wanglab/gogpt-training-data huggingface dataset:
Protein: CG17766 (Q2XXU2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VVLWGPTAPTHCISSVFLSDDQFTLVTGCYDGQICLWQVEPTTLKMSPRCLLVGHSAPVLCLVRASLLPENNFLVSSSENGEMCTWDLTDGKCMEAVKLPQVHTQIQSYHTANSEDVRLFCIGYYAEIMVMDPFSLEVIYVLSSKVKPDWISAIHVLRPMRRKDDVVLAITTTGTVKVWTLTGNENKHAEPIYENESKEIRCLNAITMNCCAQNQRTVLLVCTKYWQIYDAGDFTVLCSVIAPARERWQGGDFITSDRVMLWTDEGKGYLYKLPANCIPDNKEFHSKSVVRDAPYLYYVLQHAGDKVLSCPPAMKLLQGAGGQHNLLRGDSEGYISVWNVPEVPLDNISILQAKQMPPRPLKPHVCTSLVEAWSIMDPPPVGILDQLSRITESPVKLTSSIYLPQQSRLVIGREDGSIVIVPATQTVMMQLLVGIKQNFSDWPSHQILYGHRGRVNCLLCPSMIHSRYEKSHLLSGGIDFAVCLWDLYSGSLLHRFCVHAGEITQLLVPPESCSPRILKCICSVASDHSVTLVSLQERKCVTLASRHLFPVVTIKWRPLDDFLIVGCSDGSVYVWQMETGHLDRVLHGMLAEEVLSACDEQAEDGGSGGGGGSNGASASEMGMANPAVHFFRGLKSRNMNAIRHATQRGITQLQQLQGHNQGNFDFLMKHRSNPLVIQGLRTNPKDAESHILFFDIEGLIFELHSEEYAQMTPATLESLGVHLQNPKDGKSMHLDASKKIGDFFNKVKNKAVDVEKILKDKDKHGLVQKFKEKTEIVEKKVQAKVESLQKAVEPHEEQQDLKSKIASKMEVTHVMEVAQLLLSLLHSWGLDPHLDKMCETRLGLLRPIVPISYGVLSKAGYMSLLLPTWQNNYAIPPGIQLPSSSKKRPLPEELQRLEHLTAVFTSRLHWELSTTLTTNHILALVAMSNTLLSMSAASFLPDSEKHKKLQRLAQRTDSTLSNEEEREELMAHHISQIKHAWSLLATHHCFLLPDKIEALEPKKFKRPQVEMMVKRWQHHCIEIREAAQQILLGELTRMGKKGRKQLVESWAQYLPLYTHTEPIVGAQQQLALISQPASGGAGSGSGGNGGVGVGVSGGGGAGSGSGPGGSVPGGDAHQDEDYEEEEEEIIRKPSSLSELKRKQTTAVILLGVIGAEFGQDISQESPNHRGSISMATGANLTSGVAGGERRKSSVVEGFGIANNLARLTSMALAHLLYAPPSPKLPQYTPLRRAAIDLLGRGFTVWEPYLDVSKVLLGLLEISCEGKAVPNLNYKLPLTPQADACRTARHALRLIATARPAAFITTMAREVARYNTMQQNAQSINTPLTQSVLHKAKGEILQCVEMLIDKMQSEIAGLLVEVMDIALHCVDGNELKNRGLAELCPAICKFNQISHCAQTRRIAVGANSGNLAIYELRQNKCQMIPAHTHPITSLAFSPDGKYLVSYSCAENRLSFWQTSTGMFGLGQSQTRCTKGYSTAPIPDVSRLNPMRLAKLVWINNRTVTLM
Protein: Bifunctional sesquiterpene synthase 1 (Alpha-copaene synthase) (EC 4.2.3.133) (Delta-cadinene synthase) (EC 4.2.3.-) (Terpene synthase 1) (LdTPS1) (J7LP58)
Organism: Phyla dulcis (Aztec sweet herb) (Lippia dulcis)
Function: Sesquiterpene synthase converting farnesyl diphosphate to alpha copaene and delta-cadinene as the major products.
Interaction partners:
Sequence:
MALAKESSIVVSSSPDVTHNITRPVASYHPNVWGDRFLLSSSDQVQLTMKARDDKVVVDELKKEVRRKLKEASNDYIRLLQTVDVIQRLGLAYHFEEEIDQALRYLFETFHDYSEDSQDMYANSLSFRLLRQHGYRISCEIFEKFKDANGGFKIPNIEGVMGMLEFYEATHLRVRGEDILDHGFVFSRNYLKSVLPSLSNPLAAQVDRALNQNSNRRGLPRLEARHFMSVYEQYASHDQALLKLAKLNFNILQSLHKVELSEISRWWKGVDIARNFPYARDRIVELYFWVLGVYFEPQYAVGRKITTKVIAIASLLDDTFDAYGTFEELRIFAEAVERWSVSCLDQLPEYMKLLYKTMLEVSDEIEEEMTKLGTPFRIAYGIEAIKTFARSYFLEAKWREEKYKPTTEEYMGLATKTCGYKSLIITSFLAMGDIPKREHFDWVLSDPDFVMASCIICRLADDIVGHEFEQTRDHIPSSVECYTQEHKTSKEDAVNELYDRLESAWKDLNEGFLRPTKIPAALLYRVLNYCRIIEVMYSRGDWYTHVGPEMQGFVRQLLVDPVPE
Protein: Mycothiol S-conjugate amidase (EC 3.5.1.115) (A0R2W9)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: A mycothiol (MSH, N-acetyl-cysteinyl-glucosaminyl-inositol) S-conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine conjugate and the MSH precursor. Involved in MSH-dependent detoxification of a number of alkylating agents and antibiotics. Activity is specific for the mycothiol moiety.
Interaction partners:
- L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
- D-inositol 3-phosphate glycosyltransferase
- Secreted protein
- Spermatogenesis-associated protein 20-like TRX domain-containing protein
- Chorismate synthase
- Uncharacterized protein
- DUF4307 domain-containing protein
- DUF3151 domain-containing protein
- Steroid delta-isomerase
Sequence:
MSELRLMAVHAHPDDESSKGAATTARYAAEGARVMVVTLTGGERGDILNPAMDLPEVHGRIAEVRRDEMAKAAEILGVEHHWLGFVDSGLPEGDPLPPLPDGCFALVPLEEPVKRLVRVIREFRPHVMTTYDENGGYPHPDHIRCHQVSVAAYEAAADHLLYPDAGEPWAVQKLYYNHGFLRQRMQLLQEEFAKNGQEGPFAKWLEHWDPDNDVFANRVTTRVHCAEYFHQRDDALRAHATQIDPKGDFFHAPIEWQQRLWPTEEFELARARVPVTLPEDDLFKGVEP
Protein: Protein Niban 2 (Meg-3) (Niban-like protein 1) (Protein FAM129B) (Q8R1F1)
Organism: Mus musculus (Mouse)
Function: May play a role in apoptosis suppression.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21148485}. Cell junction, adherens junction {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q96TA1}; Lipid-anchor {ECO:0000250|UniProtKB:Q96TA1}. Note=In exponentially growing cells, exclusively cytoplasmic. Cell membrane localization is observed when cells reach confluency and during telophase (By similarity). Phosphorylation may play a role in relocalization to the membrane (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MGDVLSTHLDDARRQHIAEKTEKILTEFLRFYEDQYGVSLFNSMRHEIEGTGPPQAQLLWRKVPLDERIIFSGNLFQYQEDNKKWRNRFSLVPHNYGLVLYENKVAYERQIPPRAVINSAGYKVLTSVDQYLELVGNSLPGTTSKSGSTPILKCPTQFPLILWHPYARHYYFCMMTEAEQDKWQAVLQDCVRHCNNGIPENSKVEGPAFTDAIRMYRQSKEQYGTWEMLCGNEVQILSNLVMEELGPALKAELGPRLKGKPQERQRQWIQISDAVYRLVFEQAKVHFEDVLCKLQRARPAMEAVIRTDMDQIITSKEHLASKIRAFILPKAEVCVRNHVQPYIPSILEALMVPTSQGFTEVRDVFFKEVTDMNLNVINEGGIDKLGEYMEKLSQLAYHPLKMQSCYEKMEPLRLDGLQQRFDVSSTSVFKQRAQIHMREQMDNAVYTFETLLHQELGKGPTKEELCKSIQRILERVLKKYDYDSSSVRKRFFREALLQITIPFLLKKLAPTCKSELPRFQELIFEDFARFILVENTYEEVVLQTVMKDILQAVKEAAVQRKHNLYRDSMVLHNSDPNLHLLAEGTPIDWGEQYGDSGDSGGGDSGGSPCPSEAATLTEKRRRAKQVMSVVQDEESGLPFEAGVEPPSPASPDSVTELRGLLAQDLQAESSPPASPLLNGAPVQESSQPVAVPEASPPASPLRHLPPGKAVDLEPPKPSDQETGEQVSSPGSRPPIHTTTEDSAGVQTEF
Protein: Homeobox-leucine zipper protein HAT2 (Homeodomain-leucine zipper protein HAT2) (HD-ZIP protein 2) (P46601)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that plays a role in auxin-mediated morphogenesis. Negatively regulates lateral root elongation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor PAR1
- Transcription factor HFR1
- Auxin-responsive protein IAA19
- Homeobox-leucine zipper protein ATHB-8
- Transcription factor BEE 1
- Transcription factor PIL1
- Homeobox-leucine zipper protein HAT22
- Homeobox-leucine zipper protein HAT3
- Transcription factor BIM1
- Auxin-responsive protein IAA1
Sequence:
MMMGKEDLGLSLSLGFSQNHNPLQMNLNPNSSLSNNLQRLPWNQTFDPTSDLRKIDVNSFPSTVNCEEDTGVSSPNSTISSTISGKRSEREGISGTGVGSGDDHDEITPDRGYSRGTSDEEEDGGETSRKKLRLSKDQSAFLEETFKEHNTLNPKQKLALAKKLNLTARQVEVWFQNRRARTKLKQTEVDCEYLKRCVEKLTEENRRLQKEAMELRTLKLSPQFYGQMTPPTTLIMCPSCERVGGPSSSNHHHNHRPVSINPWVACAGQVAHGLNFEALRPRS
Protein: PPFIA binding protein 2 (A0A8I6ALR5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTSDASHMLEAALEQMDGIIAGTKTAADFSDGTCEPGLSPPSSCLNSMPVLHLIEDLRLALEMLALPQEREALLSQIPGPTAAYIKEWFEDSLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSALHSDHAERDQEIHRLKMGMETLRVANEDKDRRIEELTGLLNQYLRVKEIVMATQGSSERTLSINEDEIEGSFRKWNTTSKSPEEVMKQEVSPRCSSPTPGPPPLPQKSLETRAQKKLSCSLEDLRCESGNKCINGNQTSPVGEPKDSSFLAEQKYPTLPGKLSGATPNGEAAKSPPTASLQPDSSGSSQPKLRDTEGGWEDIVMTNELSSTSSGTESSPQSPLTPDGKRSPKGIKKFWGKIRRTQSGNFNTDTPGMVEFRRGGLRATAGPRLSRTRDTKGQKCDANAPFAQWSTERVCTWLQDFGLAQYVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAINTKQEEKSALLDHVWVTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLHVNKFNPNCLHRRPADESNLSPSEVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALIGPEAEQEKRDKMASPAYTPLTTTAKVRPRKLGFSHFGNMRKKKFDESTDYICPMEPGDAVSDSHRVYGVYRGLSPLDNHELDGLDQMAPSEGTVTQIGLLSQDIHRLTTLLSQDQLLNDPPGCP
Protein: Metastasis-associated protein MTA3 (Q924K8)
Organism: Mus musculus (Mouse)
Function: Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Plays a role in maintenance of the normal epithelial architecture through the repression of SNAI1 transcription in a histone deacetylase-dependent manner, and thus the regulation of E-cadherin levels. Contributes to transcriptional repression by BCL6.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:11483358}. Cytoplasm {ECO:0000269|PubMed:11483358}.
Interaction partners:
- Histone deacetylase 1
- Transcriptional repressor p66 alpha
- Histone deacetylase 2
- Chromodomain-helicase-DNA-binding protein 4
- DNA helicase
- Transcriptional repressor p66-beta
- Histone-binding protein RBBP7
- Metastasis-associated protein MTA1
- Histone-binding protein RBBP4
- Chromodomain-helicase-DNA-binding protein 5
Sequence:
MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTASGNVEAKVVCFYRRRDISNTLIMLADKHAKETEEESETPVEADLTEKQKHQLKHRELFLSRQYESLPATHIRGKCSVALLNETESVLSYLDKEDTFFYSLVYDPSVKTLLADKGEIRVGPKYQADIPDMLPEDSDEREQSKLEVKVWDPNSPLTDRQIDQFLVVARAVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLYRHGYDLSSAISVLVPLGGPVLCRDEMEEWSASEACLFEEALEKYGKDFNDIRQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPTYKPNPNQISSSNGKAGTVNGAVGTQFQPQSALLGRACESCYATQSHQWYSWGPPNMQCRLCATCWLYWKKYGGLKMPTQSDEEKSPSPTAEDPRARSHMSRQALQGMPVRNTGSPKSAVKTRQAFFLRTTYFTKIARQVCKSTLRLRQAARRPFVAINYAAIRAEYADRHAELSGSPLKSRSTRKPLSCIIGYLEIHPAKKPNVIRSPPSLQTPATKRMLAAPNHTSLSILGKRNYSHHNGLDGPERWLSR
Protein: Acid ceramidase (AC) (ACDase) (Acid CDase) (EC 3.5.1.23) (Acylsphingosine deacylase) (Glycosylceramide deacylase) (EC 3.5.1.109) (N-acylethanolamine hydrolase ASAH1) (EC 3.5.1.-) (N-acylsphingosine amidohydrolase) (Putative 32 kDa heart protein) (PHP32) [Cleaved into: Acid ceramidase subunit alpha; Acid ceramidase subunit beta] (Q13510)
Organism: Homo sapiens (Human)
Function: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH. Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation. Has a higher catalytic efficiency towards C12-ceramides versus other ceramides. Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine. For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro-dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used. Has also an N-acylethanolamine hydrolase activity. By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes. Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis (By similarity). By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis.
Subcellular location: Lysosome {ECO:0000269|PubMed:12764132}. Secreted {ECO:0000269|PubMed:7744740}. Note=Secretion is extremely low and localization to lysosomes is mannose-6-phosphate receptor-dependent. {ECO:0000269|PubMed:11451951}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000305|PubMed:22927646}. Cytoplasm {ECO:0000305|PubMed:22927646}. Note=A localization to the nucleus and the cytoplasm has also been reported for ASAH1, most probably for isoforms devoid of a signal peptide. {ECO:0000305|PubMed:22927646}.
Interaction partners:
- Neutral ceramidase
- Galactocerebrosidase
- Alkaline ceramidase 1
- Sphingosine kinase 1
- Ceramide kinase
- Lysosomal acid glucosylceramidase
- Alkaline ceramidase 2
- Sphingosine kinase 2
- Ceramide synthase 2
- Alkaline ceramidase 3
Sequence:
MPGRSCVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGAVPWYTINLDLPPYKRWHELMLDKAPVLKVIVNSLKNMINTFVPSGKIMQVVDEKLPGLLGNFPGPFEEEMKGIAAVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITEQLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLTLNERFSINGGYLGILEWILGKKDVMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKESLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLSTKPVLNKLTVYTTLIDVTKGQFETYLRDCPDPCIGW
Protein: Rep1p (A0A1D8PRN4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Ngs1p
- NDT80 domain-containing protein
Sequence:
MDSNKERIEDLASLFLPDLLRPSTVNSSPSNATSPHASKSEDYDMGSVFLKDSKLTNAPSNSGLPSSFQEFLSNNNFINRSNDMEDGQEERSQQQPQQYSHHYNGYMPFEMNPSVSQHMMSYNPGMQSMFQQPNNPQQQSFLSSTLPGQQQMVSNFPRTGSYAKYPGEYDEWFASTNSSITNLNGLYQQQLLQSQALQQPQPMPQPQNGAKDTRMDTQSGSSTPKRKKAKSRKRDVKNLEVQIDYKPSKLKRLLDLKQSGATSSNDYKIIDKDNNEVTIDFNGFLNGRFLTNDIDNNNYIFTQNESQRGEDELPKTVVNKKENPKVVSCYRRNYIQISANMSIRGFKNDSKLLKLQTSEYGYTTTRVIKYFKIEVSAAANNSNSKGVPIIIKNENKDIEREREKEARKMSLPSNYEYKADNVSPTYINTNEYVIILNDEPISNGMIDKYFVVKKLQFKNATPNNGSLTFQNYYHLKAKLSCIVADIYYDDYDIDVANDGGGGNNEILLAELVSEPIIVRGRNPSFYAERNDILIKGRSASSKSSFKIAGQSSELKFRAAADAEEDEDDGFVVEHEDEPEDEDDHHNHSEGDVAGQEDQLPHTQNGTGESPISSGDDDEKDNTQIPPLSYSTNQLALDVKSVDKYKYYPINSVYYLPPINVVYFPHRAHQSQKDDQEQTSIVQENRKSSNVYFK
Protein: AT4g05070 protein (T32N4.14 protein) (Wound-responsive family protein) (Q9S9T1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT1G25275 protein
- Transmembrane protein
- Glycine-rich protein / oleosin
- Succinate dehydrogenase assembly factor 4
- At3g13845
- AT4g21620/F17L22_80
- At1g67862/At1g67862
- Small polypeptide DEVIL 6
- At1g67860/T23K23_29
- Secreted transmembrane peptide 5
Sequence:
MNRVISQFSGKLMKEKSVTGVSGGDTTLRSAVKESVSSPQSASSSSSVRRLKGDLESSRFGAAASERLRQAEESLRTVMFLSCWGSC
Protein: Proline--tRNA ligase (PfPRS) (EC 6.1.1.15) (Prolyl-tRNA synthetase) (PfProRS) (Q8I5R7)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Functions in trans to edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro). Has no activity on correctly charged Pro-tRNA(Pro) or Ala-tRNA(Ala).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25047712}.
Interaction partners:
- glutamate--tRNA ligase
- leucine--tRNA ligase
- isoleucine--tRNA ligase
- Proline--tRNA ligase, putative
- aspartate--tRNA ligase
- leucine--tRNA ligase
- glutamine--tRNA ligase
- Isoleucine--tRNA ligase, putative
- arginine--tRNA ligase
- tRNA import protein tRIP
Sequence:
MNNNTNGEIIIPQEYLEKSECLFKELKELNINFKEVKHGLAATIKDLLEMNLENSTNILKNLFLKDKKKNYFLICTLNNKTVDLKNLSNILKTNNLRFVDENNLNNILNIQPGCLSPLAIKNDKENIVKLYFDEEIKNMQEVIIHPLHNYSSLYIKTQDVIKFCESFNHAPEYVQIKEDTTSKARVDKKEDVQEEMAKNEELQNNNNNNKNNSNSNNNNNNNNNHIKDTILKGKLLSNNEVEDNKSKDSNILGITSKKIENFSDWYTQVIVKSELIEYYDISGCYILRPAAYYIWECVQAFFNKEIKKLNVENSYFPLFVTKNKLEKEKNHIEGFSPEVAWVTKYGDSNLPEEIAIRPTSETIMYSVFPKWIRSYRDLPLKLNQWNTVVRWEFKQPTPFIRTREFLWQEGHTAHKNEEEAVKLVFDILDLYRRWYEEYLAVPIIKGIKSEGEKFGGANFTSTAEAFISENGRAIQAATSHYLGTNFAKMFKIEFEDENEVKQYVHQTSWGCTTRSIGIMIMTHGDDKGLVLPPNVSKYKVVIVPIFYKTTDENAIHSYCKDIEKILKNAQINCVYDDRASYSPGYKFNHWELRGIPIRIEVGPKDLQNNSCVIVRRDNNEKCNVKKESVLLETQQMLVDIHKNLFLKAKKKLDDSIVQVTSFSEVMNALNKKKMVLAPWCEDIATEEEIKKETQRLSLNQTNSETTLSGAMKPLCIPLDQPPMPPNMKCFWSGKPAKRWCLFGRSY
Protein: FG-GAP repeat-containing protein (F4J381)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- SKA complex subunit 1 homolog
- Exocyst complex component SEC8
- Exocyst complex component EXO84B
- 26S proteasome non-ATPase regulatory subunit 7 homolog A
- Protein POLAR-like 1
- Pentatricopeptide repeat-containing protein At4g18520, chloroplastic
Sequence:
MRKRDLAILMLSGFAIFFTLQHEGDFAFKEAWFHLYDEYPVKYEADRLPPPIVADLNGDGKKEVLVATNDAKIQVLEPHSRRVDEGFSEARVLAEITLLPDKIRVASGRRAVAMATGVIDRYYKNGTPQKQVVVVVTSGWSVLCFDHNLKKLWETNLQEDFPHNAHHREIAISISNYTLKHGDTGLVIVGGRMEMQPYNHMDPFEELGMTAQNADQHRRSATENQASEDSGAINLRHFSVYAFAGKTGLLRWSKKTDDVEAHTSDASQLIPQHNYKLDVHALNSRHPGEFECREFRESILSVMPHRWDRREDTLLKLAHFRRHKRKTLKKQAGSKSTAYPFHKPEEHTPAGKDLSRKIPKLIGKAARYAGSAKPKKGMQYIPTITNYTKLWWVPNVVVAHQKEGIEAIHLPTGRTLCKLSLLEGGLHADINGDGVLDHVQTVGGNVGERTVVSGSMEVLKPCWAVATSGVPIREQLFNVSICHHSPFNFLHYGGDYSRHFAQARDTSTLEIATPILIPRDDGHKHRKGSHGDVIFLTNRGEVTSYTPDVHGHDAVWQWQLQTEATWSNLPSPSGLTESGTVVPTLKPFSLRIHDNQPMILAGGDQAAVIISPGGSILASIELPSQPTHALITDDFSNDGLTDVIVMTSNGVYGFVQTRQPGALFFSSLVGCLLVVMAVIFVTQHLNSIQGKPRPSSSF
Protein: Outer membrane protein assembly factor BamE (P0A937)
Organism: Escherichia coli (strain K12)
Function: Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_00925, ECO:0000269|PubMed:17404237, ECO:0000269|PubMed:26900875, ECO:0000269|PubMed:26901871}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00925, ECO:0000269|PubMed:17404237, ECO:0000269|PubMed:27686148}.
Interaction partners:
- Outer membrane protein assembly factor BamA
- Outer membrane protein assembly factor BamB
- Outer membrane protein assembly factor BamC
- Outer membrane protein assembly factor BamD
- Chaperone SurA
- LPS-assembly protein LptD
- Chaperone protein Skp
- Outer-membrane lipoprotein carrier protein
- Phospholipase A1
- Outer-membrane lipoprotein LolB
Sequence:
MRCKTLTAAAAVLLMLTAGCSTLERVVYRPDINQGNYLTANDVSKIRVGMTQQQVAYALGTPLMSDPFGTNTWFYVFRQQPGHEGVTQQTLTLTFNSSGVLTNIDNKPALSGN
Protein: Metalloendopeptidase (EC 3.4.24.-) (Q2ABP1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MELAARCALLLSSFSLLAALDLDAIEPGYYVETSSPSDLIDYKDPCKAVAYLGDIALDEEDMRMFTVDRIVNLAERTVTILNHTNTGSLSNETSVNTTASSRGSHRRRRAATSRPERVWPEGVIPYVISGNFSGSQRAIFRQAMRHWEKHTCVTFIERTTEESYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDEHVSIIRDNIQPGQEYNFLKMEPGEVDSLGEVYDFDSIMHYARNTFSRGIFLDTILPRYDVNGVRPPIGQRTRLSKGDIAQARKLYKCPRCGDSLQESSGNFSSPGYPNGYSAYMHCIWRISVTPGEKIILNFTSMDLYRSHLCWYDHVEIRDGYWRKAPLKGRFCGDKLPDPIISTDSRLWIEFRSSSNWVGKGFSAVYEAICGGEVKKDNGQIQSPNYPDDYRPNKVCVWKITVAQGYHVGLTFQSFEIERHDNCAYDYLEVRDGNSESSPLLGRFCGYDKPDDIKSSSNQLWMKFVSDGSVNKAGFAANFFKEMDECSRPDNGRCEQRCVNTLGSYKCACDPGYELAADKRSCEAACGGFITKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRITLLFDVFETEGNDVSTRFLPLRGVCKYDFVEVRSGLSADSRLHGKFCGAEKPEAITSQYNNMRIEFKSDNTVSKKGFKAQFFSDKDECSKENGGCQHECVNTFGSYSCQCRSGFVLHENKHDCKEAGCDHVVNSVSGTITSPNWPDKYPSKKACTWALSTTPGHRIKIAFNEIDMEPHLECAYDHIEIYDGRDSKAQSLGRYCGTKKPQPIISTGNKMFIRFFSDNSVQKKGFEASHTAECGGRLKAEVKTKDLYSHAQFGDNNYPGASDCQWVITAEKGYGVELIFQTFEIEEEADCGYDYMELFDGADTKSPRLGRYCGSGPPEEIYSAGDSIVIKFHSDDTINKKGFHVRYTSTKFQDTLHSRKK
Protein: MBNL1 protein (Muscleblind like splicing regulator 1) (Muscleblind-like (Drosophila), isoform CRA_f) (Q86VM6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMTQSAVKSLKRPLEATFDLGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPGSILCMTPATSVVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM
Protein: G-protein coupled receptors family 1 profile domain-containing protein (Q8MXS7)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Serotonin-gated chloride channel mod-1
- Nuclear hormone receptor family member nhr-76
- Tyramine beta-hydroxylase
- Biopterin-dependent aromatic amino acid hydroxylase family profile domain-containing protein
Sequence:
MILLSLTLGVVNCFVVIGNLLVFYVILTKKSLQTSTNHLVLSLTISDLLLGILILPFAIIQEHSNEWIFGHFGCRLWLSVDVFLSTASIYNLLAISFDRYMAVRQPIKYPIISSTKVVRLMTFLVWFCSLLLAVILFVLLTLNAHDSEPTKDCQPTSLPSMYIIFSAMASFIVPAFVMVILNVRIFQTVLHTSRTMTVKSKNGSLRVHRRKEPIIPVKKHDKYETRLSHEEECVGSPSKEVIDPIPVVAVVEKHHKSSAVDAPAIRSFLTHTVVFGVLEAKKTNIINHITQWWRRSTVRSPNPSTRKKCMRRSLRTEIRVARTTGIVVAAFIVCWIPFTTIYVLQAYAVCTVAAGCIPASLFTTAFWLGYSNSAVNPILYAAFSRDFRIALKRLFFQKPKF
Protein: Death domain-containing membrane protein NRADD (Neurotrophin receptor homolog-2) (NRH2) (Neurotrophin receptor-alike death domain protein) (P75-like apoptosis-inducing death domain protein) (PLAIDD) (Q8K5A9)
Organism: Rattus norvegicus (Rat)
Function: Modulates NTRK1 signaling. Can activate several intracellular signaling pathways, leading to activation of JUN. Promotes translocation of SORT1 to the cell membrane, and thereby hinders lysosomal degradation of SOTR1 and promotes its interaction with NGFR (By similarity). Both isoform 1 and isoform 2 promote apoptosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12095158}; Single-pass type III membrane protein {ECO:0000269|PubMed:12095158}. Nucleus {ECO:0000250}. Note=Proteolytic processing gives rise to an intracellular domain that translocates to the nucleus. {ECO:0000250}.
Interaction partners:
- Nephrocan
Sequence:
MLHNVSKGVVYSDTALKGQDGDREGMWVGAGGALAPNTSSLFPPEPPGASSNIIPVYCALLATVVLGLLAYVAFKCWRSRKQRQQLAKARTVELGDPDRDQRHGDSSVFVDSPHGLEPCIPSQGPHADLGCRLYLHIPQQQQEEVQRLLILGEPAKGWQGLAGQLGYQAEAVETMACDQDPAYALLRDWAAQEGSGATLRVLEDALTAIGREDVVQVLSSPAEGCSVV
Protein: Growth hormone (Q0QBF0)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MMAAGPRTSLLLAFTLLCLPWTQVVGAFPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKPDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDVTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
Protein: RE67944p (Q5BII2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPGFRGRRVWCGCFKDDEPPEICVVEGAFTLQTLTPTQPMPSVDELDTKFAELVEELDLTAPNKEAMLSLPAQKKWQIYCSRKLPLDAADGPDAAAVTQPPTAEHYIERLKELVVHISLSPEDSPSHELGNRLDGHAAFVDALKTALRTSTHSFVLRFVELDGLPALLDLLLQLDIRVANSPLHTSLIGCIKALMNNSMGRAHVLAHPTAIDTIARSLAADNIRTKIAALEILGAVCLVPGGHRKVLQAMLHFQVFATERTRFQSIVNDLDRSTYAYRDNVNLKTALMSFVNAVLNYGPGQENLEFRLHLRYEFLMLGIQPVIDKLRTHENETLDRHLDFFEMVRAEDEKEFARRFKEEHVDTKSAGSMFELLRRKLSHSPAYPHMLSLLQHMLLLPYTGHCTEHWLLIDRVVQQIVLQVEQRPNSDLVVDPDDPEKQLKLAAESPVHDPDVAPLQIDVAKLVRLLVKEEQLTQARKRADELERENFDVQSRLAKKEQELDLRMQEKEDLETGLARMRERLEKESAQHSQAVQRAQTAEMRAEDLQHRLISEQQERARLERLVTEGSIPDDQKVAGLTGCNGAVSPPPAPPMLKAIPPPPPPMAPSMMPPPPPPCPGAPPPPPSMAQTMAPAPPKVDLPKKNVPQPTNPLKSFNWSKLPDAKLQGTVWSELDESKLYNNMELESIDKLFSAYQKNGVSATDGSYEDLRVTGKAAKQKVLSVIDGRRAQNCTILLSKLKMSDMEISKAILSMNSNEQLQLDMVEQLLKFTPSAEERALLDEHSEDIESLARADRFLYEISKIPHYEQRLKSLHYKKRFMLTINDLVPRITSVMEASREVARSRRLRKLLELVLALGNYMNRGARGNASGFRLASLNRLADTKSSAAKGTTLLHYLVQVIERKFKDLLKLEDDIPHVREASKVSLGEMDKDIQMLRTGLADVAREIEFHRSSGPAQQGDRFLPVMREFHAQASVRFAELEDKFQDMKTRFDRAARLFGEDGSVFAAGRVLWHL
Protein: Putative methyltransferase C9orf114 (EC 2.1.1.-) (Centromere protein 32) (CENP-32) (Kinetochore-associated protein) (SPOUT domain-containing methyltransferase 1) (Q5T280)
Organism: Homo sapiens (Human)
Function: Required for association of the centrosomes with the poles of the bipolar mitotic spindle during metaphase. Also involved in chromosome alignment. May promote centrosome maturation probably by recruiting A-kinase anchor protein AKAP9 to centrosomes in early mitosis. Binds specifically to miRNA MIR145 hairpin, regulates MIR145 expression at a postranscriptional level.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:25657325}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20813266, ECO:0000269|PubMed:25657325}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25657325}. Note=Associated with the outer kinetochore. {ECO:0000269|PubMed:20813266}.
Interaction partners:
- TBC1 domain family member 13
- Kynurenine--oxoglutarate transaminase 1
- U3 small nucleolar ribonucleoprotein protein IMP4
- Endonuclease G, mitochondrial
- WD repeat-containing protein 46
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Probable U3 small nucleolar RNA-associated protein 11
Sequence:
MAERGRKRPCGPGEHGQRIEWRKWKQQKKEEKKKWKDLKLMKKLERQRAQEEQAKRLEEEEAAAEKEDRGRPYTLSVALPGSILDNAQSPELRTYLAGQIARACAIFCVDEIVVFDEEGQDAKTVEGEFTGVGKKGQACVQLARILQYLECPQYLRKAFFPKHQDLQFAGLLNPLDSPHHMRQDEESEFREGIVVDRPTRPGHGSFVNCGMKKEVKIDKNLEPGLRVTVRLNQQQHPDCKTYHGKVVSSQDPRTKAGLYWGYTVRLASCLSAVFAEAPFQDGYDLTIGTSERGSDVASAQLPNFRHALVVFGGLQGLEAGADADPNLEVAEPSVLFDLYVNTCPGQGSRTIRTEEAILISLAALQPGLIQAGARHT