wanglab/gogpt-training-data huggingface dataset:
Protein: Protein ANTI-SILENCING 1 (Protein INCREASE IN BONSAI METHYLATION 2) (Protein SHOOT GROWTH 1) (Q9LYE3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required to prevent promoter DNA hypermethylation and transcriptional silencing of some transgenes. Plays a similar role to that of the histone H3K9 demethylase JMJ25/IBM1 in preventing CHG methylation in the bodies of numerous genes. RNA-binding protein that ensures the proper expression of JMJ25/IBM1 full-length transcript by associating with an intronic heterochromatic repeat element of JMJ25/IBM1. May associate with intronic heterochromatin and bind gene transcripts to promote their 3' distal polyadenylation. Contributes to a unique mechanism to deal with the collateral effect of silencing intronic repeat elements.
Interaction partners:
- protein SLOW GREEN 1
- Protein ENHANCED DOWNY MILDEW 2
- Lysine-specific demethylase JMJ25
- Protein PARALOG OF AIPP2
- F-box protein At1g11270
- Mediator of RNA polymerase II transcription subunit 7b
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH6
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH5
Sequence:
MEESVASEGLEFKWGKKKGVGGKKKDVQFYESFTYDGDEYRLYDCVLVGNASEPDSTEPFIGMIIKIWEHANKHIPKKVKLLWFFKPSEIAPYLEGVPNVLANEVFLASGEGLGLANTNQLEAIGGKCSVLCISKDKRNPQPSDEKFNSADFVFCRAFDVGSCKVVDTIDDKIAGVDVKFIFNRACSEKEATAVQNIEADVNGKSDSLKPNGPLARGASGSVRKIEDSAFESSDCKENSNGCKEEKEKGHYQLAIKKSTLAEERSNKDSGSRGNHYNGKDQESEVKKQLTKQKSMPGEERYSNSFEASGSRTIHSISKKAQENDVKKQLTKQKSMPAGERYSQESSGLDDRPLKKQKLDGSVTVRDGWDTTILQNITSDGKKDTGSFKRPRDKVTIEEVPPEKRSFVKNRDLVVSVSEGKTTKTVTEKGISKKPSFGRAEDKMSADDNERNYQVTEVCRRPDAGKSKWFRSLPWEESMREAEKKGTVVLLQNLDPTYTSDEVEDIVYSALNQQCEARMIERTSVTIPHIGEALVIFKTREVAERVIRRLDEGCLLLSSGRPLVASFAKITPPGKPSLFSGHIKLHKTQTRREMRDAVATSHSSQPNNLEFDMAMEWCLHQARHEQASESVSKRQLEEMKSLRINFKLKLP
Protein: Ribosomal protein S4 (Q8HCN9)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MPALRFKTCRLLLGNVWNRELSLIQRRILRRLRNKRRSIKRNLSQRENLNSNIKLQTTRKLSLYYGDLPIREMHRGRERTSYIPFLLNQETRLDVILVRLHFCDTLPQARQLISHRRVCLNNGLVTITHLKVSHGDLISFQENDARTRGEEIRRSFYIDILVGKIIGKLLPVRIWRKTKTEWFRLLTTQRVCRLLLKSWFLQELRSYMQEEDLERTKKFGSAKVCLGSSFAEHNRMKRNLFHFKYFFLLKRRKEEEELIRTIGEAENRKRAISPFVYKSSLYRNSTYCSGSPFTRKIRIKRIELPTHYLEVNYRTLKAVVFYGPNIGHIPHDIRLKDLNLLLWSGNGRGQNI
Protein: TNF alpha induced protein 8 like 3 (A0A1B0GTK8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDSDSGEQSEGEPVTAAGPDVFSSKSLALQAQKKILSKIASKTVANMLIDDTSSEIFDELYKVTKEHTHNKKEAHKIMKDLIKVAIKIGILYRNNQFSQEELVIVEKFRKKLNQTAMTIVSFYEVEYTFDRNVLSNLLHECKDLVHELVQRHLTPRTHGRINHVFNHFADVEFLSTLYSLDGDCRPNLKRICEGINKLLDEKVL
Protein: Zinc finger protein lin-13 (Abnormal cell lineage protein 13) (Q11107)
Organism: Caenorhabditis elegans
Function: Involved in repression of vulval fate, possibly by a tumor suppressor protein Rb-mediated mechanism. May act in a common pathway with retinoblastoma-like protein homolog lin-35 and hpl-2 to influence the ER stress response in the intestine. Plays a role in recruiting chromobox protein homolog hpl-2 to specific chromatin sites.
Subcellular location: Nucleus {ECO:0000269|PubMed:10880475, ECO:0000269|PubMed:16890929}. Note=Localization to nuclear foci overlaps partially with chromobox protein homolog hpl-2. {ECO:0000269|PubMed:16890929}.
Interaction partners:
- Chromo domain-containing protein.
- Protein lin-61
- RING-type domain-containing protein
- Protein let-418
- MOG interacting and ectopic P-granules protein 1
- Retinoblastoma-like protein homolog lin-35
- Protein lin-15B
- Transcription factor dpl-1
Sequence:
MDEFELFQQLNQTAPLVKTEEPEVPDEFQQANNNQSAPLRTGLSDLSHEIAAAKQREEEEAQRLADFMQKDMKEPAVKRKRGSEEYKKDPLESKAPLSTFGHSSRPRRSVNYASIERGDEAQAQSLVTDFGSRGNRKKPKRTRDELDENYMEENEGNSGRKKKPNAKGASRQFQVPGLPTYASQYSRPPKQEDVFKTIVPLAEDARAEGERVIGFRLDSQPAVRRASGGFRRFCAWLSDNQIFSIMQTVDKLCIVGANNEDHDEILLKSIRHVYNAMPPTFRRDWEYAARKDVFDSRLFVQNMPMPLSEISVTDPRHPPSPIARGTTVRPNCCENQPLFLNMCETIEHYLGHHDVVHLFGCDICYRVYPSRYELTKHDCKEFAEYLRQLTFKQQTLHLEAAYMYLCCSQCGLWLSVKPSGEGKKGWTYFATALMNHSCQPLVPVVAYFPKPLKDEGKGIRIQFQVMSELNIGLPLSCSECNIEEFHSVVEIEEHFKEKHEANHTCIKCGKTFGTEFMLKHHAQSHTTQTAQFANYLQMSATYQPPPSSGRLPYVGFGSSIPAIGGLTSGEVQALEASENKKSEFVEPDEYTIRKKLLRWKHAKTKKENRNITDSNEKEFSYEPGESSGEEDFQKSLLEQDNQSSSSSDSDSDSDDFTSSKQKKKRNIKIRGDLGYEHINRNKFFERPESEKEARKRIEKVYKKHVLLSRERLLDPEEALRILEESRMVHLNSIQSTLADDIAMSCIRTISLPASNCIDPLKDLLLVNKIFYFCTKCNYIFSKDPVVHCLSCEVTEDDLIEVYHAASGPHAGVRCIDPECKAHLCSVISLKTHLSDVHSKQATLELVSGELDNFSENRFDRSLMLMAKHFTQLQFDERTYLARFTDIECFMPFSGLLEAKDQPRPMPIRQQPQQIKPAYSLVRPDIIAPNELMRPYTLTPAIRPGQRIKPYKVPRTSRWYSCSWCDREYESLNQFVDHLTRFHTHPCPSCGKAFSSQNTRRTHVCSRLFAEIKGRGATLCGQCPSCPEIHQVERIFVHMLNRHFSTIEYVLATGELLPPARDVGIRYNHGENGGYGRSYESLRAIEQSVVDPRSPDYRLKQVKISALPIHGVELNRLPARDPPMGSFTVCPPKDKNIDPRLMCYMCELTFDSYDELTHHMDDHPEKWANCPFCAANTPTHFDLQKHLIQEHVVQISGQACCAFCQEHHRFMSSHILFRCKRVSRCTICGVKSNDPLANRVHIQRSHALTLRRFQCAYCIKVFVSVGEYYEHECASGGGRVYSCTCSPNKFFNSPIEFCDHFDSVHILRNKCQLCSYDAPSQDGMVKHRKTHMRSGCPKEQTKKLFILMKCLFPKHNSGYMRFIEGGPVPASYQDVDRSQMNYLMCNMGTVSPSCHKSYAQAPRTLLEALEGVASDSRSGGLQKVVNVTTRMNEPSSSDVIMLSDDEDDDCVVFEKAVPNGVAQGSSTSTPNPESSINCEVRVETSQAGYGGAQQPGYVDEDDTDLEVAQGGKSPYGEPVVKEVVDENGDDELAVVAEVENSTGTLPSSISAGREKKFKCQKCSLAFYTNGSLESHMRDHRQDAGAQLCTETYGIPVVTKASWLCRNCCVVFENQPKYQKHMAIHGDTCLTCIHCSGIAFNHTAIQNHMKSHEEKKVRYSCGTCLCTFASDLALFDHLSVAHGVSLYYFCKVCGFGSTSADSVFQHISIHNGHNYSLVQRFGACPAQLLNYDPTDELEFRSQILNKTIQLVSPSDCSHRSMLLQCETVVSCKTCHCTQAWFNYMAFNNHSEETGFPQFKNVDLANDYRRDFPLSRHLNERNALSMSQFGNAKHGSANHSHGQAQPNKRTFRHEVPYRTAAPRSSLQTNGSSMGSVTTNGGRVVRPSPPNSMNVTLRRAPPQQAPPRRIVIANSAPNNTNVLRNHVAVTTKCQFKDCDKVLHSEFDRQLHSMHSSNSSWFCRQCGHSPKSEIDLFLHYIQVHLKPAYDKHQSNSFKSNVFHLKCPIRSCTSPEFQSPKAFEKHMRTAHAAELPFEASCCDARFASKALCVKHDQEHASFLDSNGTDASCCPICGSLSMWSLPKDPHTDCLQSHIIRHGLDYRSSCRQCLKQFPADVNQDQVIAHILDTHGMSMHGNTFHCNLCTTGTKTVEEFAEHCRKAHVFHILVKSSHSTRGELVVTTGQEYENYVGLKSVTRASLNSISSQRASNAGETAQPSVLCAGSGNAALLTIAAAIGEPETSNNTAEVLTLD
Protein: NADH-cytochrome b5 reductase (EC 1.6.2.2) (Q9I7R1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTEFDFVPLAVGVVAVLAGALIVHYLLNKKSTKPRREPNRTARLRTLVDPNDKYLLPLIEKENLSHDTRRFRFGLPSKQHVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYFKDSHPKFPAGGKMTQHLEQLELGDKISFRGPSGRLQYLGNGTFSIKKLRKDPPKHVTAKRVNMIAGGTGITPMLQLAREVLKRSDKDKTELALLFANQSEKDILLRAELDELAQKHPDQFKIWYTVDKANEGWQYSVGFINEEMIAAHLLPAKDDTIVLLCGPPPMINFACNPALDKLGYHPDTRFAY
Protein: Serine/threonine-protein kinase BSK7 (EC 2.7.11.1) (Brassinosteroid-signaling kinase 7) (F4I3M3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Functions redundantly with BSK3, BSK5, BSK6 and BSK8.
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor {ECO:0000255}.
Interaction partners:
- Serine/threonine-protein phosphatase BSU1
- Protein BRASSINOSTEROID INSENSITIVE 1
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- Shaggy-related protein kinase eta
- Putative acyl-activating enzyme 19
- Protein BRASSINAZOLE-RESISTANT 1
- Shaggy-related protein kinase iota
- Auxin-responsive GH3 family protein
Sequence:
MGCEVSKLCAFCCVSDPEGSNHGVTGLDEDRRGEGNDLPQFREFSIETLRNATSGFATENIVSEHGEKAPNVVYKGKLDNQRRIAVKRFNRKAWPDSRQFLEEAKAVGQLRNYRMANLLGCCYEGEERLLVAEFMPNETLAKHLFHWESQPMKWAMRLRVALHIAQALEYCTGKGRALYHDLNAYRVLFDDDSNPRLSCFGLMKNSRDGKSYSTNLAFTPPEYLRTGRVTPESVMYSYGTLLLDLLSGKHIPPSHALDLIRDRNIQMLIDSCLEGQFSSDDGTELIRLASRCLQYEPRERPNPKSLVTAMIPLQKDLETPSHQLMGIPSSASTTPLSPLGEACLRTDLTAIHEILEKLSYKDDEGAATELSFQMWTNQMQDSLNFKKKGDVAFRHKEFANAIDCYSQFIEGGTMVSPTVYARRSLCYLMNEMPQEALNDAMQAQVISPAWHIASYLQAVALSALGQENEAHAALKDGSMLESKRNRL
Protein: Fibronectin type-III domain-containing protein (G5EGA4)
Organism: Caenorhabditis elegans
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Nidogen
- Basement membrane proteoglycan
- Agrin
- GlyPicaN
- Probable syndecan
- D-glucuronyl C5-epimerase
- Laminin EGF-like domain-containing protein
- Fibulin-1
- Laminin-like protein epi-1
- Dystroglycan 1
Sequence:
MIETGSQYLLFLLFICSLFNSGSTALQHEDRVPNAPQNVRIKTQSTSATLWWDAPPDPTVLIRGYTVEYGEGSISQRILIEGPDSTSFTVTRLSPNTNYVFAVSAYNEAEGEDGTKVMVAAKTRPSEGSQTEKLWPPTSVRARIDEKSAAGSAFVSWDDPNPESSSENSIDSTQKQYVINYGIYESDTQQKVRSNAKAVRLTGLIPGKEYEVAVKVVAGDGRESPWSIRDLFLVPETKTVSKFDWFCRLNDTEMCSIHSSPHWKLCSEKHDTYTQRDAGACPRVQYPSSPAHLTTPAINLPDAQRLCLYFRFALLNFHPGQMKVEIFRDGDMANKQIVWKTRMANVRTHVVQNVYVPFSQQIKPFKVSVSLKWDGQPMPRVIVHEMDVLSGGCSERSTDSETEVDLLAPVKASLNADARVFRAKGIESLPAIGLQRGVEIAVPYRLYLPRNFFKQFSLLATIKPMDKRGGYLFAAVNAYDSAVDIGLLIEPAGTKQTNISLIVRSVAIVSFLVEDFSQQWTQFALEVVDQTVTFYFKCRRFASRQVTSLPDFSFDEAEKLYIASAGPIIDNGFEGAIQELKLIDDATQGSRQCDEQWWRRRKIEKELQGRKGAEGSGTPEEFKKTQESSELQKISDFPPTPAPPPPYPTPQLAPHDLFLSDDSLVVPFIGGYGSPAARDLRSYEQQAATTPFQGAPPSNQCTQVCRGEPGPQGPSGNDGIPGSHGAPGHQGERGADGAPGLHGSRGDQGLPGPPGMPGLAGPPGPPGSGTGHGSGADGPQGPPGLPGAPGRDGTSGVEGQRGPQGPPGPKGDDGVSMESLTDDDIERIARRVASIQKESNEPMRGDLPEYNSKVHSFTTKGEKGERGAPGAPGAPAPPAYGTLTTGTAVNVHATTVELFASARSTSVGQLAFATSSQQLFIRVTNGWKEIQLTHFHPFVETRHSTQNSRQNDASHAGRSRTGSAAAPWYPKANLDEPQRDAGVHNKDRVIHMIALSQPFSGNLHGLRGADLQCYREARAAGYTTTFRAMLSSNVQDLVRIVHSVDFDTTVVNVAGHHLFPSWRSFVNGAQMNPHAKLFSFDRHDVLNDSRWPDKRVWHGSKDGGIRAEQYCDGWRRADSSLTSLAGHISSNTSIFQSSGSEKCENKLVVLCVENMSKYHGDRILRLHRITSDFKK
Protein: L-serine dehydratase 2 (SDH 2) (EC 4.3.1.17) (L-serine deaminase 2) (L-SD2) (P30744)
Organism: Escherichia coli (strain K12)
Function: Deaminates also threonine, particularly when it is present in high concentration.
Interaction partners:
- Serine transporter SdaC
- D-serine dehydratase
- Serine hydroxymethyltransferase
- Phosphoserine phosphatase
- L-threonine dehydratase biosynthetic IlvA
- L-threonine dehydratase catabolic TdcB
- Serine acetyltransferase
- L-serine dehydratase 1
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
- L-serine dehydratase TdcG
Sequence:
MISVFDIFKIGIGPSSSHTVGPMKAGKQFTDDLIARNLLKDVTRVVVDVYGSLSLTGKGHHTDIAIIMGLAGNLPDTVDIDSIPSFIQDVNTHGRLMLANGQHEVEFPVDQCMNFHADNLSLHENGMRITALAGDKVVYSQTYYSIGGGFIVDEEHFGQQDSAPVEVPYPYSSAADLQKHCQETGLSLSGLMMKNELALHSKEELEQHLANVWEVMRGGIERGISTEGVLPGKLRVPRRAAALRRMLVSQDKTTTDPMAVVDWINMFALAVNEENAAGGRVVTAPTNGACGIIPAVLAYYDKFIREVNANSLARYLLVASAIGSLYKMNASISGAEVGCQGEVGVACSMAAAGLAELLGASPAQVCIAAEIAMEHNLGLTCDPVAGQVQVPCIERNAIAAVKAVNAARMALRRTSEPRVCLDKVIETMYETGKDMNAKYRETSRGGLAMKIVACD
Protein: Intraflagellar transport protein 70A1 (Tetratricopeptide repeat protein 30A1) (TPR repeat protein 30A1) (Q99J38)
Organism: Mus musculus (Mouse)
Function: Required for polyglutamylation of axonemal tubulin. Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip.
Subcellular location: Cell projection, cilium {ECO:0000250}.
Interaction partners:
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 57 homolog
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 56
- Intraflagellar transport protein 80 homolog
- Intraflagellar transport protein 172 homolog
- TRAF3-interacting protein 1
- Intraflagellar transport protein 27 homolog
Sequence:
MAWQSSSKVPDGEFTAVVYRLIRDSRYSEAVQLLSAELQRSSRSRAGLSLLAYCYYRLQEFELAAECYEQLSQMHPELEQYRLYQAQALYKACLYPEATRVTFLLDNPAYQTRVLRLQAAIKYSEGDLPGARSLVEQLLSGEAGEDSGGENDPDGLVNMGCLLYKEGHYEAACSKFLAALQASGYQPDLSYNLALAYYSSRQYAPALKHIADIIERGIRQHPELGVGMTTEGIDVRSVGNTVVLHQTALIEAFNLKAAIEYQLRNFEVAQETLTDMPPRAEEELDPVTLHNQALMNMDAKPTEGFEKLQFLLQQNPFPPETFGNLLLLYCKYEYFDLAADVLAENAHLTYKFLTPYLYDFLDAMITCQTAPEEAFIKLDGLAGMLTEQLRRLTKQVQEARHNRDDEIIKKAMNEYDETLEKYIPVLMAQAKIYWNLENYPMVEKIFRKSVEFCNDHDVWKLNVAHVLFMQENKYKEAIGFYEPIVKKNYDNILSVSAIVLANLCVSYIMTSQNEEAEELMRKIEKEEEQLSYGDPDKKIYHLCIVNLVIGTLYCAKGNYDFGISRVIKSLEPYHKKLGTDTWYYAKRCFLSLLENMSKHMIVLCDGVVQECVQFLEYCELYGRNIPAVLEQPLEEERIHTGKNTVTYESRLLKALIYEVIGWNM
Protein: Varicose-related protein (Q9LTT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: As a component of the decapping complex, may play a role in the degradation of mRNAs.
Subcellular location: Cytoplasm, P-body {ECO:0000250}.
Interaction partners:
- mRNA-decapping enzyme-like protein
- mRNA-decapping enzyme subunit 2
- Enhancer of mRNA-decapping protein 4
- DEAD-box ATP-dependent RNA helicase 12
- DEAD-box ATP-dependent RNA helicase 6
- Decapping 5-like protein
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- Protein PAT1 homolog 2
- DEAD-box ATP-dependent RNA helicase 8
- Pumilio homolog 4
Sequence:
MASSPGNTNPHNPPPFDLGTIFKPSSNPYPPPTGPFLNNQYNQQLYAPPGIAAQPSPVNQTQQDVSSSSSATNLQPQRTLSYPTPPLNPQSPRVNHNPGTHILALLNNGGAVANQEPSHHNEIARAFPGGSGPIHVPSGKMPKGRRLVGEHAVYDVDVRLQGEIQPQLEVTPITKYGSDPQLVLGRQIAVNKVYICYGLKGGSIRVLNINTALRSLFRGHSQRVTDMAFFAEDVHLLASVSLDGKVFVWKISEGSEGDEQSQITGKIVVALQILGEEDTKHPRVCWHCHKQEILVVSIGKHVLRIDTTKVGRGEVFSAEAPLQCHLDKLIDGVQIVGKHDGEVTDLSMCQWMTTRLVSSSVDGTVKIWQDRKTQPLVVLRPHDGLPVNSAIFVTSPERPDHIILITGGPLNREIKIWVSAGEEGWLLPADTESWRCTQTLDLKSSTEPQAEKAFFNQVIALSEAGLLLLANARRNAIYSVHLDYGSSPVETLMDYLSEFTVTMPILSFIGTNDHPEEPFVKVYCVQTLAIQQYTLDLFLCMPPPRENVGFEKSDSTVSREANLVESTLETSGMKPTELPSVGSVPKPSILVNRSENANMLSFPAGPASAGITPPAIVPPNGEPKTSGMPSETSDVDSAYAPSPQLPLSPRLSSKLSGYHTPVEAFEQVLPHHKLGGKTSSADYFYVRQTDDVGGRNLDVSSVEENCRSKDTNVTPDDDVSGIRSPSAFFKQPTHLVTPSEILMGVSSTEASITTEDKRDRDANIEEVNNDARGLEVELKEVGEAQTSQNGEINYHETTENHTSESRENIFCSQASNLSTEMARDRHPITEGSAIPGDSMAYGQPLQAGDERGLDSRDVSAKLPESGSSSGLVATNSKGKKQKAKNSQGPGLSSTSSNVANLADSFNEQSQSLNHPMADLLPQLLALQETMTQVMASQKEMQRQLSNAVTGPIVKEGKKLEVALGRMIEKSSKSNADALWAHFQEEAVKNEKALRDHGQQIMNETTNFTSKELNAMFEKTMKKEFASVGPTLARVVTPVIEKTVSSAITESFQRGIGDKAVNQLEKSVNSKLETTVARQIQAQFQTSGRQVLQEGLRSSMESSVIPSFERSCKTMFEQVDSTLQKGIGKHTSATQQRIDSGQSQLAHTLRETISSASSVTQALNRELAESQRNRLALTAAGSNPLVTQLSNGPLGALLEKVEAPMDPTTELSRLISERKYEESFTSALQRSDVSIVSWLCSQVDLRGLLAMNPLPLSQGVLLSLLQQLACDISTDTSRKLGWMTDVVTAINPSDQMIAVHARPIFEQVYQILHHHRNAPGSDVSAVRLIMHVINSLLMSCK
Protein: Protein SIP18 (P50263)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Protein GRE1
- Protease A inhibitor 3
- Stationary phase protein 4
- Protein DDR2
- Uncharacterized protein YJL144W
- Inactive diphosphatase DCS2
- ATPase-stabilizing factor 15 kDa protein
- 12 kDa heat shock protein
- Transketolase 2
- Protein FMP16, mitochondrial
Sequence:
MSNMMNKFAEKLQGNDDSHQKGKNAKSSNKERDDMNMDMGMGHDQSEGGMKMGHDQSGTKMNAGRGIANDWKTYENMKK
Protein: Protein PHOTOSYSTEM I ASSEMBLY 2, chloroplastic (A0A1D6KL43)
Organism: Zea mays (Maize)
Function: Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI) during plant development. May form a complex with PSAG and mediate thiol transactions in the thylakoid lumen that are important for the assembly of PSI. Possesses protein-disulfide reductase activity in vitro.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:25228689}.
Interaction partners:
- magnesium chelatase
- magnesium chelatase
- Magnesium protoporphyrin IX methyltransferase chloroplastic
- Bystin
Sequence:
MASSGSCHSLLSSASPISPALFSRHRAAAVGGGASRASKVQSQVRCLARDEDSKGCANVSKAETNEEKETTPSSRRRCLVCLGAVTLISATGPPNGLAADAMNKAGVQKAVCRNCNGSGAVICDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLVCPVCLGTGLPNNKGLLRRPEAKQLLDKMYNGKILPRS
Protein: P-selectin (CD62 antigen-like family member P) (Granule membrane protein 140) (GMP-140) (Leukocyte-endothelial cell adhesion molecule 3) (LECAM3) (Platelet activation dependent granule-external membrane protein) (PADGEM) (CD antigen CD62P) (Q01102)
Organism: Mus musculus (Mouse)
Function: Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with SELPLG.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P16109}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16109}.
Interaction partners:
- P-selectin glycoprotein ligand 1
- Platelet glycoprotein Ib alpha chain
- von Willebrand factor
- CD44 antigen
- Signal transducer CD24
- L-selectin
- Golgi apparatus protein 1
- Tumor necrosis factor receptor superfamily member 5
- Sorting nexin-17
- Integrin alpha-IIb
Sequence:
MAGCPKGSWTPRLRSVILGGAQLIWFSALISELVNQKEVAAWTYNYSTKAYSWNNSRVFCRRHFTDLVAIQNKNEIAHLNDVIPFFNSYYWIGIRKINNKWTWVGTNKTLTEEAENWADNEPNNKKNNQDCVEIYIKSNSAPGKWNDEPCFKRKRALCYTASCQDMSCSNQGECIETIGSYTCSCYPGFYGPECEYVKECGKVNIPQHVLMNCSHPLGEFSFNSQCTFSCAEGYELDGPGELQCLASGIWTNNPPKCDAVQCQSLEAPPHGTMACMHPIAAFAYDSSCKFECQPGYRARGSNTLHCTGSGQWSEPLPTCEAIACEPPEIPIHGSMDCVPSTGTFGYNSSCTFLCAEGFVLKGNDAIQCADSGQWTAPAPFCEALQCPEFPVPSKAQVNCSDPFGTLTYQSVCSFSCDEGSLLVGASVIRCLATGHWNGAPPECQAVSCAPMLSPENGSMTCVQPLGNSTYKSTCQFMCDEGFYLSGPERLDCSPSGHWTGTPPTCEAIKCPGIFAPEQGNLDCSHVHGEFGVGSICHFSCNEDFELLGSENVECTVSGRWSAPPPTCKGITSLPAPAVRCPALTTPGQGTMSCQHHLGSFGPNTTCYFGCKTGFTLRGANSLRCRASGQWTAVTPMCRAVKCSELHMDTAVAMNCSNPWGNFSYGSTCTFQCPEGQSLNGSVRATCREDGHWSDAMPTCQAGTLTIQEALTYLGGAVASTTGLAVGGTLLALLRKRLRKKDDGKCPLNPHSHLGTYGVFTNAAYDPTP
Protein: Cylicin-1 (Cylicin I) (Multiple-band polypeptide I) (P35663)
Organism: Homo sapiens (Human)
Function: Possible architectural role during spermatogenesis. May be involved in spermatid differentiation.
Subcellular location: Cytoplasm, cytoskeleton, perinuclear theca, calyx {ECO:0000269|PubMed:38013430, ECO:0000269|PubMed:38573307, ECO:0000269|PubMed:8354692}. Cytoplasm, cytoskeleton, perinuclear theca {ECO:0000250|UniProtKB:A0A1B0GR13}. Note=Localizes to the subacrosomal layer of the perinuclear theca in round and elongating spermatids. Localizes to the calyx, also known as post-acrosomal region, in spermatozoa. {ECO:0000250|UniProtKB:A0A1B0GR13}.
Interaction partners:
- Calicin
Sequence:
MSLPRLLKVNIRTYDNSIPISESSRKSWNQKHFALTFPKPLQRGTNDKSRPLKSQITVTRHDKRKLEEGQKPAHKWIRHSFRKILQWPPIYTAAREQTPFRHLYTSKTHLKKAEYKKSKDEKGGTPLKKDSKKKGGSYATNPESKQIVEEKTKRQNEADKTPLKSSHENEQSKKSKSSSETNPESQNSKTVSKNCSQKDKKDSKNSKKTNTEFLHTKNNPKKDLKRSKTSNDPISEICSENSLNVDFLMLVGQSDDESINFDAWLRNYSQNNSKNYSLKYTKYTKKDTKKNAKKSSDAESEDSKDAKKDSKKVKKNVKKDDKKKDVKKDTESTDAESGDSKDERKDTKKDKKKLKKDDKKKDTKKYPESTDTESGDAKDARNDSRNLKKASKNDDKKKDAKKITFSTDSESELESKESQKDEKKDKKDSKTDNKKSVKNDEESTDADSEPKGDSKKGKKDEKKGKKDSKKDDKKKDAKKNAESTEMESDLELKKDKKHSKEKKGSKKDIKKDARKDTESTDAEFDESSKTGFKTSTKIKGSDTESEESLYKPGAKKKIDESDGTSANSKMEGLESKRGFRMSSKKTTFNEKGEKASTGRVPPSREKPPLPACEPSLPSPKVRRLCWCKMPPPPPKPRYAPLPEAPWIHKLL
Protein: Adenylate isopentenyltransferase 4 (AtIPT4) (EC 2.5.1.112) (Adenylate dimethylallyltransferase 4) (Cytokinin synthase 4) (Q9SB60)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cytokinin biosynthesis. Catalyzes the transfer of an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP and ADP, but not to AMP. Has no DMAPP:tRNA isopentenyltransferase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14726522}.
Interaction partners:
- Cytokinin hydroxylase
- Cytokinin hydroxylase
- Isopentenyl-diphosphate Delta-isomerase II, chloroplastic
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
- Cytokinin dehydrogenase 2
- Cytokinin dehydrogenase 3
- Cytokinin dehydrogenase 1
- Cytokinin dehydrogenase 7
- Cytokinin dehydrogenase 5
Sequence:
MKCNDKMVVIMGATGSGKSSLSVDLALHFKAEIINSDKMQFYDGLKITTNQSTIEDRRGVPHHLLGELNPEAGEVTAAEFRVMAAEAISEITQRKKLPILAGGSNSYIHALLAKSYDPENYPFSDHKGSICSELKYDCCFIWIDVDQSVLFEYLSLRLDLMMKSGMFEEIAEFHRSKKAPKEPLGIWKAIGVQEFDDYLKMYKWDNDMDKWDPMRKEAYEKAVRAIKENTFQLTKDQITKINKLRNAGWDIKKVDATASFREAIRAAKEGEGVAEMQRKIWNKEVLEPCVKIVRSHLDQPINYYYYYFYLLKRFLSLN
Protein: Glucose-1-phosphate thymidylyltransferase 2 (G1P-TT 2) (EC 2.7.7.24) (dTDP-glucose pyrophosphorylase 2) (dTDP-glucose synthase 2) (P61887)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.
Interaction partners:
- dTDP-glucose 4,6-dehydratase 2
- dTDP-glucose 4,6-dehydratase 1
- dTDP-4-dehydrorhamnose reductase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- dTDP-fucosamine acetyltransferase
- dTDP-4-amino-4,6-dideoxygalactose transaminase
- Lipid III flippase
- UDP-N-acetyl-D-mannosaminuronic acid transferase
- UDP-N-acetyl-D-mannosamine dehydrogenase
- UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPEDKGYFQRLLGDGSEFGIQLEYAEQPSPDGLAQAFIIGETFLNGEPSCLVLGDNIFFGQGFSPKLRHVAARTEGATVFGYQVMDPERFGVVEFDDNFRAISLEEKPKQPKSNWAVTGLYFYDSKVVEYAKQVKPSERGELEITSINQMYLEAGNLTVELLGRGFAWLDTGTHDSLIEASTFVQTVEKRQGFKIACLEEIAWRNGWLDDEGVKRAASSLAKTGYGQYLLELLRARPRQY
Protein: Biotin carboxyl carrier protein of acetyl-CoA carboxylase (BCCP) (P0ABD8)
Organism: Escherichia coli (strain K12)
Function: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
Interaction partners:
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- Biotin carboxylase
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- Malonyl CoA-acyl carrier protein transacylase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
- Bifunctional ligase/repressor BirA
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Phosphate acetyltransferase
- Probable pyruvate-flavodoxin oxidoreductase
Sequence:
MDIRKIKKLIELVEESGISELEISEGEESVRISRAAPAASFPVMQQAYAAPMMQQPAQSNAAAPATVPSMEAPAAAEISGHIVRSPMVGTFYRTPSPDAKAFIEVGQKVNVGDTLCIVEAMKMMNQIEADKSGTVKAILVESGQPVEFDEPLVVIE
Protein: Cilia and flagella associated protein 68 (E9PS33)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
Sequence:
MEQPSKDFCDSHKKSSKSSTYSASSYSSSGKRQNLACFLTNPHCGSLVNADGHGEVWTDWNNMSKFFQYGWRCTTNENTYSNRTLMGNWNQERYDLRNIVQPKPLPSQFGHYFETTYDTSYNNKMPLSTHRFKREPHWFPGH
Protein: DNA-directed RNA polymerase subunit Rpo7 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit E) (P39466)
Organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00865}.
Interaction partners:
- DNA-directed RNA polymerase subunit Rpo11
- DNA-directed RNA polymerase subunit Rpo3
- DNA-directed RNA polymerase subunit Rpo6
- DNA-directed RNA polymerase subunit Rpo5
- DNA-directed RNA polymerase subunit Rpo12
- DNA-directed RNA polymerase subunit Rpo10
- DNA-directed RNA polymerase subunit Rpo2
- DNA-directed RNA polymerase subunit Rpo1C
- DNA-directed RNA polymerase subunit Rpo1N
- DNA-directed RNA polymerase subunit Rpo4
Sequence:
MFKLVRAKGIVRIPPEYFGQSVDEIAIKILRQEYQEKLIKDIGVVLGIVNAKASEEGFIIFGDGATYHEVEFDMLVYTPIIHEVIEGEVSQVDNYGVYVNMGPVDGLVHISQITDDNLKFDSNRGILIGEKSKKSIQKGDRVRAMIISASMSSGRLPRIALTMKQPYLGKIEWINQEIAKASK