wanglab/gogpt-training-data huggingface dataset:
Protein: C-1-tetrahydrofolate synthase, cytoplasmic (C1-THF synthase) [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9); Formyltetrahydrofolate synthetase (EC 6.3.4.3)] (P27653)
Organism: Rattus norvegicus (Rat)
Function: Trifunctional enzyme that catalyzes the interconversion of three forms of one-carbon-substituted tetrahydrofolate: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate, 5,10-methenyltetrahydrofolate and (6S)-10-formyltetrahydrofolate. These derivatives of tetrahydrofolate are differentially required in nucleotide and amino acid biosynthesis, (6S)-10-formyltetrahydrofolate being required for purine biosynthesis while (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate is used for serine and methionine biosynthesis for instance.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11586}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- Bifunctional purine biosynthesis protein ATIC
- Methionine synthase
- Methylenetetrahydrofolate reductase
- Dihydrofolate reductase
- Formimidoyltransferase-cyclodeaminase
- Methionyl-tRNA formyltransferase, mitochondrial
- Thymidylate synthase
Sequence:
MAPAGILNGKVVSAQIRNRLKTQVTQMQEQVPGFTPGLAILQVGDRDDSNLYINVKLKAAQEIGIKATHIKLPRTSTESEVLKYVISLNEDATVHGFIVQLPLDSENSINTEAVINAIAPEKDVDGLTSINAGKLARGDLKDCFIPCTPKGCLELIKETGVQIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTADLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPDDTKPNGRKVVGDVAYDEAKEKASFITPVPGGVGPMTVAMLMQSTVESAQRFLKKFKPGKWTIQYNKLNLKTPVPSDIAISRSCKPKLIGNLAREIGLLTEEVELYGETKAKVLLSALDRLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLVPSVNGVRKFSDIQIRRLRRLGIEKTDPAALTDDEINRFARLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGHTRTAQFDISVASEIMAVLALTSSLEDMRARLGKMVVASSKKGEPISCEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVGPEGFVVTEAGFGADIGMEKFFNIKCRYSGLQPHVVVLVATVRALKMHGGGPTVTAGLPLPKAYTEEDLDLVEKGFSNLRKQIENARMFGVPVVVAMNAFKTDTDTELDLIGRLSREHGAFDAVKCTHWAEGGQGALALAQAVQRASQAPSSFQLLYDLKLSVEDKIRIIAQKIYGADDIELLPEAQNKAEIYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFVLPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
Protein: Purine permease, putative (Q4WGR0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- allantoinase
- Got1 family protein
- Dihydroorotate dehydrogenase
- adenine phosphoribosyltransferase
- Nucleoside transporter, putative
- Uricase
Sequence:
MDGPDRIGPDHSPRRTLRDKARRLVKTWTTKEGLVGDYNYAYLFTPRIPFTKNIRRTAPFFGLHDRLPVLLAFILGLQHALAMLAGVISPPIILGGSSGANFGDAEYQYLVSTSLIASGLLSAVQMARLRIWKTRYFIGTGLISVVGTSFSTITVASGTFSQMYASGYCPTDANGNRLPCPRGYGAILGTACLCSLLTIGLSFMSPRILKRIFPPMVTGPTVLLIGASLIESGMKDWAGGSGCGSDPSARALCPSAGAPHALPWGSAEFIGLGFLVFVTIILCERFGSPIMKSCAVVVGLLVGCIVAAACGYFDRSGIDSAPVVSFIWVKTFPLTIYAPLILPFLALYIVIMMESIGDITATCDVSQLEVEGADFDSRVQGGVLGNGLTCLLAGLFTITPMSVFAQNNGVIALTKCANRKAGYCCCFFLVVMGVFAKFAAAIVAIPKPVLGGMTTFLFSSVAISGIRIISTIPFTRRNRFILTASFAVGMAATLVPDWFSYFFTYSGDNHALEGLLNAVELVMENGFAITAVIGLVLNLVLPEDPEDEAAIVEATARDAPTEELKDSDPSSLKAGQPSGSLAV
Protein: Histone transcription regulator slm9 (O74309)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probably required for replication-independent chromatin assembly (By similarity). Required for transcriptional silencing in the outer repeat (otr) centromeric repeats and the Tf2 long terminal repeat retrotransposons. May play an indirect role in the regulation of cdc2 and/or wee1 at the G2/M stage of mitosis.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Protein hir1
- Histone promoter control protein 2
- Histone transcription regulator 3 homolog
- Histone chaperone cia1
- UPF0656 protein C926.02
- LIMR family protein C622.11
- Chromatin assembly factor 1 subunit A
- Pre-rRNA-processing protein esf1
Sequence:
MHIFVPKLLENHQFSSISSSKDFVAVSAETNVYILSKDFFYPKSSEKRIIQSLNGHKTTHLSFDSPISCIRFTYDGSCLAVATEAGTFLYHSEKWDKAFQVLSGPAYEVCWSQQGHILATSWKQISIYVKDEGLRTETIVKKTEHADSNHQPAVSIEESKEAVESTSQSSEISFKLIKVIEGHHTFVGGLAFDPMGQFLASQSFDHTLKVWKLSTFGVEKSIAKPFEQMPTGNRFLRLSWSPDGAHIASVNAVNEGAYVIAIVQRDTWTYDINLVGHQGPLECATFNPYLYEDPFQKSIIASAAHDGCVSIWNTACARPMAVIHELSCSSFVDLQWSTSGFELYGVSLDGNLMLLQFEESEFGEKMDTIHYPDDLSYFNSSRSKAHVNKNAAADRTTSPTQGQPESPSKSILLRPPPSIASSPESKRRKCPKKFVARPPVPHPTSLYSQIRIGCPYLKPKLVISKSFGTLIVKNHNQLSLLKCTFSNLDGNDCSWFSYLPNAIVLANGTSVFWAVATEDSSIYIYSPAGRLLLPPVVVAATPCFLECCGDFLCCIVSTGLLYIWNIKNFEAIHSPVSTLPLFHSNFSVSKIARGPSIEQFFVTKQGHPVAIMSDGNAFAFIRDSSSWLRVSEGWWMIGSQYWGPLASESNEESPLGFLERCTDEEIIKAGRGRFLQRLVKALMLRQGYDNYEMLVSIRHLENRLMSSAKLDLEYDFRENLILYAKKIAEEGMKDKMDELCKELLGPLRIPHNGIDTVKVGNRLWSPTIAGNNKRNLLKDIIIHTAKYRDMQRITSQYSDLLRRSALL
Protein: Translocated actin-recruiting phosphoprotein (Tarp protein) (O84462)
Organism: Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx)
Function: Appears to initiate or participate in signaling events that regulate the actin recruitment, which ultimately leads to internalization.
Subcellular location: Secreted. Note=Secreted via type III secretion system and translocated into host cell. {ECO:0000250}.
Interaction partners:
- Type III secretion system effector protein
- Major outer membrane porin, serovar D
- Adherence factor
- Large cysteine-rich periplasmic protein OmcB
Sequence:
MTNSISGYQPTVTTSTSSTTSASGASGSLGASSVSTTANATVTQTANATNSAATSSIQTTGETVVNYTNSASAPNVTVSTSSSSTQATATSNKTSQAVAGKITSPDTSESSETSSTSSSDHIPSDYDDVGSNSGDISNNYDDVGSNNGDISSNYDDAAADYEPIRTTENIYESIGGSRTSGPENTSGGAAAALNSLRGSSYSNYDDAAADYEPIRTTENIYESIGGSRTSGPENTSGGAAAALNSLRGSSYSNYDDAAADYEPIRTTENIYESIGGSRTSGPENTSDGAAAAALNSLRGSSYTTGPRNEGVFGPGPEGLPDMSLPSYDPTNKTSLLTFLSNPHVKSKMLENSGHFVFIDTDRSSFILVPNGNWDQVCSIKVQNGKTKEDLDIKDLENMCAKFCTGFSKFSGDWDSLVEPMVSAKAGVASGGNLPNTVIINNKFKTCVAYGPWNSQEASSGYTPSAWRRGHRVDFGGIFEKANDFNKINWGTQAGPSSEDDGISFSNETPGAGPAAAPSPTPSSIPIINVNVNVGGTNVNIGDTNVNTTNTTPTTQSTDASTDTSDIDDINTNNQTDDINTTDKDSDGAGGVNGDISETESSSGDDSGSVSSSESDKNASVGNDGPAMKDILSAVRKHLDVVYPGENGGSTEGPLPANQTLGDVISDVENKGSAQDTKLSGNTGAGDDDPTTTAAVGNGAEEITLSDTDSGIGDDVSDTASSSGDESGGVSSPSSESNKNTAVGNDGPSGLDILAAVRKHLDKVYPGDNGGSTEGPLQANQTLGDIVQDMETTGTSQETVVSPWKGSTSSTESAGGSGSVQTLLPSPPPTPSTTTLRTGTGATTTSLMMGGPIKADIITTGGGGRIPGGGTLEKLLPRIRAHLDISFDAQGDLVSTEEPQLGSIVNKFRQETGSRGILAFVESAPGKPGSAQVLTGTGGDKGNLFQAAAAVTQALGNVAGKVNLAIQGQKLSSLVNDDGKGSVGRDLFQAAAQTTQVLSALIDTVG
Protein: Early endosome antigen 1 (A0A8I5ZV67)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MFRRILQRTPGRVGSQGSDLDSSATPINTVDVNNESSSEGFICPQCMKSLGSADELFKHYQAVHDAGNDSGHGGEASLALTRDDIALLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKGLRAAAEQKATHLTEELSKQTTVIQDLKTELLQRPGIEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHANSEATINQLRSELAKGPQEVAVYVQEIQKLKGSVNELTQKSQTLMEKLQKKDLDYTHLEEKHNEEALSRKNTQAALHQRDLDCQQLQARLTASEGSLQRIQGELREKGEAAQKLKEELREVETKHQHLKVEFKQLQQQREEKEQHGLQLQGEVSQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLMEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKVSAQLDQVTAKFQEKQEHCTQLESHLKDYKEKHLSLEQKAEDLEGQIKKLEANNLEVKASREQAVQSLQQQRQLSTDLELRNAELRKQLQEQKEVVSHTKLDLQNKSEALENIKQTLTKKEEEKVVLKQEFEKLSQDSEAQHKELSDRMQAAITELMVMTAQKDALLAELSTTKGKLSKVSDSLQTSRSEFEKESQKGKAAVLDLEKACKELKHQLQQQTESALKEQSELKKSLEKERETSQQLMIELNSVKGEVTQAQNTLKQKEKEEQQLQGNINQLKQATEQKKKQMEALQGELKNVTSQKAQLESKLQQQAAQAAQELAVEKGKLSALQSTYDKCQADLQQLQSDLYGKESELLATRQDLKCVEEKLALAQEDLISNRNQIGNQNKSIQELQAAKAALEQDLAKKEEVLKEQSKALQDAQREKSVKEKELVTEKSKLAEMEEIKCRQEKEIAKLKEELKSHKQESIKEVTNLKDAKQLLIQQKLELQGKVDSLKAALEQEKERQQLMREQMRKEEEKRKEEFSEKEAKLHSEIKEKEAGVKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKVLELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKPVRVCDACFNDLQG
Protein: Sex muscle abnormal protein 5 (P29355)
Organism: Caenorhabditis elegans
Function: Adapter protein which modulates signaling mediated by several receptor tyrosine kinases such as egl-15 and let-23 probably acting upstream of let-60/ras. Negatively regulates vulva induction probably downstream of let-23. Involved in sex myoblast migration. Negatively regulates fluid homeostasis probably downstream of egl-15. During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles probably downstream of egl-15. Involved in cytoskeleton dynamics and is recruited by mig-13 to the leading edge of Q neuroblasts and their descendants to signal downstream to activate the wsp-1 pathway and direct migration along the anteroposterior body axis during larval development. Involved in let-23-mediated regulation of fertility independently of let-60/Ras. Negatively regulates daf-2-mediated repression of dauer formation. Plays a role in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine. Regulates synaptic levels of nAchR subunit lev-1 in the nerve cord. May play a role in oocyte development upstream of let-60/Ras and the MAP kinase pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27780040}. Note=Targeted to the leading edge of Q neuroblasts by mig-13. {ECO:0000269|PubMed:27780040}.
Interaction partners:
- Son of sevenless homolog
- E3 ubiquitin-protein ligase CBL
- Receptor tyrosine-protein kinase let-23
- SHC-transforming protein homolog 1
- Inactive tyrosine-protein kinase kin-32
- Ras protein let-60
- Tyrosine-protein phosphatase non-receptor type ptp-2
- Myoblast growth factor receptor egl-15
- Phosphoinositide 3-kinase adapter subunit
- IRS-type PTB domain-containing protein
Sequence:
MEAVAEHDFQAGSPDELSFKRGNTLKVLNKDEDPHWYKAELDGNEGFIPSNYIRMTECNWYLGKITRNDAEVLLKKPTVRDGHFLVRQCESSPGEFSISVRFQDSVQHFKVLRDQNGKYYLWAVKFNSLNELVAYHRTASVSRTHTILLSDMNVETKFVQALFDFNPQESGELAFKRGDVITLINKDDPNWWEGQLNNRRGIFPSNYVCPYNSNKSNSNVAPGFNFGN
Protein: FI01450p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B (EC 3.1.1.3)) (Q9VX69)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- RT03039p
- Seminal fluid protein 24F
- Lipase
Sequence:
MGRVPAKMHTLLALLLQLLVASIHAIEWSLPDVINSIGNVGTSIVDPSLLPTPQGLLEGSKQLIAGYPFEFVSNSLNVICSQALASNKIKSKYSPDINKMNFQLQTACEKKNFPLTSPESMWKSPLFDVKKKVVILATGWTTTVNGSDTIEVFSKAYNCRGDVNFVAVDAARFVDTLYTWSAFNTEEIGENIALGLVKLLDLVPVENIHLIGHSLGAHIVGSAGRHLQHLTNQTIPRITGLDPAKPCFNEGEALSGLMRGDAHFVDVIHSNPGVLGKRDPVGDVDFYPGGMSPLAAGCFSVTCAHARSWEYFAETVFPGNERNFMATRCNSISKLRDFRCPGDEVPMGYAVPQNIKGNYFLEVSASAPFGMHASVVRSAHLEHCGLCPESTSTTEVPSTTTTGKPGSWFSG
Protein: Lysine-specific demethylase hairless (EC 1.14.11.65) ([histone H3]-dimethyl-L-lysine(9) demethylase hairless) (O43593)
Organism: Homo sapiens (Human)
Function: Histone demethylase that specifically demethylates both mono- and dimethylated 'Lys-9' of histone H3. May act as a transcription regulator controlling hair biology (via targeting of collagens), neural activity, and cell cycle.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MESTPSFLKGTPTWEKTAPENGIVRQEPGSPPRDGLHHGPLCLGEPAPFWRGVLSTPDSWLPPGFPQGPKDMLPLVEGEGPQNGERKVNWLGSKEGLRWKEAMLTHPLAFCGPACPPRCGPLMPEHSGGHLKSDPVAFRPWHCPFLLETKILERAPFWVPTCLPPYLVSGLPPEHPCDWPLTPHPWVYSGGQPKVPSAFSLGSKGFYYKDPSIPRLAKEPLAAAEPGLFGLNSGGHLQRAGEAERPSLHQRDGEMGAGRQQNPCPLFLGQPDTVPWTSWPACPPGLVHTLGNVWAGPGDGNLGYQLGPPATPRCPSPEPPVTQRGCCSSYPPTKGGGLGPCGKCQEGLEGGASGASEPSEEVNKASGPRACPPSHHTKLKKTWLTRHSEQFECPRGCPEVEERPVARLRALKRAGSPEVQGAMGSPAPKRPPDPFPGTAEQGAGGWQEVRDTSIGNKDVDSGQHDEQKGPQDGQASLQDPGLQDIPCLALPAKLAQCQSCAQAAGEGGGHACHSQQVRRSPLGGELQQEEDTATNSSSEEGPGSGPDSRLSTGLAKHLLSGLGDRLCRLLRREREALAWAQREGQGPAVTEDSPGIPRCCSRCHHGLFNTHWRCPRCSHRLCVACGRVAGTGRAREKAGFQEQSAEECTQEAGHAACSLMLTQFVSSQALAELSTAMHQVWVKFDIRGHCPCQADARVWAPGDAGQQKESTQKTPPTPQPSCNGDTHRTKSIKEETPDSAETPAEDRAGRGPLPCPSLCELLASTAVKLCLGHERIHMAFAPVTPALPSDDRITNILDSIIAQVVERKIQEKALGPGLRAGPGLRKGLGLPLSPVRPRLPPPGALLWLQEPQPCPRRGFHLFQEHWRQGQPVLVSGIQRTLQGNLWGTEALGALGGQVQALSPLGPPQPSSLGSTTFWEGFSWPELRPKSDEGSVLLLHRALGDEDTSRVENLAASLPLPEYCALHGKLNLASYLPPGLALRPLEPQLWAAYGVSPHRGHLGTKNLCVEVADLVSILVHADTPLPAWHRAQKDFLSGLDGEGLWSPGSQVSTVWHVFRAQDAQRIRRFLQMVCPAGAGALEPGAPGSCYLDAGLRRRLREEWGVSCWTLLQAPGEAVLVPAGAPHQVQGLVSTVSVTQHFLSPETSALSAQLCHQGPSLPPDCHLLYAQMDWAVFQAVKVAVGTLQEAK
Protein: YTH domain-containing protein ECT3 (Protein EVOLUTIONARILY CONSERVED C-TERMINAL REGION 3) (F4K1Z0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability (Probable). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (Probable). Required for the correct timing of leaf formation and normal leaf morphology. Required for proper trichome branching and morphology. Functions redundantly with ECT2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29643069}.
Interaction partners:
- FKBP12-interacting protein of 37 kDa
- RNA demethylase ALKBH10B
- N
- E3 ubiquitin-protein ligase HAKAI homolog
- N6-adenosine-methyltransferase non-catalytic subunit MTB
- Protein virilizer homolog
- RNA demethylase ALKBH9B
- Alkylated DNA repair protein ALKBH8 homolog
- Actin-related protein 2/3 complex subunit 2A
- Alkylated DNA repair protein ALKBH6 homolog
Sequence:
MANPDHVSDVLHNLSIDPTTKALAPDSETKLQGAYGGNGNDFLLNDELVEATKIGKPSLLSKDGGVTKDKGSNLKKLGYQSAAYNAKGSYGKGAYAYGYYPPAYQYPRHGYTGSYASGKTNLQYQYLTQQGRSAGNGQSYGGYMDNIYSNYGMCGPYTNGYGYGSYGYDSWKYMPNWYAVNNTYKPRNGYHGYGKENIEGLNEMNRGPRAKGFNSQDGSKVMAVSLKEQRVTETEKLSEDVSLLDPKDYNKIDFPETYTEAKFYVIKSYSEDDIHKSIKYSVWSSTPNGNKKLDASYNEAKQKSDGCPVFLLFSVNTSGQFVGLAEMVGPVDFNKTVEYWQQDKWIGCFPVKWHFVKDIPNSSLRHITLENNENKPVTNSRDTQEVKLEQGIKVIKIFKDHASKTCILDDFEFYENRQKIIQERKSKHLQIKKQTLVANADKGVMSKINLVKPQESTTASEDAAALGVAAEVTKESKVVKETELPVEKNAVATAC
Protein: Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2 (EC 3.1.3.16) (Nuclear LIM interactor-interacting factor 2) (NLI-interacting factor 2) (Protein OS-4) (Small C-terminal domain phosphatase 2) (Small CTD phosphatase 2) (SCP2) (O14595)
Organism: Homo sapiens (Human)
Function: Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells. May contribute to the development of sarcomas.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Matrilin-3
- Secreted frizzled-related protein 3
- Cell division cycle-associated protein 3
- Asporin
- X-box-binding protein 1
- Growth/differentiation factor 5
- General transcription factor IIF subunit 1
- RNA polymerase II subunit A C-terminal domain phosphatase
- RE1-silencing transcription factor
- Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1
Sequence:
MEHGSIITQARREDALVLTKQGLVSKSSPKKPRGRNIFKALFCCFRAQHVGQSSSSTELAAYKEEANTIAKSDLLQCLQYQFYQIPGTCLLPEVTEEDQGRICVVIDLDETLVHSSFKPINNADFIVPIEIEGTTHQVYVLKRPYVDEFLRRMGELFECVLFTASLAKYADPVTDLLDRCGVFRARLFRESCVFHQGCYVKDLSRLGRDLRKTLILDNSPASYIFHPENAVPVQSWFDDMADTELLNLIPIFEELSGAEDVYTSLGQLRAP
Protein: Dynein light chain 2B, cytoplasmic, putative (Q580Q0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cytoplasmic dynein 2 light intermediate chain 1
- Dynein light chain, putative
- Dynein light chain, putative
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Uncharacterized protein
Sequence:
MEFNASTTNERERRIKSVEEVLLRIAKHEGVVGYLVLNPADGRVMRYSGFSSDERKVKKYADKINGFTALAASTIRTIDWKDDLTFLRMGLGLTEILIAPDVDKQYVLIVVQEIRS
Protein: Autophagy and beclin 1 regulator 1 (A0A0G2K5B6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKVVPEKNAVRILWGRERGTRAMGAQRLLQELVEDKTRWMKWEGKRVELPDSPRSTFLLAFSPDRTLLASTHVNHNIYITEVKTGKCVHSLIGHRRTPWCVTFHPTISGLIASGCLDGEVRIWDLHGGSESWFTDSNNAIASLAFHPTAQLLLIATANEIHFWDWSRREPFAVVKTASEMERVRLVRFDPLGHYLLTAIVNPSNQQGDDEPEIPIDGTELSHYRQRALLQSQPVRRTPLLHNFLHMLSSRSSGIQTEPFHPPEQASSTQQDQGLLNRPSAFSTVQSSTAGNTLRNLSLGPTRRSLGGPLSSHPSRYHRELAPGLTGSEWTRTVLTLNSRSEVESMPPPRTSASSVSLLSVLRQQEGGSQASVYTSATEGRGFPSSGLATESDGGNGSSQNNSGNIRHELQCDLRRFFLEYDRLQELDQSLSGETPQTQQAQEMLNNNIESERPGPSHQPTPHSSENNSNLSRGHLNRCRACHNLLTFNNDTLRWERTTPNYSSGEASSSWHVSTTFEGMPPSGNQLPPLERTEGQMPNSSRLELSSSASSQEERTVGVAFNQETGHWERIYTQSSRSGTVSQEALHQDMPEESSEEDSLRRRLLESSLISLSRYDGAGSREHPIYPDPARLSPAAYYAQRMIQYLSRRDSIRQRSMRYQQNRLRSSTSSSSSDNQGPSVEGTDLEFEDFEDNGDRSRHRAPRNARMSAPSLGRFVPRRFLLPEYLPYAGIFHERGQPGLATHSSVNRVLAGAVIGDGQSAVASNIANTTYRLQWWDFTKFDLPEISNASVNVLVQNCKIYNDASCDISADGQLLAAFIPSSQRGFPDEGILAVYSLAPHNLGEMLYTKRFGPNAISVSLSPMGRYVMVGLASRRILLHPSTEHMVAQVFRLQQAHGGETSMRRVFNVLYPMPADQRRHVSINSARWLPEPGLGLAYGTNKGDLVICRPEALNSGIEYYWDQLNETVFTVHSSSRSSERPGTSRATWRTDRDMGLMNAIGLQPRNPTTSVTSQGTQTLALQLQNAETQTEREEEEPGTASSGPGEGEGSEYGGSGEDALSRIQRLMAEGGMTAVVQREQSTTMASMGGFGNNIIVSHRIHRSSQTGTESGAARTSSPQPSTSRGLLSEPGQLAERGLSPRTASWDQPSTSGRELPQPALSSSSPVPIPVPLASNEGPTMHCNVTNNSHLPEGDSSNVGEAAGPSGEPRNR
Protein: Mechanosensitive ion channel MscS domain-containing protein (Q38A71)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKRFFDKLYHTTGFIVDPSQRSVASHVSSLLLQGSIAFSLLGTIGVDTSPLVAAAGVIGATAGFACKDFGANFIASIVLSSQPSLRTGNRISIGTGAGAVKGEVVDWDTRYLYLRTSEGHLLHVPNSMILTSIVTWESSESKQRLGGNEPQGYSPTPPHTVPCNDSASGTK
Protein: Protein HIRA (Q8QFR2)
Organism: Xenopus laevis (African clawed frog)
Function: Required for the periodic repression of histone gene transcription during the cell cycle (By similarity). Required for replication-independent chromatin assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:12049744}.
Interaction partners:
Sequence:
MKLLKPSWVNHNGKPIFSVDIHPDGTKFATGGQGQDSGKVVIWNMPPMLKEEDEKNENIPKMLCQMDNHLACVNCVRWSNNGAYLASGGDDKLIMVWKRSGYIGPSTVFGSSSKLANVEQWRCLSILRSHSGDVMDVAWSPHDAWLASCSVDNTVVIWNALKFPEIISTLRGHSGLVKGLTWDPVGKYIASQADDHSIKVWRTMDWQLETSITKPFDECGGTTHVLRLSWSPDGHYLVSAHAMNNSGPTAQIIERDGWKTNMDFVGHRKAVTVVKFNPKIFKKKQKNGSSTKTSCPYCCCAVGSKDRSLSVWLTCLKRPLVVIHELFDKSIMDISWTLNGLGILVCSMDGSVAYLDFSQDELGDPLSEEEKNNIHQSTYGKSLAITTEPQLPNTVIENPEMLKFQQRQQLQQDGEHMVQAQMEAPIHNMASMMNGESLEDIRKNLLKKQVETRTADGRRRITPLCIAQLDTGDFSTAFFNSIPISGSLPGSMMSSQSNQQLISLDSNTTSSSGALKSNVELVGNNTKPAEETANKESGNVSSSSPVAPTSITAQPKIEPMKALDSRFTERSKATSGTAGVAHLNQTAVDRLKEQNVTKDSKPRVVESSSDSEEKIPASKQLSKRKGEADADLAEKRKKGRPRKESQRLMSVSLTVQSQVASTSEKELTCVTTSSLTLRLPTPTPQKSFTLQLSSDPSMYIEVENEVKTVGGNKLSQLKCHREGKEWEAVLTSRIVAAAGSKEVVCVACEKRMLSIFSGSGRRIFPPIILPSPISTLQCTGSYVMALTAAAALSVWDVQNQNIIIKNESLQPLLSGNDLTVSQTLLTKRGIPVLSLSNGKAYCFSPSLSTWSLVSDKQDSLAQCADYRSCMPSQDAVMCSGPLAIIQGRVSNAGRQAAHLFTMPHLVQKETTMAYLENQVAAALMLQSSQEYRHWLLIYAQYLVNEGFEQRLREVCQDLLGPVHRSSDSQWESRILGLWKRELLKELLPLIGQNLRFQRLFTEYQEQLDILRDK
Protein: Dynein axonemal intermediate chain 4 (WD repeat-containing protein 78) (Q5XPS1)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}. Dynein axonemal particle {ECO:0000256|ARBA:ARBA00024190}.
Interaction partners:
- Dynein-1, subspecies f
- Dynein light chain roadblock
- Uncharacterized protein
- AAA+ ATPase domain-containing protein
- Axonemal inner arm dynein I1/f subunit
- Dynein-1, subspecies f
- Uncharacterized protein
- ODAD1 central coiled coil region domain-containing protein
- Dynein axonemal heavy chain 7
- Uncharacterized protein
Sequence:
MSDQKKALPPKPSQSQVGGYKPRQSTTQGWGGGGTRQTSTGGQPGPRASISGGPRGSFRQSKRQSNRSVNGAENERLQVIIDGVDRTPKPLLSLNPTVLKGGAGDTTTPNSETSDFFMDRISTAAFTKAGWYSNADSGTHTPKSEADYDYEGEKKHRELKGAEDAAAAAMGDDAGPGIESSRGPREEELPPPPPPLLTEKDLERSVYLTLHETETIFIWQATGVTVAMDTEEAKLVEEANRRYANLLHTKHATDKYVDAEAQTLVALKKSREAQSAVLVTRATGVQATAWDISDTFRALDEAAADAEDDPRGGAVLPSISQLAGGVAKYTGGGGGGKAGGMPGDPTSGRGTMAGGASSQSMMVRPSAYHGQSMAFGAQPSYMSGVGGNMSGLSGANLPNGVPVDQQQAAPEVLDPLLSLRGLPDALELMDLAINQNNYLQQLLLYRDIQPLQGVRATVTSAMRGMGGGGDDDATSEAASHAGRDNRPMSAAPSEGGRSHAESVAARSAYGGNRPSMANVAAATGQLSRQPSERSGFSRAMSIKGGRGGDDDARSVRQSHAGAGGGGGGGGGGAGPGYAASVAESNWPEELLQELADLGDDAPRMEHLWDWSCPLTAGKNVACMGWNKANPDLLAVGYGSYAFGSGTPGAGAAGDPLSTTHKSSAAGAAAAAAAAAAARPVTAESAAAGEVGAAGAGATTTSGQQTTGHEPRGLVAFWSLKNLQHPLWWFEVKAAVTALDFSTYSPNLLALGMYDGTVAIYDIKSRQGTPSMESDVHSGKHSDPVWKVKWLDHGPERDEPLVSISTDGRVTQWSIAKGLEFSDLMKLKRMARRGAGGPPAAAKDGSKAAAVPEQQDAFISRLTSGMAFDFSGRDERIYVAATEDGWLHKCSTSYSEQYLESYRGHMGPVYQVQFSPYKKDMFISSSGDWTIRMWQEGRDTPLLTFQASTNEINDVQWCPTNSTVFGSVTATGRLEIWDFALSTVKPVMHQKTPAKLSCMLFAPNYPVVVCGGEDGTVKAYRLYNVSHEYDTLEEQLGRLDAVIKANVMKKETGQAGQA
Protein: DnaJ-related protein SCJ1 (J protein SCJ1) (P25303)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulates protein folding in the endoplasmic reticulum lumen. Probably acts as a J-protein for the Hsp70-type chaperone KAR2 by stimulating its ATP-dependent reaction cycle and initiating folding reactions. Also involved in the endoplasmic reticulum-associated degradation (ERAD) process. Cooperates with KAR2 and another J-protein JEM1 to facilitate the export of ERAD substrates to the cytoplasm by maintaining them in a translocation-competent state and preventing their aggregation in the endoplasmic reticulum lumen.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:7744969}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- DnaJ-like chaperone JEM1
- Heat shock protein 70 homolog LHS1
- ER-localized J domain-containing protein 5
- Protein disulfide-isomerase
- Glucosidase 2 subunit alpha
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Zuotin
- Auxilin-like clathrin uncoating factor SWA2
- Pre-mRNA-splicing factor CWC23
Sequence:
MIPKLYIHLILSLLLLPLILAQDYYAILEIDKDATEKEIKSAYRQLSKKYHPDKNAGSEEAHQKFIEVGEAYDVLSDPEKKKIYDQFGADAVKNGGGGGGPGGPGAGGFHDPFDIFERMFQGGHGGPGGGFGQRQRQRGPMIKVQEKLSLKQFYSGSSIEFTLNLNDECDACHGSGSADGKLAQCPDCQGRGVIIQVLRMGIMTQQIQQMCGRCGGTGQIIKNECKTCHGKKVTKKNKFFHVDVPPGAPRNYMDTRVGEAEKGPDFDAGDLVIEFKEKDTENMGYRRRGDNLYRTEVLSAAEALYGGWQRTIEFLDENKPVKLSRPAHVVVSNGEVEVVKGFGMPKGSKGYGDLYIDYVVVMPKTFKSGQNMLKDEL
Protein: Methenyltetrahydrofolate synthase domain-containing protein (Q2M296)
Organism: Homo sapiens (Human)
Interaction partners:
- Formimidoyltransferase-cyclodeaminase
- Nucleolar protein 56
- Small integral membrane protein 12
- NHP2-like protein 1
- U3 small nucleolar RNA-associated protein 15 homolog
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
Sequence:
MEPRAVGVSKQDIREQIWGYMESQNLADFPRPVHHRIPNFKGSYLACQNIKDLDVFARTQEVKVDPDKPLEGVRLLVLQSKKTLLVPTPRLRTGLFNKITPPPGATKDILRKCATSQGVRNYSVPIGLDSRVLVDLVVVGSVAVSEKGWRIGKGEGYADLEYAMMVSMGAVSKETPVVTIVHDCQVVDIPEELVEEHDITVDYILTPTRVIATGCKRPKPMGITWFKISLEMMEKIPILRSLRAREQQAGKDVTLQGEHQHLPEPGCQQTVPLSVGRRPPDTPGPETNSMEAAPGSPPGEGAPLAADVYVGNLPGDARVSDLKRALRELGSVPLRLTWQGPRRRAFLHYPDSAAAQQAVSCLQGLRLGTDTLRVALARQQRDK