPYPRSIAQYWLGCPTSEK
Protein: Mitochondrial translation factor sls1 (Q9UT03)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in aerobic respiration where it is required for assembly of respiratory chain enzyme complexes III and IV. Also has a role in mitochondrial gene expression (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Mitochondrial translation ATP-dependent RNA helicase mrh5
- Cytochrome b translation regulator cbp8
- Cytochrome b translation regulator cbp7
- Small ribosomal subunit protein L51-b
- ATP-dependent RNA helicase mss116, mitochondrial
- Mitochondrial cox1 translation regulator ppr4
Sequence:
MVKGSLLNRNINALNCRCLAQKLTSWGLLNIRSIHADSNRGVVNSSNLIIIPPYKPKSKSVLRSPYLTSHYVDALAFKLVEDPTVHNTLEDVFQDIESYKPKSVNTSAKSFRQLVNTLEVAFRKEQLRKFAKVFHIKSSSLRKKEIIERILLDHWKLRIHGDAMDDMLAIKDVTLCPLEMFFLLLNNASALRDISQKHAAHVVINVTNNNIKIEAKKRDVAIVEELISGIFKHLKSKTIDVTEYYANIINKNAVLLSERCKAYIELSGKAQIKITTAFGNCSFDEIERKLLSFVMLFENTDKCLIDSECLTSKKSFTLNDFTYDFRLPWYLKDDSWKRWCRVKEYSWNTSVLSDEALTRNSLTLPVPIKPSINKDISSIEVKDLSQKNTTQSKKLNSYIRDSFHSVNDFWFSSHATNTEQCFTKRLTATFGYSLFSSSFLSHTKNPDVASFYVKERSKAHHFLFNTFVDQIPSYLKNHSILDETTRKSFYRIILSSNSLSTSLTYPLIEIILPIKNGFLMGKETFQIAFKKSRGYQILLPESELDLKINTTTFKTIANNKSVDAFLDDCVSFFSRPEMTQDSQLNASSGFLTNFSLKDSTDRFYKVLSYEKVSERFVKIDDSYITYSDIFSPLSHSHKDWFRIHTEENSSKNFYEIISEIVGGFPYYSQANERSLIS
Protein: IQ motif and Sec7 domain ArfGEF 2 (A0A8I6APH1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MEPPWKSSRSTASHTLHQYCCPTQVLDSMKLTPSGRLAESSVEGDAPGSDLSTAVDSPGSQPPYRLSQLPPTSSHMGGPPAGVGLPWSQRARLQPASVALRKQEEEEIKRSKALSDSYELSTDLQDKKVEMLERKYGGSFLSRRAARTIQTAFRQYRMNKNFERLRSSASESRMSRRIILSNMRMQFSFEEYEKAQNPAYFEGKPASLDEGAMAGARSHRLERGLPYGGSCGGGIDGGGSSVTTSGEFSNDITELEDSFSKQVKSLAESIDEALNCHPSGPMSEEPGSAQLEKRESKEQQEDSSATSFSDLPLYLDDPVPPPSPERLPSTEPPPQGRPEFWAPAPLPPVPPPMPPGTREDGSREEGTRRGPGCLECRDFRLRAAHLPLLTIEPPSDSSVDLSDRSDRGSVHRQLVYEADGCSPHGTLKHKGPPGRAPIPHRHYPAPEGPAPAPPGPLPPAPNSGTGPSGVAGGRRLGKCEAAGENSDGGDNESLESSSNSNETINCSSGSSSRDSLREPPATGLCKQTYQRETRHSWDSPAFNNDVVQRRHYRIGLNLFNKKPEKGIQYLIERGFLSDTPVGVAHFILERKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSSMDLDDALRKFQSHIRVQGEAQKVERLIEAFSQRYCVCNPALVRQFRNPDTIFILAFAIILLNTDMYSPSVKAERKMKLDDFIKNLRGVDNGEDIPRDLLVGIYQRIQGRELRTNDDHVSQVQAVERMIVGKKPVLSLPHRRLVCCCQLYEVPDPNRPQRLGLHQREVFLFNDLLVVTKIFQKKKILVTYSFRQSFPLVEMHMQLFQNSYYQFGIKLLSAVPGGERKVLIIFNAPSLQDRLRFTSDLRESIAEVQEMEKYRVESELEKQKGMMRPNASQPGGAKDSVNGTLARSSLEDTYGAGDGLKRGALSSSLRDLSDAGVCY
Protein: Small ribosomal subunit protein uS17 (30S ribosomal protein S17) (P9WH51)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Interaction partners:
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein bL20
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL21
Sequence:
MAEAKTGAKAAPRVAKAAKAAPKKAAPNDAEAIGAANAANVKGPKHTPRTPKPRGRRKTRIGYVVSDKMQKTIVVELEDRMRHPLYGKIIRTTKKVKAHDEDSVAGIGDRVSLMETRPLSATKRWRLVEILEKAK
Protein: N(6)-adenosine-methyltransferase subunit METTL3 (EC 2.1.1.348) (N(6)-adenosine-methyltransferase 70 kDa subunit) (MT-A70) (F1R777)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some RNAs and regulates various processes such as the circadian clock, differentiation of embryonic and hematopoietic stem cells, cortical neurogenesis, response to DNA damage, differentiation of T-cells and primary miRNA processing. In the heterodimer formed with mettl14, mettl3 constitutes the catalytic core (By similarity). N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability, processing and translation efficiency (By similarity). M6A is also involved in hematopoietic stem cells specification: m6A methylation and subsequent destabilization of mRNAs, such as notch1a, leads to decreased Notch signaling, promoting endothelial to hematopoietic transition. M6A also takes place in other RNA molecules, such as primary miRNA (pri-miRNAs) (By similarity). Mediates methylation of pri-miRNAs (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q86U44}. Nucleus speckle {ECO:0000250|UniProtKB:Q86U44}. Cytoplasm {ECO:0000250|UniProtKB:Q86U44}. Note=Colocalizes with speckles in interphase nuclei. Suggesting that it may be associated with nuclear pre-mRNA splicing components. {ECO:0000250|UniProtKB:Q86U44}.
Interaction partners:
- Pre-mRNA-splicing regulator WTAP
- N
- Protein virilizer homolog isoform X2
- Zinc finger CCCH domain-containing protein 13
- RNA-binding protein 15
- YTH domain-containing family protein 2
- RNA demethylase ALKBH5
- YTH domain-containing family protein
- YTH domain-containing 1.
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
Sequence:
MSDTWSHIQAHKKQLDSLRERLQRRRKDPTQLGTEVGSVESGSARSDSPGPAIQSPPQVEVEHPPDPELEKRLLGYLSELSLSLPTDSLTITNQLNTSESPVSHSCIQSLLLKFSAQELIEVRQPSITSSSSSTLVTSVDHTKLWAMIGSAGQSQRTAVKRKADDITHQKRALGSSPSIQAPPSPPRKSSVSLATASISQLTASSGGGGGGADKKGRSNKVQASHLDMEIESLLSQQSTKEQQSKKVSQEILELLNTSSAKEQSIVEKFRSRGRAQVQEFCDYGTKEECVQSGDTPQPCTKLHFRRIINKHTDESLGDCSFLNTCFHMDTCKYVHYEIDSPPEAEGDALGPQAGAAELGLHSTVGDSNVGKLFPSQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRKLNIPILQDDGFLFLWVTGRAMELGRECLSLWGYDRVDEIIWVKTNQLQRIIRTGRTGHWLNHGKEHCLVGVKGNPQGFNRGLDCDVIVAEVRSTSHKPDEIYGMIERLSPGTRKIELFGRPHNVQPNWITLGNQLDGIHLLDPEVVARFKKRYPDGVISKPKNM
Protein: Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5) (D4N2R0)
Organism: Meleagris gallopavo (Wild turkey)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000256|HAMAP-Rule:MF_03205}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000256|HAMAP-Rule:MF_03205}.
Interaction partners:
Sequence:
MERLDKTINSYLDVWLGPRDPRVKGWLLLENYTPTFIFSVLYLLIVWLGPKYMRNKQPFSCRGILVVYNLGLTLLSLYMFYELVTGVWEGGYNFYCQDTRSGGEADMKIIHVLWWYYFSKLIEFMDTFFFILRKNNHQITVLHVYHHATMLNIWWFVMNWVPCGHSYFGATLNSFIHVLMYSYYGLSAVPAMRPYLWWKKYITQGQLIQFVLTIFQTSCGVVWPCAFPQGWLYFQIFYMISLIILFTNFYIQTYNKKASSRRKEYQNGSTATVNGYTNSFSSLENNVKQRKQRKD
Protein: Bax inhibitor 1 (Q9VSH3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Suppressor of apoptosis (By similarity). Modulates unfolded protein response signaling. Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P55061}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55061}.
Interaction partners:
- Uncharacterized protein, isoform B
- GEO07442p1
- Presenilin homolog
- IP10175p
- AT21555p
Sequence:
MADTANYINDRFQTFMNGLGDRYEPYVREHLSKVYMVLGSTAAATAMGAMLQMRDFLDLGVLAAVATLVLVLGLHFYKDDGKNYYTRLGMLYAFGFCSGQTLGPLLGYICSINPAIILSALTGTFVTFISLSLSALLAEQGKYLYLGGMLVSVINTMALLSLFNMVFKSYFVQVTQLYVGVFVMAAFIVYDTQNIVEKCRNGNRDVVQHALDLFFDVLSMFRRLLIILTQKEERKQNERRQNKTK
Protein: Virion host shutoff protein (Vhs) (EC 3.1.27.-) (Q82171)
Organism: Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
Function: Minor structural protein that acts as an endoribonuclease during lytic infection. Degrades host mRNAs in the cytoplasm by cutting them at preferred sites, including some in regions of translation initiation. Together with inhibition of host splicing by ICP27, contributes to an overall decrease in host protein synthesis. Also, after the onset of viral transcription, accelerates the turnover of viral mRNA, thereby facilitating the sequential expression of different classes of viral genes. Binds translation initiation factors eIF4H, eIF4AI, and eIF4AII, thereby may interact directly with the translation initiation complex and thus digest specifically mRNAs. Also impedes antigen presentation by major histocompatibility complex class I and class II molecules, inhibits secretion of cytokines that would otherwise recruit lymphocytes and neutrophils cells to the site of infection and blocks the activation of dendritic cells. Impedes the alpha/beta interferon-mediated response to infection by evading the cGAS/ STING-mediated DNA-sensing pathway and degrading CGAS via its RNase activity.
Subcellular location: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MGLFGMMKFAHTHHLVKRQGLGAPAGYFTPIAVDLWNVMYTLVVKYQRRYPSYDREAITLHCLCRLLKVFTQKSLFPIFVTDRGVNCMEPVVFGAKAILARTTAQCRTDEEASDVDASPPPSPITDSRPSSAFSNMRRRGTSLASGTRGTAGSGAALPSAAPSKPALRLAHLFCIRVLRALGYAYINSGQLEADDACANLYHTNTVAYVYTTDTDLLLMGCDIVLDISACYIPTINCRDILKYFKMSYPQFLALFVRCHTDLHPNNTYASVEDVLRECHWTPPSRSQTRRAIRREHTSSRSTETRPPLPPAAGGTEMRVSWTEILTQQIAGGYEDDEDLPLDPRDVTGGHPGPRSSSSEILTPPELVQVPNAQLLEEHRSYVASRRRHVIHDAPESLDWLPDPMTITELVEHRYIKYVISLIGPKERGPWTLLKRLPIYQDIRDENLARSIVTRHITAPDIADRFLEQLRTQAPPPAFYKDVLAKFWDE
Protein: Pantothenate kinase 2 (AtPANK2) (Pantothenic acid kinase 2) [Includes: Pantothenate kinase (EC 2.7.1.33); 4'-phosphopantetheine phosphatase (EC 3.1.3.-)] (Q8L5Y9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the phosphorylation of pantothenate the first step in CoA biosynthesis. May play a role in the physiological regulation of the intracellular CoA concentration. Functionally redudant with PANK1. The phosphatase activity shows preference for normal or oxidatively damaged intermediates of 4'-phosphopantetheine, which provides strong indirect evidence that the phosphatase activity pre-empts damage in the CoA pathway. Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms. Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein.
Interaction partners:
- Pantoate--beta-alanine ligase
- Phosphopantothenoylcysteine decarboxylase
- Phosphopantetheine adenylyltransferase
- Phosphopantothenate--cysteine ligase 1
- Probable phosphopantothenoylcysteine decarboxylase
- Pantothenate kinase 1
- 3-methyl-2-oxobutanoate hydroxymethyltransferase 2, mitochondrial
- 3-methyl-2-oxobutanoate hydroxymethyltransferase 1, mitochondrial
- Alkaline-phosphatase-like family protein
- Dephospho-CoA kinase
Sequence:
MAGQEDEYDPILDNKREAEAKSQVSVAADKNMAPSTSGTPIHRSGSRPQLDLSKAEIQGNLEERDPTILLPNQSDDISHLALDIGGSLIKLLYFSRHEDYSNDDDKRKRTIKERLGITNGNLRSYPVLGGRLHFVKFETHKINECLDFIHSKQLHRRDPYPWSSKTLPLGTGVIKVTGGGAFKFADLFKERLGVSIEKEDEMHCLVSGANFLLKAIRHEAFTHMEGEKEFVQIDPNDLYPYLLVNVGSGVSIIKVDGEGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELSQKGDNSAIDMLVGDIYGGMDYSKIGLSASTIASSFGKAISENKELDDYRPEDISLSLLRMISYNIGQISYLNALRFGLKRIFFGGFFIRGHAYTMDTISFAVHFWSKGEMQAMFLRHEGFLGALGAFMSYEKHGLDDLMSHQLVERFPMGAPYTGGNIHGPPLGDLDEKISWMEKFVRRGTEITAPVPMTPSKTTGLGGFEVPSSRGSALRSDASALNVGVLHLVPTLEVFPLLADPKTYEPNTIDLSDQGEREYWLKVLSEHLPDLVDTAVASEGGTEDAKRRGDAFARAFSAHLARLMEEPAAYGKLGLANLLELREECLREFQFVDAYRSIKQRENEASLAVLPDLLEELDSMSEEARLLTLIEGVLAANIFDWGSRACVDLYHKGTIIEIYRMSRNKMQRPWRVDDFDAFKERMLGSGGKQPHRHKRALLFVDNSGADVILGMLPLAREFLRRGTEVVLVANSLPALNDVTAMELPDIVAGAAKHCDILRRAAEMGGLLVDAMVNPGDGSKKDSTSAPLMVVENGCGSPCIDLRQVSSELAAAAKDADLVVLEGMGRALHTNFNAQFQCEALKLAMVKNQRLAEKLIKGNIYDCVCRYEPPSL
Protein: MFS transporter, putative (Q4WAM1)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSCGNTNPRTQTQLTKHDVGWRRIVRNFTPSWFSVTMGTGIVSILLNTLPYNAQWLYWISVVIFAINVLLFITGCIISFLRYTLYPEIFGAMIVHSVQSMFIGTFPMGLTTIINMFCFVCVPAWGEWTRNFAWGLWIFDAILSVVTALSLPFLLYVFPLFQTYPTVTLKSYSMAHGNETQLSSMTAIWLLPIVSCIVAASSGAIVADVLPNPQHALWTVLVSYVLWGIGVPLAMMVMVIYLQRLTLHKLPPKAVIVSVFLPLGPLGQGGYGAMKLGKSAQTIFAQTHTLEASSGSTFYTLGFLVALILWSFGLVWLFFASASIARCRSFPFNIGWWGFTFPLGVFAASTCQMGRELPSEFFKMLGTVRRSYNVF
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 (Complex I-19kD) (CI-19kD) (Complex I-PGIV) (CI-PGIV) (NADH-ubiquinone oxidoreductase 19 kDa subunit) (Q9DCJ5)
Organism: Mus musculus (Mouse)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000250|UniProtKB:P51970}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P51970}. Mitochondrion {ECO:0000250|UniProtKB:P51970}.
Interaction partners:
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 subunit C2
- NADH-ubiquinone oxidoreductase chain 3
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
Sequence:
MPGIVELPTLEELKVEEVKVSSAVLKAAAHHYGAQCDKTNKEFMLCRWEEKDPRRCLKEGKLVNGCALNFFRQIKSHCAEPFTEYWTCLDYSNMQLFRHCRQQQAKFDQCVLDKLGWVRPDLGQLSKVTKVKTDRPLPENPYHSRARPEPNPVIEGDLKPAKHGTRFFFWTV
Protein: PPFIA binding protein 2 (A0A8I5ZVX1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTSDASHMLEAALEQMDGIIAGTKTAADFSDGTCEPGLSPPSSCLNSMPVLHLIEDLRLALEMLALPQEREALLSQIPGPTAAYIKEWFEDSLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAESVLNVISELQEQMCRLQLDIHRQIQERLLLARDHPEEVVAGDHEAKPQPCSRDCAPWEGSPELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSALHSDHAERDQEIHRLKMGMETLRVANEDKDRRIEELTGLLNQYLRVKEIVMATQGSSERTLSINEDEIEGSFRKWNTTSKSPEEVMKQEVSPRCSSPTPGPPPLPQKSLETRAQKKLSCSLEDLRCESGNKCINGNQTSPVGEPKDSSFLAEQKYPTLPGKLSGATPNGEAAKSPPTASLQPDSSGSSQPKLNRGWSISAPVLGDTEGGWEDIVMTNELSSTSSGTESSPQSPLTPDGKRSPKGIKKFWGKIRRTQSGNFNTDTPGMVEFRRGGLRATAGPRLSRTRDTKGQKCDANAPFAQWSTERVCTWLQDFGLAQYVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAINTKQEEKSALLDHVWVTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLHVNKFNPNCLHRRPADESNLSPSEVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALIGPEAEQEKRDKMASPAYTPLTTTAKVRPRKLGFSHFGNMRKKKFDESTDYICPMEPGDAVSDSHRVYGVYRGLSPLDNHELDGLDQMAPSEGTVTQIGLLSQDIHRLTTLLSQDQLLNDPPGCP
Protein: 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (Sks1 multidrug resistance protein homolog) (Q86IJ1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The function of the 'Lys-63'-specific deubiquitination of the proteasome is unclear (By similarity).
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 6A homolog
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 12
Sequence:
MNRSLMSLLGREGLGEKITDATPLPDTAETIHISSLALLKMLQHARAGVPLEVMGLMLGELIDEYTIRVIDVFAMPQSGTSVSVEAIDPVFQTKMLDMLKQTGRDEIVIGWYHSHPGFGCWLSSVDVNTQQSFEQLQSRAVAVVVDPLQSVRGKVVIDAFRTIKTSPTAEPRQITSNLGHLQDPSIQALIHGLNRNYYSIAINYRKNELEQKMLLNLHKKKWTEGLIVDKFDTHEQSNEKQINNLLELTKQYQKSIQDEDKIEPEKKEVSAVGKLDPKRHLISDVHTLMANNVVRVLTVMLDTVTF
Protein: Methionyl-tRNA formyltransferase, mitochondrial (MtFMT) (EC 2.1.2.9) (Q9D799)
Organism: Mus musculus (Mouse)
Function: Methionyl-tRNA formyltransferase that formylates methionyl-tRNA in mitochondria and is crucial for translation initiation.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:O77480}.
Interaction partners:
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- Dihydrofolate reductase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Trifunctional purine biosynthetic protein adenosine-3
- Serine hydroxymethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Formimidoyltransferase-cyclodeaminase
- Methionine--tRNA ligase, cytoplasmic
- Methionine synthase
Sequence:
MLLPRCCWGRWLMGRRPRCSCQAPAGFDGKDGRGSRVREKPPWRVLFLGTDHFARETLRALHAARDGKEEKLIEKLEVVTVPSLSPKGLPVKQYAIQSQLPVYEWPDVGSGEYDVGVVASFGRLLSEALILKFPYGILNVHPSCLPRWRGPAPIIHTVLHGDTVTGVTIMQIRPKRFDIGPILQQETIPVPPKSTSKELEAVLSKLGANMLISVLKNLPESLNNGRPQPAEGVTYAPKVSAGTSCVKWEEQTSEQVLRLHLAIGDIVPLQTLWMENTVKLLDLVEVNNSILADPKLTGQTVTPGFVVYHRPSQMLLVRCKDGWIGVRSVMLKKTLTATDFYNGYLHAWYQKNSHAHPSQCRFQTLRLPTKMQQKTKLLLCNSALSS
Protein: Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) (Q57ZS7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Adenylosuccinate synthetase
- GMP synthase
- Adenosine monophosphate deaminase, putative
- AMP deaminase, putative
- AMP deaminase
- Adenylosuccinate lyase
- Hypoxanthine phosphoribosyltransferase
- Hypoxanthine phosphoribosyltransferase
- Inosine-5'-monophosphate dehydrogenase
- Nucleoside diphosphatase, putative
Sequence:
MSFNESASIPTGLTYDDVLIIPQHSRVTSRKEVNTTTRLSRNVKLSIPIVASNMDTVCEQRMAVAMAREGGIGILHRFCSIEEQCAMLREVKRAQSFLIESPRIILPHETAREAWEGLNWKGRVGGVGCLLVVNCKNERKLLGIITRHDLKLADESTTVESLMTPVDKMVVSTNTSISLEEVTHLMRKGRTANVPIVGQNGQLLYLVTLSDVVKLRKNKQASLDSRGRLLVGAAVGVKKDDMNRAIRLVEAGADVLVVDIAHGHSDLCINMVKRLKGDPRTASVDIIAGNIASAEAAEALIDAGADGLKIGVGPGSICITRLVAGAGVPQLSAVLACTRVARRRGVPCIADGGLRTSGDISKAIGAGADTVMLGNMLAGTDEAPGRVLVKDGQKVKIIRGMAGFGANLSKAERERTQDEDVFSSLVPEGVEGSVACKGPVGPIVRQLVGGLRSGMSYSGAKSIEEMQRRTRFVRMTGAGLRESGSHGVAKL
Protein: 5-pentadecatrienyl resorcinol O-methyltransferase (EC 2.1.1.n7) (O-methyltransferase 3) (SbOMT3) (A8QW53)
Organism: Sorghum bicolor (Sorghum) (Sorghum vulgare)
Function: O-methyltransferase involved in the biosynthetic pathway of the phytotoxin sorgoleone, a potent broad-spectrum inhibitor active against many agronomically important monocot and dicot weed species. Substrate specificity for alkylresorcinols. Strong preference for a five carbons alkyl side chain.
Interaction partners:
Sequence:
MVLISEDSRELLQAHVELWNQTYSFMKSVALAVALDLHIADAIHRRGGAATLSQILGEIGVRPCKLPGLHRIMRVLTVSGTFTIVQPSAETMSSESDGREPVYKLTTASSLLVSSESSATASLSPMLNHVLSPFRDSPLSMGLTAWFRHDEDEQAPGMCPFTLMYGTTLWEVCRRDDAINALFNNAMAADSNFLMQILLKEFSEVFLGIDSLVDVAGGVGGATMAIAAAFPCLKCTVLDLPHVVAKAPSSSIGNVQFVGGDMFESIPPANVVLLKWILHDWSNDECIKILKNCKQAIPSRDAGGKIIIIDVVVGSDSSDTKLLETQVIYDLHLMKIGGVERDEQEWKKIFLEAGFKDYKIMPILGLRSIIELYP
Protein: T-complex protein 1 subunit theta-like 2 (Chaperonin containing T-complex polypeptide 1 subunit 8-like 2) (Q96SF2)
Organism: Homo sapiens (Human)
Function: Possible molecular chaperone; assists the folding of proteins upon ATP hydrolysis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P40227}.
Interaction partners:
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit zeta-2
- T-complex protein 1 subunit zeta
- Endoplasmic reticulum membrane-associated RNA degradation protein
- BBSome complex assembly protein BBS10
Sequence:
MDSTVPSALELPQRLALNPRESPRSPEEEEPHLLSSLAAVQTLASVIRPCYGPHGRQKFLVTMKGETVCTGCATAILRALELEHPAAWLLREAGQTQAENSGDGTAFVVLLTEALLEQAEQLLKAGLPRPQLREAYATATAEVLATLPSLAIQSLGPLEDPSWALHSVMNTHTLSPMDHLTKLVAHACWAIKELDGSFKPERVGVCALPGGTLEDSCLLPGLAISGKLCGQMATVLSGARVALFACPFGPAHPNAPATARLSSPADLAQFSKGSDQLLEKQVGQLAAAGINVAVVLGEVDEETLTLADKYGIVVIQARSWMEIIYLSEVLDTPLLPRLLPPQRPGKCQRVYRQELGDGLAVVFEWECTGTPALTVVLRGATTQGLRSAEQAVYHGIDAYFQLCQDPRLIPGAGATEMALAKMLSDKGSRLEGPSGPAFLAFAWALKYLPKTLAENAGLAVSDVMAEMSGVHQGGNLLMGVGTEGIINVAQEGVWDTLIVKAQGFRAVAEVVLQLVTVDEIVVAKKSPTHQEIWNPDSKKTKKHPPPVETKKILGLNN
Protein: histidine kinase (EC 2.7.13.3) (Q9L906)
Organism: Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MMRAVDRPEFDMSASLSHQEWVRLRTLILLRWAAVVGQLAALIAAYGYYDIALNLPMCIGTIGFAVAANIAAIYLYPESRRLSQAEVTATLLFDTAQLALLLSLTGGLNNPFALLILVPVTIAATALKLRPTLLLGGATIAMITFVAVFNEPLQTRDGAHIGLPPMIEFGSWVAIVIGVIFLGAYAHRIAQEIHSMSDALFATQMALSREQKLTDLGGVVAAAAHELGTPLATIKLVSTELAEELVDDPELHDDAVLIREQAERCRDILRSMGRAGKDDVHLRTAPLLAVLREAAEPHLDRGKMIYFDVVPGEGGSERQPTIYRYPELVHALRNLIQNAVDFAQTTVWVDAEWTDRSIIVRVTDDGRGYSPNVLNRIGDPFISTRSADAKEYEGMGLGLFIAKTLLERTGAKLRFANGSEPYQKNAPVRGSGAVVELRWHIGRLIAPETGPLGENVPITA
Protein: Leucine-rich repeat-containing protein 23 (Leucine-rich protein B7) (O35125)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:34585727, ECO:0000269|PubMed:38091523}. Cytoplasm {ECO:0000250|UniProtKB:Q53EV4}. Note=Within the sperm flagellum, may be associated with the head of radial spoke 3. {ECO:0000305|PubMed:38091523}.
Interaction partners:
- Cilia- and flagella-associated protein 263
- Translin-associated factor X-interacting protein 1
- Radial spoke head protein 3 homolog B
- Cilia- and flagella-associated protein 161
- Cilia- and flagella-associated protein 52
- Leucine-rich repeat-containing protein 34
Sequence:
MSDEDDVDDVDAEQDEVESDKEIEEWEDYRKETEEASEEWLPTPITEAMMKEGLSLLCKIGSGLAHAYIKLEAKDRDLTDISLLRSYIHLRYVDISENHITDISPLNSLTHLLWLKADGNQLRSARMNELPYLQIASFSYNQIIDTEGIFHPRLGSLDLKGNRIHQVTGLDPERLSSLHTLELRGNQLESTKGIYLPKLKNLYLAQNLLKKVEGLENLSNLTTLHLRDNQIETLNGFSQEMKSLQYLNLRSNMISDLAELAKLRDLPKLRALVLLDNPCADETDYRQEALVQMAHLERLDKEFYEDDDRAEAEEIRQRLKEEQDQDLDPDQDMEPYLPPV