wanglab/gogpt-training-data huggingface dataset:
Protein: TRAF3-interacting protein 1 C-terminal domain-containing protein (Q38CJ3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
Interaction partners:
- Intraflagellar transport protein 57/55
- Intraflagellar transport protein A1
- Intraflagellar transport protein 80
- IFT80/172/WDR35 TPR domain-containing protein
- Uncharacterized protein
- C2H2-type domain-containing protein
- Intraflagellar transport
- Intraflagellar transport protein IFT88, putative
- Intraflagellar transport protein component, putative
- Intraflagellar transport protein 56 homolog
Sequence:
MLDSANVSDKEKKIQFLSLLIAAVESATGSKVSANPSKIVAGHEPEQTNELLQLLASCAALPSDKKAAAVKAAKSAGDATKSSSSKGGDDDEKRKRREEEKKKRKEEEGDGEKKKHKEEDGEKKKHKEEDGEKKKHREEDGERKKHKEEDSEKKKRKEGEGEEKKKHKEEDGEKKKRKEEEGDGEKKKHRDEDGEKKKHREDDGERKKRKEEEGDGEKKKHKEEDGEKKKRKEEEGDEKKKHREDESERKKRKEEDGEKKKRKEEEGEKKKRKEEDGDGEKKKRRDEDDEERRRRHEERKRQEKKAAEQAQGSAGAEPSEGKGADGTTEGATGQQQLPTRQLIRKSSAGKAPPRSKASHEVVADDGSSANVAEVIRETKRGAAGEGSKEDGEENDWMRVAEQQAARPTKDSDGTLQDGEAKGYLGQQALRAKREQEEETARLAQDGGARGPREGGIIIHSNRAGKSGGTMAEGELSKLRQQLQLLTKASNPLGKLLESIHDDIDTMGRELEMWRSEARSQALAAADARRQTTESLQEVHAQLQALEDAISDQILKNHNIRRNIISNDNAIAGMVRMFVNPDALTR
Protein: p53 apoptosis effector related to PMP-22 (E9QHT9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, desmosome {ECO:0000250|UniProtKB:Q9JK95}. Cell membrane {ECO:0000250|UniProtKB:Q9JK95}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9JK95}.
Interaction partners:
- Plakophilin 1b
Sequence:
MFRCGIDYTRCRWILPMLLLFAIIFDIIAIAAQSGWVEDQDAKTHYASMWKQCRGRNDQWDCKSLMEFSWAQAVAALMIIGLIILIFAFIISLVALCSTVNVSLLPFIGLLLILAVIVQIIALIIYPVKFNEQIYEGYYDYTWAYGFGWGATILTLGCAILFCCLPRYESEITGLEKTKYIYQSG
Protein: MYND-type domain-containing protein (Q381B9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTGGVHSGLFTLHFTFFANSATDDERLLHTGRKAGTKSSGEFGDWHVLLRFAVEDEVISVRHQGKIFAMSDECCEGSSGEEPVVIPGLGRIPRPLKDRYATVVMRSHYHWQLNEPCRFDVHFDQLEGRIVGSTEPMLSDVTVSCEGYTAYGWYMGEATVTVGGSPYAMQQQLRFVLTPYIGPQCTMCLDPVYAQGYTCAECGGVEYCSRACQLAHMSGGHGLLCQTIGCTYTQRSGKITTELEDGTDLVAWWRCLEDAHYSILVDYRNPIGQAVEFFLCTLKPAQEEGIHYRFIVEEGTTPQKVDQEKFVDFACTVFRAVSENAISEGCASLAAACLNYLFVYSCNTGVIVESHVLYYYSCLSEDFEGAIYSLEEYVAYARPMHELGVALIEFALKSPTAHLFWQRMKLVKNVFINLYNINTSCQGSGSSELIKAIPGQQRETLHLLAKVFLIMASRAPKKEVLFMLKQAEKCLRDCLPERGDCDEAVENALEARLNDGDKCEESEGSMLMDDNMEEMDSSNLATLYYRLSVLLLLYGDPKKAQEAEALKAQGDLLIARKRQLSGQTVG
Protein: DNAJC4 protein (DnaJ (Hsp40) homolog, subfamily C, member 4, isoform CRA_i) (DnaJ heat shock protein family (Hsp40) member C4) (DnaJ homolog subfamily C member 4) (Q96FY5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPPLLPLRLCRLWPRNPPSRLLGAAAGQRSRPSTYYELLGVHPGASTEEVKRAFFSKSKEEGEADAP
Protein: Cyclin-dependent protein kinase inhibitor SMR5 (Protein SIAMESE-RELATED 5) (Q9LNX4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable cyclin-dependent protein kinase (CDK) inhibitor that functions as a repressor of mitosis in the endoreduplication cell cycle. Acts as a potent cell cycle inhibitor, regulating a hydroxyurea-dependent checkpoint in leaves. Essential to activate a high-light-dependent cell cycle checkpoint.
Interaction partners:
- Cyclin-dependent protein kinase inhibitor SMR7
- SUPPRESSOR OF GAMMA RESPONSE 1
- Transcription factor MYB3R-3
- Wee1-like protein kinase
- NAC domain containing protein 85
- NAC domain containing protein 44
- Cyclin-dependent protein kinase inhibitor SMR3
- Cyclin-U3-1
- Protein BREAST CANCER SUSCEPTIBILITY 1 homolog
- Serine/threonine-protein kinase ATR
Sequence:
MEEKNYDDGDTVTVDDDYQMGCTTPTRDDCRIPAYPPCPPPVRRKRSLLGFGKKREPPKKGYFQPPDLDLFFSVVAASQAAT
Protein: Probable undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase (EC 2.7.8.33) (UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase) (Undecaprenyl-Phosphate GlcNAc-1-phosphate transferase) (O34753)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the formation of undecaprenyl-PP-N-acetylglucosamine. Involved in the synthesis of anionic cell-wall polymers as it mediates the initiation of the linkage unit formation that appears to be common to the two types of teichoic acids attached to the peptidoglycan of B.subtilis; may also be involved in teichuronic acid biosynthesis (Probable).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- UDP-N-acetylglucosamine 2-epimerase
- N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase
- Teichoic acid glycerol-phosphate primase
- Teichoic acid poly
- Glycerol-3-phosphate cytidylyltransferase
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- Teichoic acid translocation permease protein TagG
- Poly
- Putative teichuronic acid biosynthesis glycosyltransferase TuaH
- Teichoic acids export ATP-binding protein TagH
Sequence:
MLDERMIRIVVAFIVSLLTVLIITPIVKRIAIKIGAVDQPSNRKVHDKIMPRMGGLAIFIGVVAGVLASGIYTETRMTAITVGAFIIIVLGILDDKYQLSAKVKFLIQLGVAIMIVSTGLKMDFFSVPFLTERFELGWMAYPLTVLWIVGITNAINLIDGLDGLAAGLSVIGLSTIAVMALSGGKVLILSLSLVVIASTLGFLFYNFHPAKIFMGDTGSLFLGYSISILSLLGLYKSVTLFSIVIPIIILGVPIFDTTFAIIRRILNKQPISAPDKSHIHHRLMAFGLSHRMSVLVIYLIGFIFSISAIVLKSATIWLSLFIIFILIIFMQIIAEVTGLVNEKFKPFTKFYKRLVKRN
Protein: Rac family small GTPase 2 (F7EM94)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKCRPSSVWWWVMAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLRDDKDTIEKLKEKKLAPITYPQGLALAKDIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQPTRQQKRPCSLL
Protein: Cell cycle control protein 50B (P4-ATPase flippase complex beta subunit TMEM30B) (Transmembrane protein 30B) (Q3MIR4)
Organism: Homo sapiens (Human)
Function: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate (Probable). Can mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2 and ATP8B4 from the ER to the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20961850}; Multi-pass membrane protein {ECO:0000269|PubMed:20961850}.
Interaction partners:
- Phospholipid-transporting ATPase IC
- Phospholipid-transporting ATPase IG
- Phospholipid-transporting ATPase ID
- Probable phospholipid-transporting ATPase IM
- Phospholipid-transporting ATPase IA
- Phospholipid-transporting ATPase IB
- Phospholipid-transporting ATPase IF
- Phospholipid-transporting ATPase IH
- Phospholipid-transporting ATPase VD
- Phospholipid-transporting ATPase IK
Sequence:
MTWSATARGAHQPDNTAFTQQRLPAWQPLLSASIALPLFFCAGLAFIGLGLGLYYSSNGIKELEYDYTGDPGTGNCSVCAAAGQGRALPPPCSCAWYFSLPELFQGPVYLYYELTNFYQNNRRYGVSRDDAQLSGLPSALRHPVNECAPYQRSAAGLPIAPCGAIANSLFNDSFSLWHQRQPGGPYVEVPLDRSGIAWWTDYHVKFRNPPLVNGSLALAFQGTAPPPNWRRPVYELSPDPNNTGFINQDFVVWMRTAALPTFRKLYARIRQGNYSAGLPRGAYRVNITYNYPVRAFGGHKLLIFSSISWMGGKNPFLGIAYLVVGSLCILTGFVMLVVYIRYQDQDDDDEE
Protein: Zinc transporter 6, chloroplastic (ZRT/IRT-like protein 6) (O64738)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in the transport of zinc in the plastids.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Putative zinc transporter At3g08650
- Putative cadmium/zinc-transporting ATPase HMA4
- Metal tolerance protein 1
- TPR repeat-containing protein ZIP4
- Metal transporter Nramp5
- Metal transporter Nramp3
- Metal transporter Nramp4
Sequence:
MASCVTGTEAAIRAAACRDGEEASHLKIVAVFAIFLTSVFGVWGPVLLAKYFHGKPLYDKAILVIKCFAAGVILSTSLVHVLPEAFESLADCQVSSRHPWKDFPFAGLVTMIGAITALLVDLTASEHMGHGGGGGGDGGMEYMPVGKAVGGLEMKEGKCGADLEIQENSEEEIVKMKQRLVSQVLEIGIIFHSVIIGVTMGMSQNKCTIRPLIAALSFHQIFEGLGLGGCIAQAGFKAGTVVYMCLMFAVTTPLGIVLGMVIFAATGYDDQNPNALIMEGLLGSFSSGILIYMALVDLIALDFFHNKMLTTCGESGSRLKKLCFVALVLGSASMSLLALWA
Protein: OFD1 centriole and centriolar satellite protein (A0A8I3Q5R3)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Interaction partners:
Sequence:
MCIGGVACDEISRKGTGQVRPGRLQAGWRHSHNSRRAGPGMSSKAPAPYSLHLLPAARIRQSQQPHFPRPTRAAPRRAPWVGTPRAILARVRRWHLARVRCWRLARGGRSFRPEYGACAVALPAWAVPLGGPRGGAGSTLNAPNSCSCAFVFCCLTTGPRPRGAWESLLWATTPPTHGPPRGSANGLQFLVHSKRRSSASFFSTAPRRRLGSGGRDSPSSCACRPGGVLTRAKTTMPSKPDMLSQDELRKKLYQTFKDRGILDTLKTQLRNKLIHELMHPVLNGELQPPSVSVEGSALLTSASNSLVADYLQRCGYEYSLSVFFPESGLAKEKVLTMQDLLQLIKINPESSLYKSLISGFDKENKGFLLHFLRELADYHQSKASCDAETQTSLAFPGKDSLAEKLQLIDDQFADASPQRPKLESLEIKLNEYKKEIEQQLQAEMCHKLKYFKDTEVAKIKMEEKRKAEKELAKFRNQFEQALRAKSEAFISRERLALERIQKHQEIETKEIYAQRQLLLKDIDLLRGREAELKQRIEAFELAQRLQEEQNKSITDALRKRELNIKSIEESYDQKLKNELLKYQLELKDDYIARTNRLIDDERKNKEKAIHLQEELSAINSKKEELNHSVNRVKELELELESVRAQCLAITNQNHLLNEKVKEMSDYSLLKEGKLELQAQNRLLKQQVEDSRNENLRLLNHIAQPSPELVVFQKELKKAENAIALEHKEFENHKLALQKQLQSEIEHSAQLKAQIRDYDESVNRLTIQVADLRLQLKQTQTALENEVYRNPKQSLIDRSVSRLLSGKTVVPWNGDLNGDFLKNPLKQERLMAIIPRITSLPNASTESSSPDSDLEFVVNTKMRVKELEQEAERLEKAFQNYHRRVSQHPAKSPLTSKSPPSLHLVGTLKNITSGAPQRPPSAEDKVVSEQCAVGTPDEDKSSASEAQTGNMASRPRRSISSRRLSSTPLPKAKRSLDDEMYLEGLAQSHAAGPSPGPDGTPQPSPTESRHSLSLHPLPSSPEQASLYQKQLKLQDKTEFSNPDKPPFKDNEELESSFECAGSTPKQFEVNVLHPAGDMPHMDAAAAAVSFHYPSKDQKQMGEPKEEEKIWEGHMRERKEREERRQNEWQEALERERKELEKLDQERSSKKIVREGSEVDTLPSSDKDESFRGFFPEEPDDFW
Protein: Inactive hyaluronidase B (Hya B) (Hyaluronoglucosaminidase B) (allergen Ves v 2b) (Q5D7H4)
Organism: Vespula vulgaris (Yellow jacket) (Wasp)
Function: Has no hyaluronidase activity.
Subcellular location: Secreted {ECO:0000269|PubMed:16218950}.
Interaction partners:
Sequence:
DRTIWPKKGFSIYWNIPTHFCHNFGVYFKELKQFNIKYNSMNNFRGETISLFYDPGNFPSMVLLKNGTYEIRNEGVPQKGNLTIHLEQFTKELDEIYPKKIAGGIGVIHFHNWRPIFRRNVDNLKINKDISIDLVRKEHPKWDKSMIEKEASNRFETSAKIFMEKTLKLAKEIRKKTEWGYHGYPHCLSGSTDKPSFDCDALSMSENDKMSWLFNNQNVLLPSIYLKNVLKPDEKIHLVQERLKEAIRISKNFKHLPKVLPYWWYTYQDKESIFLTEADVKNTFKEILTNGADGIIIWGVSYELTDRKRCEKLKEYLMKILGPIAFKVTKAVKENTPLNF
Protein: Cytosolic carboxypeptidase 6 (EC 3.4.17.-) (ATP/GTP-binding protein-like 4 homolog) (CeAGBL4) (Q09296)
Organism: Caenorhabditis elegans
Function: Metallocarboxypeptidase that catalyzes the removing of polyglutamate side chains that are present on the gamma-carboxyl group of glutamate residues of tubulin in sensory cilia. Probably via the deglutamylation of tubulin, promotes microtubule stability required for axon regrowth after injury. Also regulates microtubule dynamics in uterine muscle cells.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q09LZ8}.
Interaction partners:
- Mitogen-activated protein kinase pmk-3
- Tubulin polyglutamylase ttll-4
- Kinesin-like protein
- Mitogen-activated protein kinase pmk-2
- Mitogen-activated protein kinase pmk-1
- Tubulin polyglutamylase ttll-5
- Probable tubulin polyglutamylase ttll-15
- Tubulin--tyrosine ligase-like protein 12
- Kinesin-like protein
- Probable tubulin polyglutamylase ttll-9
Sequence:
MGYVGNVSYPDTIPGQGNLVFEASFESGNLGRVDKVSCSEYDLFIRPDTLNNKYRVWFYFECKNASENQRAIFNIVNFSKQRTLFEMGIAAPVVKSNAQNSWARIPSRHIYYYRSSQHNDRWILSFAFIFESPDPVQFAYCIPYTYGQMQIWLNELESRKYPFFHRDLLVQTVQKRRVDLITIDATPDTFQGSKKMIFLTARVHPGESPSSHVMHGIIEFLVSKDDRAQKLRKVYCFKIIPMLNPDGVFLGNYRCSLMGHDLNRMWRTPSDWAHPSIYAVKNLLTQYDNNPQAQTVIYVDLHAHSQKPNCFLYGNVNMSAVEEKSTFRQLWLPHLLADLSEDYSLEFTQFNTDVEKAGTGRRTMGDLLSCLCYTLEVSFFSYRHTDSSGNGIQHCTPYLQYKYEALGEAFCRALLNFYEADCGLREIVLERPFKTFLPARAQKTLKKQARKVIQTVMMK
Protein: Lipase member I (A0A087WZG8)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MCWVRSDNKRPCLEFSQLSVKDSFRDLFIPRIETILMMYTRNNLNCAEPLFEQNNSLNVNFNTQKKTVWLIHGYRPVGSIPLWLQNFVRILLNEEDMNVIVVDWSRGATTFIYNRAVKNTRKVAVSLSVHIKNLLKHGASLDNFHFIGVSLGAHISGFVGKIFHGQLGRITGLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCDCFKEKSCPRLGYQAKLFKGVLKERMEGRPLRTTVFLDTSGTYPFCTYYFVLSIIVPDKTMMDGSFSFKLLNQLGMIEEPRLYEKNKPFYKLQEVKILAQFYNDFVNISSIGLTYFQSSNLQCSTCTYKIQSLMLKSLTYPERPPLCRYNIVLKDREEVFLNPNTCTPKNT
Protein: Suppressor of fused homolog (Q4V8C6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR011844}. Nucleus {ECO:0000256|PIRNR:PIRNR011844}.
Interaction partners:
- GLI family zinc finger 2
- Kinesin family member 7
- GLI family zinc finger 1
- GLI family zinc finger 3
- Protein smoothened
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase ULK3
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Speckle-type POZ protein, isoform CRA_a.
Sequence:
MAELRPSVAPGPAAPPASGPSAPPAFASLFPPGLHAIYGECRRLYPDQPNPLQVTAIVKYWLGGPDPLDYVSMYRNMGSPSANIPEHWHYISFGLSDLYGDNRVHEFTGTDGPSGFGFELTFRLKRETGESAPPTWPAELMQGLARYVFQSENTFCSGDHVSWHSPLDNSESRIQHMLLTEDPQMQPVQTPFGVVTFLQIVGVCTEELHSAQQWNGQGILELLRTVPIAGGPWLITDMRRGETIFEIDPHLQQERVDKGIETDGSNLSGVSAKCAWDDLSRPPEDDEDSRSICLGTQPRRLSGKDTEQIRETLRRGLEINSKPVLPPINSQRQNGLTYDRAPSRKDSLGSDISTAVIPHELIRTRQLESVHLKFNQESGALIPLCLRGRLLHGRHFTYKSITGDMAITFVSTGVEGAFATEEHPYAAHGPWLQILLTEEFVEKMLEDLEDLTSPEEFKLPKEYSWPEKKLKVSILPDVVFDSPLH
Protein: Protein arginine N-methyltransferase 7 (EC 2.1.1.321) (Histone-arginine N-methyltransferase PRMT7) ([Myelin basic protein]-arginine N-methyltransferase PRMT7) (Q922X9)
Organism: Mus musculus (Mouse)
Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Protein arginine N-methyltransferase 5
- Transcriptional repressor CTCFL
- Methylosome protein WDR77
- Small nuclear ribonucleoprotein Sm D3
Sequence:
MKVFCGRANPTTGSLEWLEEDEHYDYHQEIARSSYADMLHDKDRNIKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMAEAAVKIVERNGFSDKIKVINKHSTEVTVGPDGDLPCRANILITELFDTELIGEGALPSYEHAHKHLVQEDCEAVPHRATVYAQLVESRRMWSWNKLFPVRVRTSLGEQVIVPPSELERCPGAPSVCDIQLNQVSPADFTVLSDVLPMFSVDFSKQVSSSAACHSRQFVPLASGQAQVVLSWWDIEMDPEGKIKCTMAPFWAQTDPQELQWRDHWMQCVYFLPQEEPVVQGSPRCLVAHHDDYCVWYSLQRTSPDENDSAYQVRPVCDCQAHLLWNRPRFGEINDQDRTDHYAQALRTVLLPGSVCLCVSDGSLLSMLAHHLGAEQVFTVESSVASYRLMKRIFKVNHLEDKISVINKRPELLTAADLEGKKVSLLLGEPFFTTSLLPWHNLYFWYVRTSVDQHLAPGAVVMPQAASLHAVIVEFRDLWRIRSPCGDCEGFDVHIMDDMIKHSLDFRESREAEPHPLWEYPCRSLSKPQEILTFDFQQPIPQQPMQSKGTMELTRPGKSHGAVLWMEYQLTPDSTISTGLINPAEDKGDCCWNPHCKQAVYFLSTTLDLRVPLNGPRSVSYVVEFHPLTGDITMEFRLADTLS
Protein: LD17393p (Lk6 kinase, isoform A (EC 2.7.11.1, EC 2.7.11.17)) (Q9VGI4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Eukaryotic translation initiation factor 4G1, isoform B
- Eukaryotic translation initiation factor 4E1
Sequence:
MVEPKSGTAASAAAAKASNNNNNNHPRGSGDSGIRSGSGISCSNTDNSCSQSQSDGQNELTRYSSEDVSGNESSEAPNMTEVERQAELNRHKEEMQKKRRKKRISSSLHSSTFQELYKLTGEILGEGAYASVQTCVNIYTDLEYAVKVIDKIPGHARARVFREVETFHHCQGHLGILQLIEFFEDDEKFYLVFEKINGGPLLSRIQEHICFSEHEASQIIKEIASGLDFLHKKGIAHRDLKPENILCVKTDSLCPIKICDFDLGSGIKFTTDISSPAATPQLLTPVGSAEFMAPEVVDLFVGEAHYYDKRCDLWSLGVIAYILLCGYPPFSGNCGEDCGWNRGENCRTCQELLFESIQEGHFSFPEAEWHDVSDEAKDLISNLLVKKASNRLSAEAVLNHPWIRMCEQEPPASKHGRRHKALQTPSNIRRNHQSAREISQFAESAMAVKRVVLQHFSMRYDYMKERPNIYQPSQAYMDAYSDENYNPKPPGHYTRNRSQRNPASSLCGYGGRMSSMHGQRANSRRSSRNASRNASAIYPNSGGFKTLNVHEEDDDDEGLEAFGHIDDDDEWSRSRREYQQQCETLGEDRFRRQSGSEGDEVEDDEDGENEDYQHYKHYWRELDEEEGDDYLYEQQQRVDDKFGEEEFEDEPKEETQADNLKLSKAYVEQVGETNVEKSKPQDDNGGYIREDLIMDNMDMKKNTQQSEFAKLTIMRNDAQTEENKIMQQQDEEKKEEKQQDDVDGAKKQGPSSDISATTITDNNKLQTPVMTTTHINNWQTGDAIEDDDVKLLDSISDLNEKLPEIYETANIVVNSAAVPAASTPAASATRPPTDNPEEDDSNVTKPTTTAEGTTMQTTFGMSAEEEKPVALSHTAGHHSKTGRTVNFAPDAYQNDEDADIDEDDDYDDEENLHEHSKQQLPSNAYTRKQRQQHQRYIVPRYQLADQVPQRQHTENWRYRTHHSQEQQPTADYRKYRPPFSTGGGGGHHGNQQRNYLGSFSHSGGAAGYKIAPMPPPMQPPPRHNSAGSSGSGSGSGGSPPSDEQSAIRNWRQDCVYARSCGMNQGPEQQRHNRSSGQRVQQQPRIGSGRFAHLQAAQLMDELPDMRIGLSPPSESVLLQRRLRQQQRANDLSEYCEPATASG
Protein: DNA nucleotidylexotransferase (EC 2.7.7.31) (EC 3.1.11.-) (Terminal addition enzyme) (Terminal deoxynucleotidyltransferase) (TDT) (Terminal transferase) (P09838)
Organism: Mus musculus (Mouse)
Function: Transferase that catalyzes the nontemplated addition of nucleoside triphosphate to coding ends during V(D)J recombination (N addition). Involved in the generation of diversity in the antigen-binding region of immunoglobulin heavy and light chains and T-cell receptors during B- and T-cell development. Does not act on double-stranded DNA with blunt ends.
Subcellular location: [Isoform TDT-S]: Nucleus {ECO:0000269|PubMed:7556063}.; SUBCELLULAR LOCATION: [Isoform TDT-L]: Nucleus {ECO:0000269|PubMed:11136823}. Cytoplasm {ECO:0000269|PubMed:7556063}. Note=The subcellular location is controversial. Detected in the nucleus (PubMed:11136823). Found mainly in the cytoplasm (PubMed:7556063). {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:7556063}.
Interaction partners:
- Caspase-3
- V
- Deoxynucleotidyltransferase terminal-interacting protein 1
- Apoptosis regulator Bcl-2
- Peroxidasin homolog
- Annexin A5
- Proliferation marker protein Ki-67
- Actin, cytoplasmic 1
- Albumin
- DNA repair protein XRCC4
Sequence:
MDPLQAVHLGPRKKRPRQLGTPVASTPYDIRFRDLVLFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKASSELELLDISWLIECMGAGKPVEMMGRHQLVVNRNSSPSPVPGSQNVPAPAVKKISQYACQRRTTLNNYNQLFTDALDILAENDELRENEGSCLAFMRASSVLKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIEDGESSEAKAVLNDERYKSFKLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYEDLVSCVNRPEAEAVSMLVKEAVVTFLPDALVTMTGGFRRGKMTGHDVDFLITSPEATEDEEQQLLHKVTDFWKQQGLLLYCDILESTFEKFKQPSRKVDALDHFQKCFLILKLDHGRVHSEKSGQQEGKGWKAIRVDLVMCPYDRRAFALLGWTGSRQFERDLRRYATHERKMMLDNHALYDRTKRVFLEAESEEEIFAHLGLDYIEPWERNA
Protein: tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)] (EC 1.3.1.88) (A0A178U7R5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKLNLSNLRFLRTRKSLISQTRAMTQNPDPKPDPSQVLDDILCSEQRDGQIEETVDTAPASLGSPSRVLSIDTRVERAWAHWKKLGRPKYIVAPMVDNSELPFRLLCQKYGAQAAYTPMLHSRIFTETEKYRNQEFTTCKEDRPLFVQFCANDPDTLLEAAKRVEPYCDYVDINLGCPQRIARRGNYGAFLMDNLPLVKSLVEKLAQNLNVPVSCKIRIFPNLEDTLKYAKMLEDAGCSLLAVHGRTRDEKDGKKFRADWSAIKEVKNAMRIPVLANGNVRCIEDVDNCIKETGVEGVLSAETLLENPAAFAGFRTAEWAKDNEEEGFVDGGLDQGDLVVEYLKLCEKHPVPWRMIRSHVHKMLGEWFRIHPQVREQLNAQNILTFEFLYGLVDQLRELGGRVPLYKKKKIDTLTPQDSPQRV
Protein: Peroxisomal membrane protein 2 (22 kDa peroxisomal membrane protein) (P42925)
Organism: Mus musculus (Mouse)
Function: Seems to be involved in pore-forming activity and may contribute to the unspecific permeability of the peroxisomal membrane.
Subcellular location: Peroxisome membrane; Multi-pass membrane protein.
Interaction partners:
- Peroxisomal membrane protein 11B
- Peroxisomal membrane protein 4
- Peroxisomal membrane protein PMP34
- Peroxisomal membrane protein PEX16
- Peroxisomal biogenesis factor 19
- ATP-binding cassette sub-family D member 1
- Acyl-CoA-binding domain-containing protein 5
- Outer mitochondrial transmembrane helix translocase
- ATP-binding cassette sub-family D member 3
- Peroxisomal membrane protein PEX13
Sequence:
MAPAASRLRVESELGSLPKRALAQYLLLLKLYPVLTKAVSSGILSALGNLLAQTIEKKQRKDSRLLEVSGLLRYLVYGLFVTGPLSHYLYLFMEYSVPPEVPWASVKRLLLDRLFFAPTFLLLFFFVMNLLEGKNVSVFVAKMRSGFWPALQMNWRMWTPLQFININYVPLQFRVLFANMAALFWYAYLASLGK
Protein: NAD(P)H-quinone oxidoreductase subunit K, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit K) (NADH-plastoquinone oxidoreductase subunit K) (O98679)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. It has NADH- and deamino-NADH-specific dehydrogenase activity, using ferricyanide or quinones as acceptors. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305|PubMed:10202810, ECO:0000305|PubMed:9448329}; Peripheral membrane protein {ECO:0000305|PubMed:10202810, ECO:0000305|PubMed:9448329}; Stromal side {ECO:0000305|PubMed:10202810, ECO:0000305|PubMed:9448329}.
Interaction partners:
Sequence:
MNSIEFPLLDQKTKNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDAITKLRKKISREIDEDPISYQRENRSFTTNHKFDVGRSTHTGNSNQGLFYQPSSISEMTSDTFLKYKKVQYPATNEKVN
Protein: Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (Immunoglobulin heavy chain-binding protein homolog) (BiP) (Q6FW50)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P16474, ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Heat shock protein 70 homolog LHS1
- Candida glabrata strain CBS138 chromosome G complete sequence
- Derlin
- Nucleoporin NSP1
- Protein disulfide-isomerase
- Ribosome-associated molecular chaperone SSB
- protein disulfide-isomerase
- Nucleotide exchange factor SIL1
- Candida glabrata strain CBS138 chromosome D complete sequence
Sequence:
MNAIKRLLPVSLFLYALFVVLLPFQARAKDDVENYGTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQIAANPTNTIFDIKRLIGLKFNDRSVQRDIKHLPFKVVDKDGKPVVQVKVKGEDRVFTPEEISGMILGKMKQIAEDYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKTFKKKHGIDVSDNEKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLEDAGLEKKDIDDFVLVGGSTRIPKVQQLLESFFNGKKASKGINPDEAVAYGAAVQAGVLSGEEGVEDIVLLDVNALTLGIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVQIKVYEGERAMSKDNNLLGKFELTGIPPAPRGIPQIEVTFALDANGILKVSATDKGTGKSESITITNDKGRLTQDEIDRMVEEAEKFASEDAVLRTKIEARNKLENYAHSIKNQVEGDLAEKLEEEDKETLLDAANDTLEWLEDNFDSATTEEFEEKFEALSKTAYPITSKLYGGADGSAPVYDDDEDEDDDTDYFDDEL