wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein mS86 (AtRBG6) (Glycine-rich RNA-binding protein 6, mitochondrial) (AtGR-RBP6) (Q9FZ84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possibly has a role in RNA transcription or processing during stress.
Subcellular location: Mitochondrion {ECO:0000250, ECO:0000303|PubMed:36423343}.
Interaction partners:
- tRNA-specific adenosine deaminase TAD2
- Membrane fusion protein Use1
- Protein DEHYDRATION-INDUCED 19 homolog 7
- Calcium uptake protein, mitochondrial
- Probable receptor-like protein kinase At1g30570
Sequence:
MHYMGLFSRAGNIFRQPRALQASNAMLQGNLSLTPSKIFVGGLSPSTDVELLKEAFGSFGKIVDAVVVLDRESGLSRGFGFVTYDSIEVANNAMQAMQNKELDGRIIGVHPADSGGGGGGGGFARRGGYGGGRGGYARGGFGRGGFGGGGYGFVR
Protein: Fumarate hydratase class II (Fumarase C) (EC 4.2.1.2) (Aerobic fumarase) (Iron-independent fumarase) (P9WN93)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305}.
Interaction partners:
- Malate synthase G
- Succinate dehydrogenase flavoprotein subunit
- Malate dehydrogenase
- Putative malate oxidoreductase
- Citrate synthase 1
- Fumarate reductase flavoprotein subunit
- Probable succinate dehydrogenase [iron-sulfur subunit]
- Probable malate:quinone oxidoreductase
- Putative citrate synthase 2
- Succinate dehydrogenase 2 membrane subunit SdhC
Sequence:
MAVDADSANYRIEHDTMGEVRVPAKALWRAQTQRAVENFPISGRGLERTQIRALGLLKGACAQVNSDLGLLAPEKADAIIAAAAEIADGQHDDQFPIDVFQTGSGTSSNMNTNEVIASIAAKGGVTLHPNDDVNMSQSSNDTFPTATHIAATEAAVAHLIPALQQLHDALAAKALDWHTVVKSGRTHLMDAVPVTLGQEFSGYARQIEAGIERVRACLPRLGELAIGGTAVGTGLNAPDDFGVRVVAVLVAQTGLSELRTAANSFEAQAARDGLVEASGALRTIAVSLTKIANDIRWMGSGPLTGLAEIQLPDLQPGSSIMPGKVNPVLPEAVTQVAAQVIGNDAAIAWGGANGAFELNVYIPMMARNILESFKLLTNVSRLFAQRCIAGLTANVEHLRRLAESSPSIVTPLNSAIGYEEAAAVAKQALKERKTIRQTVIDRGLIGDRLSIEDLDRRLDVLAMAKAEQLDSDRL
Protein: BAG family molecular chaperone regulator 2 (BAG-2) (Bcl-2-associated athanogene 2) (Q91YN9)
Organism: Mus musculus (Mouse)
Function: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release.
Interaction partners:
- Heat shock cognate 71 kDa protein
- E3 ubiquitin-protein ligase CHIP
- Heat shock protein 105 kDa
- Heat shock 70 kDa protein 1B
- BAG family molecular chaperone regulator 1
- Hsp70-binding protein 1
- Heat shock 70 kDa protein 4L
- BAG family molecular chaperone regulator 3
- Small glutamine-rich tetratricopeptide repeat-containing protein alpha
- Heat shock protein HSP 90-beta
Sequence:
MAQAKISAKAHEGRFCRSSSMADRSSRLLESLDQLELRVEALRDAATAVEQEKEILLEMIHSIQNSQDMRQISDGEREELNLTANRLMGRTLTVEVSVETIRNPQQEESLKHATRIIDEVVSKFLDDLGNAKSHLMSLYSACSSEVPPGPVDQKFQSIVIGCALEDQKKIKRRLETLLRNIDNSDKAIKLLEHAKGAGSKSLQNTDGKFN
Protein: MAPK/MAK/MRK overlapping kinase (EC 2.7.11.22) (MOK protein kinase) (Renal tumor antigen 1) (RAGE-1) (Q9UQ07)
Organism: Homo sapiens (Human)
Function: Able to phosphorylate several exogenous substrates and to undergo autophosphorylation. Negatively regulates cilium length in a cAMP and mTORC1 signaling-dependent manner.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9WVS4}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9WVS4}. Nucleus {ECO:0000250|UniProtKB:Q9WVS4}.
Interaction partners:
- DNA replication licensing factor MCM2
- Cell division control protein 6 homolog
- DNA replication factor Cdt1
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM6
- Origin recognition complex subunit 2
- Origin recognition complex subunit 4
- Origin recognition complex subunit 5
Sequence:
MKNYKAIGKIGEGTFSEVMKMQSLRDGNYYACKQMKQRFESIEQVNNLREIQALRRLNPHPNILMLHEVVFDRKSGSLALICELMDMNIYELIRGRRYPLSEKKIMHYMYQLCKSLDHIHRNGIFHRDVKPENILIKQDVLKLGDFGSCRSVYSKQPYTEYISTRWYRAPECLLTDGFYTYKMDLWSAGCVFYEIASLQPLFPGVNELDQISKIHDVIGTPAQKILTKFKQSRAMNFDFPFKKGSGIPLLTTNLSPQCLSLLHAMVAYDPDERIAAHQALQHPYFQEQRKTEKRALGSHRKAGFPEHPVAPEPLSNSCQISKEGRKQKQSLKQEEDRPKRRGPAYVMELPKLKLSGVVRLSSYSSPTLQSVLGSGTNGRVPVLRPLKCIPASKKTDPQKDLKPAPQQCRLPTIVRKGGR
Protein: Secondary thiamine-phosphate synthase enzyme (T22I11.11 protein) (Q9LPU1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Superoxide dismutase 1, mitochondrial
Sequence:
MVMMVKVKGLIGRFWFGVGGGIVLAIVVVIIGLRGTQKAMSSTFLFSGVVPLRVRSVLTPANPATDRASMASSSGAKWAQKTITLPPLRRGCHLITPKILKEIREDLSDFNCGLAHVFLQHTSASLTINENYDPDVQADTETFLNRIVPEGNSAPWRHTMEGPDDMPAHIKSSMFGCQLTIPITKGKLSMGTWQGIWLCEHRDAPTARRVVVTLNGI
Protein: Small ribosomal subunit protein eS1 (40S ribosomal protein S3a) (V-fos transformation effector protein) [Cleaved into: 40S ribosomal protein S3b] (P49242)
Organism: Rattus norvegicus (Rat)
Function: May play a role during erythropoiesis through regulation of transcription factor DDIT3.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P97351, ECO:0000255|HAMAP-Rule:MF_03122}. Nucleus {ECO:0000250|UniProtKB:P97351, ECO:0000255|HAMAP-Rule:MF_03122}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P61247}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P97351}.
Interaction partners:
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS15
Sequence:
MAVGKNKRLTKGGKKGAKKKVVDPFSKKDWYDVKAPAMFNIRNIGKTLVTRTQGTKIASDGLKGRVFEVSLADLQNDEVAFRKFKLITEDVQGKNCLTNFHGMDLTRDKMCSMVKKWQTMIEAHVDVKTTDGYLLRLFCVGFTKKRNNQIRKTSYAQHQQVRQIRKKMMEIMTREVQTNDLKEVVNKLIPDSIGKDIEKACQSIYPLHDVFVRKVKMLKKPKFELGKLMELHGEGGSSGKTTGDETGAKVERADGYEPPVQESV
Protein: Large ribosomal subunit protein eL14A (60S ribosomal protein L14-A) (P36105)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS7A
- Large ribosomal subunit protein eL20A
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL6A
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein eL6B
- Large ribosomal subunit protein uL13A
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL32
Sequence:
MSTDSIVKASNWRLVEVGRVVLIKKGQSAGKLAAIVEIIDQKKVLIDGPKAGVPRQAINLGQVVLTPLTFALPRGARTATVSKKWAAAAVCEKWAASSWAKKIAQRERRAALTDFERFQVMVLRKQKRYTVKKALAKA
Protein: Aromatic-amino-acid aminotransferase (ARAT) (AROAT) (EC 2.6.1.57) (Beta-methylphenylalanine transaminase) (EC 2.6.1.107) (P04693)
Organism: Escherichia coli (strain K12)
Function: Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin produced by Streptomyces hygroscopicus NRRL3085.
Subcellular location: Cytoplasm.
Interaction partners:
- Bifunctional chorismate mutase/prephenate dehydratase
- T-protein
- Histidinol-phosphate aminotransferase
- Hydroxycarboxylate dehydrogenase B
- Aspartate aminotransferase
- Methionine synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- S-adenosylmethionine synthase
- Catalase-peroxidase
- Homocysteine S-methyltransferase
Sequence:
MFQKVDAYAGDPILTLMERFKEDPRSDKVNLSIGLYYNEDGIIPQLQAVAEAEARLNAQPHGASLYLPMEGLNCYRHAIAPLLFGADHPVLKQQRVATIQTLGGSGALKVGADFLKRYFPESGVWVSDPTWENHVAIFAGAGFEVSTYPWYDEATNGVRFNDLLATLKTLPARSIVLLHPCCHNPTGADLTNDQWDAVIEILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPALVSNSFSKIFSLYGERVGGLSVMCEDAEAAGRVLGQLKATVRRNYSSPPNFGAQVVAAVLNDEALKASWLAEVEEMRTRILAMRQELVKVLSTEMPERNFDYLLNQRGMFSYTGLSAAQVDRLREEFGVYLIASGRMCVAGLNTANVQRVAKAFAAVM
Protein: Protein CONSERVED ONLY IN THE GREEN LINEAGE 160, chloroplastic (AtCGL160) (O82279)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Facilitates the assembly of the membrane proton channel of the chloroplastic F-type ATPase. Specifically required for the efficient assembly and integration of the CF(0) subunit c into the chloroplastic ATPase complex in the thylakoid membrane.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:24664203}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ALBINO3-like protein 1, chloroplastic
- Kinesin-like protein KIN-7D, mitochondrial
- K
- AT1G30475 protein
- Ubiquitin-like protein 5
Sequence:
MAILSYISATSTTPPIPQDQSPNSRLPTKIILPNKKPEKWSTGVAPGEYGGPPTTTKLRKYWGGEKEDPITSTDLIWNRDFMDQMKKLFDDPNDSSLDPSPSKEKSSGFLSFSRVMSLDSMDVDLSKELASSSKSVVKNRLDTSKSEAKKQMSKAIVSPKWKLAPTRREQEKWDRATKAATGGSDVMFRELRRPRGDPEVQAAKDREQYFKLKNKIQVLTLGIGGVGLVSAYISYTPEIALSFGAGLLGSLAYMRMLGNSVDAMADGARGVAKGAANQPRLLVPVVLVMIFNRWNAILVPEYGFMHLELIPMLVGFFTYKIATFFQAIEEAISITTQKPESISPDTQASD
Protein: Aspartyl protease family protein 2 (EC 3.4.23.-) (Q9LNJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aspartyl protease. Not able to cleave BAG6.
Interaction partners:
- Uncharacterized protein
- Protein PHOX1
- AIG2-like protein D
- Alcohol dehydrogenase-like protein
- Alcohol dehydrogenase-like protein
- TORTIFOLIA1-like protein 3
Sequence:
MVGRRKALLFSLCFFFLSLPSFSSLPSFQTLFPNSHSLPCASPVSFQPDSDSESLLESEFESGSDSESSSSITLNLDHIDALSSNKTPDELFSSRLQRDSRRVKSIATLAAQIPGRNVTHAPRPGGFSSSVVSGLSQGSGEYFTRLGVGTPARYVYMVLDTGSDIVWLQCAPCRRCYSQSDPIFDPRKSKTYATIPCSSPHCRRLDSAGCNTRRKTCLYQVSYGDGSFTVGDFSTETLTFRRNRVKGVALGCGHDNEGLFVGAAGLLGLGKGKLSFPGQTGHRFNQKFSYCLVDRSASSKPSSVVFGNAAVSRIARFTPLLSNPKLDTFYYVGLLGISVGGTRVPGVTASLFKLDQIGNGGVIIDSGTSVTRLIRPAYIAMRDAFRVGAKTLKRAPDFSLFDTCFDLSNMNEVKVPTVVLHFRGADVSLPATNYLIPVDTNGKFCFAFAGTMGGLSIIGNIQQQGFRVVYDLASSRVGFAPGGCA
Protein: Nuclear factor of activated T cells 3 (I3L3K7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTANCGAHDELDFKLVFGEDGAPAPPPPGSRPADLEPDDCASIYIFNVDPPPSTLTTPLCLPHHGLPSHSSVLSPSFQLQSHKNYEGTCEIPESKYSPLGGPKPFECPSIQITSISPNCHQELDAHEDDLQINDPEREFLERPSRDHLYLPLEPSYRESSLSPSPASSISSRSWFSDASSCESLSHIYDDVDSELNEAAARFTLGSPLTSPGGSPGGCPGEETWHQQYGLGHSLSPRQSPCHSPRSSVTDENWLSPRPASGPSSRPTSPCGKRRHSSAEVCYAGSLSPHHSPVPSPGHSPRGSVTEDTWLNASVHGGSGLGPAVFPFQYCVETDIPLKTRKTSEDQAAILPGKLELCSDDQGSLSPARETSIDDGLGSQYPLKKDSCGDQFLSVPSPFTWSKPKPGHTPIFRTSSLPPLDWPLPAHFGQCELKIEVQPKTHHRAHYETEGSRGAVKASTGGHPVVKLLGYNEKPINLQMFIGTADDRYLRPHAFYQVHRITGKTVATASQEIIIASTKVLEIPLLPENNMSASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGKVLSLQIASIPVECSQRSAQELPHIEKYSINSCSVNGGHEMVVTGSNFLPESKIIFLEKGQDGRPQWEVEGKIIREKCQGAHIVLEVPPYHNPAVTAAVQVHFYLCNGKRKKSQSQRFTYTPVLMKQEHREEIDLSSVPSLPVPHPAQTQRPSSDSGCSHDSVLSGQRSLICSIPQTYASMVTSSHLPQLQCRDESVSKEQHMIPSPIVHQPFQVTPTPPVGSSYQPMQTNVVYNGPTCLPINAASSQEFDSVLFQQDATLSGLVNLGCQPLSSIPFHSSNSGSTGHLLAHTPHSVHTLPHLQSMGYHCSNTGQRSLSSPVADQITGQPSSQLQPITYGPSHSGSATTASPAASHPLASSPLSGPPSPQLQPMPYQSPSSGTASSPSPATRMHSGQHSTQAQSTGQGGLSAPSSLICHSLCDPASFPPDGATVSIKPEPEDREPNFATIGLQDITLDDGFVKAEKPLSHD
Protein: Methionine synthase (EC 2.1.1.13) (5-methyltetrahydrofolate--homocysteine methyltransferase) (Methionine synthase, vitamin-B12 dependent) (MS) (O33259)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity).
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Conserved protein
- Cystathionine gamma-synthase
- Probable O-acetylhomoserine sulfhydrylase MetC
- O-succinylhomoserine sulfhydrylase
- Adenosylhomocysteinase
- S-adenosylmethionine synthase
- Aminomethyltransferase
- Homoserine dehydrogenase
- S-methylmethionine:homocysteine methyltransferase
Sequence:
MTAADKHLYDTDLLDVLSQRVMVGDGAMGTQLQAADLTLDDFRGLEGCNEILNETRPDVLETIHRNYFEAGADAVETNTFGCNLSNLGDYDIADRIRDLSQKGTAIARRVADELGSPDRKRYVLGSMGPGTKLPTLGHTEYAVIRDAYTEAALGMLDGGADAILVETCQDLLQLKAAVLGSRRAMTRAGRHIPVFAHVTVETTGTMLLGSEIGAALTAVEPLGVDMIGLNCATGPAEMSEHLRHLSRHARIPVSVMPNAGLPVLGAKGAEYPLLPDELAEALAGFIAEFGLSLVGGCCGTTPAHIREVAAAVANIKRPERQVSYEPSVSSLYTAIPFAQDASVLVIGERTNANGSKGFREAMIAEDYQKCLDIAKDQTRDGAHLLDLCVDYVGRDGVADMKALASRLATSSTLPIMLDSTETAVLQAGLEHLGGRCAINSVNYEDGDGPESRFAKTMALVAEHGAAVVALTIDEEGQARTAQKKVEIAERLINDITGNWGVDESSILIDTLTFTIATGQEESRRDGIETIEAIRELKKRHPDVQTTLGLSNISFGLNPAARQVLNSVFLHECQEAGLDSAIVHASKILPMNRIPEEQRNVALDLVYDRRREDYDPLQELMRLFEGVSAASSKEDRLAELAGLPLFERLAQRIVDGERNGLDADLDEAMTQKPPLQIINEHLLAGMKTVGELFGSGQMQLPFVLQSAEVMKAAVAYLEPHMERSDDDSGKGRIVLATVKGDVHDIGKNLVDIILSNNGYEVVNIGIKQPIATILEVAEDKSADVVGMSGLLVKSTVVMKENLEEMNTRGVAEKFPVLLGGAALTRSYVENDLAEIYQGEVHYARDAFEGLKLMDTIMSAKRGEAPDENSPEAIKAREKEAERKARHQRSKRIAAQRKAAEEPVEVPERSDVAADIEVPAPPFWGSRIVKGLAVADYTGLLDERALFLGQWGLRGQRGGEGPSYEDLVETEGRPRLRYWLDRLSTDGILAHAAVVYGYFPAVSEGNDIVVLTEPKPDAPVRYRFHFPRQQRGRFLCIADFIRSRELAAERGEVDVLPFQLVTMGQPIADFANELFASNAYRDYLEVHGIGVQLTEALAEYWHRRIREELKFSGDRAMAAEDPEAKEDYFKLGYRGARFAFGYGACPDLEDRAKMMALLEPERIGVTLSEELQLHPEQSTDAFVLHHPEAKYFNV
Protein: Zinc transporter ZupT (Divalent metal ion transporter ZupT) (Zinc uptake transporter) (P0A8H3)
Organism: Escherichia coli (strain K12)
Function: Mediates zinc uptake. Has broad metal specificity and can also mediate the uptake of cadmium, cobalt, iron, manganese and possibly copper. Has a slight preference for zinc.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00548, ECO:0000269|PubMed:20225068, ECO:0000269|PubMed:34793140}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00548}.
Interaction partners:
- Zinc/cadmium/lead-transporting P-type ATPase
- Zinc transporter ZitB
- Divalent metal cation transporter MntH
- Zinc import ATP-binding protein ZnuC
- High-affinity zinc uptake system protein ZnuA
- High-affinity zinc uptake system membrane protein ZnuB
- Metal-binding protein ZinT
- Cation-efflux pump FieF
- Transcriptional regulator MntR
- Fe
Sequence:
MSVPLILTILAGAATFIGAFLGVLGQKPSNRLLAFSLGFAAGIMLLISLMEMLPAALAAEGMSPVLGYGMFIFGLLGYFGLDRMLPHAHPQDLMQKSVQPLPKSIKRTAILLTLGISLHNFPEGIATFVTASSNLELGFGIALAVALHNIPEGLAVAGPVYAATGSKRTAILWAGISGLAEILGGVLAWLILGSMISPVVMAAIMAAVAGIMVALSVDELMPLAKEIDPNNNPSYGVLCGMSVMGFSLVLLQTAGIG
Protein: Floral homeotic protein PISTILLATA (Transcription factor PI) (P48007)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in the genetic control of flower development. Is required for normal development of petals and stamens in the wild-type flower. Forms a heterodimer with APETALA3 that is required for autoregulation of both AP3 and PI genes. AP3/PI heterodimer interacts with APETALA1 or SEPALLATA3 to form a ternary complex that could be responsible for the regulation of the genes involved in the flower development. AP3/PI heterodimer activates the expression of NAP. AP3/PI prevents GATA22/GNL and GATA21/GNC expression.
Subcellular location: Nucleus.
Interaction partners:
- Floral homeotic protein APETALA 3
- MATH domain and coiled-coil domain-containing protein At3g29580
- F-box/kelch-repeat protein At3g44120
- Putative F-box protein At1g64540
- B3 domain-containing protein REM2
- Protein CRABS CLAW
- Transcription factor IND
- Floral homeotic protein AGAMOUS
Sequence:
MGRGKIEIKRIENANNRVVTFSKRRNGLVKKAKEITVLCDAKVALIIFASNGKMIDYCCPSMDLGAMLDQYQKLSGKKLWDAKHENLSNEIDRIKKENDSLQLELRHLKGEDIQSLNLKNLMAVEHAIEHGLDKVRDHQMEILISKRRNEKMMAEEQRQLTFQLQQQEMAIASNARGMMMRDHDGQFGYRVQPIQPNLQEKIMSLVID
Protein: Uncharacterized protein (Q587C2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Trans-sialidase
- Ribosomal protein S23 mitochondrial conserved domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Rhodanese domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- 30S ribosomal protein S8, putative
- Uncharacterized protein
Sequence:
MRKFCHFMANCWNSARSHATYGAVPLTHSQVTSVYATDGGKVDELGLLELVEERIFSWKLNKWEMRIPPNLPNDQKELIRQEQENLKQILSGWRKCFGALNADILQISSLTGVPKEVVREKNRTWLQEEVAKLRWMGEVNKAALLRDAFMRLEAFGSRDFMFMERLCCIYGLARQGTFDEAFTNYITEDPVTNDIFVDERNPFKELVAHIVRNYSQIDIIYDFLGFNYSEGYRSSLRRYMEYLQCKTAENVRASGRLVTGDKGEHNILFDYCVSRESLVSGDSCQGIIDFLYINGNDVTLIIIASDNPWLRNRQLPHRRQMEGIARRVCFVLGIPPSEVRIRNLLLPPTYLDKGSIVRLNDIVFRLSNEQSNLLIPWLTNYNKELDPKDVDYTALAKTTNEEEWLTL
Protein: Uncharacterized protein (Q54X71)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MKLNLCLIILSLSLIGLTRSTQISDEYVNFVAFSDSECLTPALNGFGYSMATKTCTTLDYINNFLFTVDSGEVSWGSYENNYYEGETCTLPNSPSVSYPVNSCIQSSTVYINMNSGKTNTPFYYKLTTSSTPYIAQNSFIYTYMGEQCSPNNIVALEYYLNDTRLFKNLSSYLYYCDPNTHFPVTQFCADYPSECNPPPSQNQPHCFATQPFYNTSGDSSITSICPTCCTSGSSCATSGGSTGSYTGEGWSKPENEKQQIIKLEKQDKPFTVTNSNDQIAYYKYLYCS
Protein: DNA topoisomerase 2-alpha (EC 5.6.2.2) (DNA topoisomerase II, alpha isozyme) (O42130)
Organism: Gallus gallus (Chicken)
Function: Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand (By similarity). May play a role in the regulation of circadian rhythm (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11388}.
Interaction partners:
- DNA topoisomerase I
- Uncharacterized protein.
- G2/mitotic-specific cyclin-B2
- Cyclin-dependent kinase 1
- FHA domain-containing protein.
- DNA topoisomerase I
- Structural maintenance of chromosomes protein 2
- Ubiquitin-conjugating enzyme E2 C
- Nucleolar and spindle-associated protein 1
- DLG associated protein 5.
Sequence:
MELLDSPAPLRPLHDNPRLPKADGAQKRLSVERIYQKKTQLEHILLRPDTYIGSVETVTQQMWVFDEDVGLNCRDVTFVPGLYKIFDEILVNAADNKQRDKSMSCIKVTIDPENNTISVWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACREYKKLFKQTWTDNMGKAGEMTLKHFDGEDYTCVTFQPDLSKFKMTILDKDIVALMSRRAYDIAGSTKDVKVFLNGKRLPVKGFRSYVDLYLKDKVDETGNALKVIHEEVNSRWEVCLTLSEKGFQQVSFVNSIATTKGGRHVDYVADQIVTKLIDVVKKKNKNGVGVKPFQVKNHMWIFVNSLIENPTFDSQTKENMTLQAKSFGSTCKLSEKFIKGAVGCGIVESILNWVKFKAQTQLNKKCSAVKHTKIKGVPKLDDANDAGSKNSIDCTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKMLNVREASHKQIMENAEINNIIKIVGLQYKKNYEDRESLKSLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHNFLEEFITPIIKVSKNKEEIPFYSIPEFEEWKSSTQNYNSWKIKYYKGLGTSTSKEAKEYFADMARHRIGFKYSGPEDDAAITLAFSKKKVEERKEWLTNFMEDRRQRNVHGLPEDYLYGKDTNYLTYNDFINKELVLFSNSDNERSIPSLVDGLKPGQRKVLFTCFKRNDKREVKGAQLAGSVAEMSSYHHGEASLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSPLARLLFPPVDDNVLRFLYDDNQRVEPEWYMPIIPMVLINGAEGIGTGWSCKIPNFDIRETVNNIRCLLDGKEPLPMLPSYKNFKGTIDELGPNQYVISGEVSILDSTTIEITELPVRTWTQTYKEQVLEPMLNGTEKTPPLITDYKEYHTDTTVKFVVKMSEEKLAEAEAVGLHKVFKLQTNLTCNSMVLFDHVGFLKKYESPQDILKEFFELRLRYYGLRKEWLIGMLGAESAKLNNQARFILEKIDGKIVIENKPKKELIQVLIQRGYESDPVKAWKELQNKEEEEGDESGEESAAATGPDFNYLLNMPLWYLTKEKKDELCKQRDNKDKELEDLKHKSPSDLWKEDLAAFVEELDAVEAKQMQDEMAGITGKPLKVKGGKQGGKQKVTKAQLAEVMPSPHGIRVVPRVTAEMKAEAEKRIKKKIKSEKNESDEKQEGNSSGDKEPSSLKQRLAQKRKAEQGTKRQTTLPFKPIKKMKRNPWSDSESDSESDDFEVPSKRERVVRQAAAKIKPMVNSDSDADLTSSDEDSEYQENSEGNTDSDTTSKKKPPKAKAVPKEKKGKAPKEKPLPDAVPVRVQNVAAESASQDPAAPPVSVPRAQAVPKKPAAAKKGSTAKDNQPSIMDILTKKKAAPKAPRRAQREESPPSEATAAVAKKPGPPRGRKATKRLTSSSDSDSDFGSRPSKSVAAKKSKRDDDDSYSIDLTADSPAAAAPRTRPGRLKKPVQYLESSDEDDMF
Protein: Signal peptidase complex subunit 2 (Q59SJ1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Signal peptidase complex catalytic subunit SEC11
- Signal peptidase subunit 3
- Mitochondrial inner membrane protease subunit
- Mitochondrial inner membrane protease subunit
- Protein-arginine omega-N methyltransferase
- Alpha-1,3/1,6-mannosyltransferase ALG2
- Avt1p
Sequence:
MSQLKKTNLNSVNDLRQTTDDHLGLVFQQLGYNESFTLIDLKLGLGLSTVVIAGLLFLVDKKYAWKDSYNLTVIACVLYGIISGVLYLINFFNKNVKYIGYDNKGNKLSVATSSNKLDPIYNVTISLNDRSVNAAFGFNKFFDVVGFFNRDAFTKLVENELNKLNKKNE
Protein: C-type lectin domain family 4 member F (C-type lectin superfamily member 13) (C-type lectin 13) (Kupffer cell receptor) (P70194)
Organism: Mus musculus (Mouse)
Function: Receptor with an affinity for galactose and fucose. Could be involved in endocytosis.
Subcellular location: Membrane; Single-pass type II membrane protein.
Interaction partners:
- V-set and immunoglobulin domain containing 4
- CD5 antigen-like
- T-cell immunoglobulin and mucin domain-containing protein 4
Sequence:
MKEAELNRDMARYCTDNQCVSLQPQGLGPKSAALMAPRTLRHVQVILALMVVTVIFSLLALFVVASQPWRPEWNKEPPSLLLRGSNNSGHDNHSQFVRETEMQVAIQRLRDYEENSSSCHKEVQILKYQMDNVSSLVQLLGSHLEDVNADILQTKDVLKESGALALETQALRSSLEVASADIHSLRGDLEKANAMTSQTRGLLKSSTENTSAELHVLGRGLEEAQSEIQALRGSLQSANDLSSQTQGFLQHSMDNISAQIQTVRDGMERAGEKMNSLKKELETLTAQTQKANGHLEQTDAQIQGLKAELKSTSSLNSRIEVVNGQMKDASRELQTLRRDLSDVSALKSNVQMLQSNLQRAKTEMQTLKADLQATKALTAKIQGEQNRLGALQEAVAAQKQEQKTQNQVLQLIAQNWKYFNGNFYYFSRDKKPWREAEKFCTSQGAHLASVTSQEEQAFLVQTTSSGDHWIGLTDQGTEGIWRWVDGTPFNNAQSKGFWGKNQPDNWRHRNGEREDCVHVRQQWNDMACGSSYPWVCKKSTGWSAARVG
Protein: Transcriptional activator HAP2 (P06774)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts a component of the CCAT-binding factor, which is a transcriptional activator and binds to the upstream activation site (UAS2) of the CYC1 gene and other genes involved in mitochondrial electron transport and activates their expression. Recognizes the sequence 5'-CCAAT-3'. HAP2 has primarily a structural role in the HAP complexes I and II.
Subcellular location: Nucleus.
Interaction partners:
- Transcriptional activator HAP5
- Transcriptional activator HAP3
- Transcriptional activator HAP4
- AP-1-like transcription factor YAP5
Sequence:
MSADETDAKFHPLETDLQSDTAAATSTAAASRSPSLQEKPIEMPLDMGKAPSPRGEDQRVTNEEDLFLFNRLRASQNRVMDSLEPQQQSQYTSSSVSTMEPSADFTSFSAVTTLPPPPHQQQQQQQQQQQQQQLVVQAQYTQNQPNLQSDVLGTAIAEQPFYVNAKQYYRILKRRYARAKLEEKLRISRERKPYLHESRHKHAMRRPRGEGGRFLTAAEIKAMKSKKSGASDDPDDSHEDKKITTKIIQEQPHATSTAAAADKKT
Protein: Adenylyl-sulfate kinase (EC 2.7.1.25) (ATP adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenosine-5'-phosphosulfate kinase) (APS kinase) (Q9P7G9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the synthesis of activated sulfate. Required for methionine synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Sulfate adenylyltransferase
- Probable phosphoadenosine phosphosulfate reductase
- Sulfite reductase subunit beta
- 3'
- Probable FAD synthase
- Elongation factor Tu
- Probable sulfite reductase flavoprotein component
- Siroheme biosynthesis protein met8
- Inorganic pyrophosphatase
- Eukaryotic peptide chain release factor GTP-binding subunit
Sequence:
MATNITFHPGSVTKEERIKFVGHPGMTIWMTGLSASGKSTIACALEQYLLQRGVTTYRLDGDNVRFGLNSDLGFSEQDRNENIRRIGHVAKLFADACVVAVTSFISPYRKDRDQAREFHKKDGLPFIEVYVECPVEVAEQRDPKGLYKRARAGEIKEFTGISAPYEAPISPEIVVSSHTQSIEECVEKIVNYLLEKDLITLK