wanglab/gogpt-training-data huggingface dataset:
Protein: Twinkle mtDNA helicase (EC 5.6.2.3) (Progressive external ophthalmoplegia 1 protein homolog) (T7 gp4-like protein with intramitochondrial nucleoid localization) (T7-like mitochondrial DNA helicase) (Twinkle protein, mitochondrial) (Q8CIW5)
Organism: Mus musculus (Mouse)
Function: Mitochondrial helicase involved in mtDNA replication and repair (By similarity). Might have a role in mtDNA repair (By similarity). Has DNA strand separation activity needed to form a processive replication fork for leading strand synthesis which is catalyzed by the formation of a replisome complex with POLG and mtSDB (By similarity). Preferentially unwinds DNA substrates with pre-existing 5'-and 3'- single-stranded tails but is also active on a 5'- flap substrate (By similarity). Can dissociate the invading strand of immobile or mobile D-loop DNA structures irrespective of the single strand polarity of the third strand (By similarity). In addition to its DNA strand separation activity, also has DNA strand annealing, DNA strand-exchange and DNA branch migration activities (By similarity).
Subcellular location: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q96RR1}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96RR1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96RR1}. Note=Colocalizes with mtDNA in mitochondrial nucleoids, a nucleoproteins complex consisting of a number of copies of proteins associated with mtDNA, probably involved in mtDNA maintenance and expression (By similarity). Associates with phospholipid membranes via electrostatic binding (By similarity). Preferentially associates with membranes enriched with cardiolipin, a lipid abundant in the mitochondrial inner membrane (By similarity). ATPase and helicase activity is enhanced by binding to lipid membranes (By similarity). {ECO:0000250|UniProtKB:Q96RR1, ECO:0000250|UniProtKB:Q9VL76}.
Interaction partners:
- DNA polymerase subunit gamma-1
- Single-stranded DNA-binding protein, mitochondrial
- DNA polymerase subunit gamma-2
- Transcription factor A, mitochondrial
- Mitochondrial genome maintenance exonuclease 1
- DNA-directed RNA polymerase, mitochondrial
- Ribonuclease H1
- Deoxyguanosine kinase, mitochondrial
- Dimethyladenosine transferase 2, mitochondrial
- DNA replication ATP-dependent helicase/nuclease DNA2
Sequence:
MWLLLRRAYPLRILLPLRGEWVGRRGLPRSLAPGPPRRRYRKEALPALEMPVSPVTTTEIRQYLRAHGIPFQDGHSCLRAPSPFVVSSDIKNEKKDAPTSFCLFIDKTTGHFLCMTSLAEGSWEDLQASVEGRGDGAKEGVLLREGPEAEVREEVLRIWNRAIPLWELPDPEEAQLARVMFGLTKVTDDTLRRFSVRYLRSARSLVFPWFTPGSSGLRGLKLLGAEGQENGVQYVETTIPRPGVYHNLFGLPLISRRDTEVVVTSRELDSLALSQSTGLPTLSLPRGTVCLPPALLPYLEQFRRIVFWLGDDLRSWEAAKLFARKLNPKRCSLVRPGNQQPRPLEALNQGLSLPRILRTALPAWHKSIVSFRQLREEVLGELSNVEQAAGVRWSRFPDLNRLLKGHRKGELTVFTGPTGSGKTTFISEYALDLCTQGVNTLWGSFEISNVRLARVMLTQFAVTRLEEQLDKYEEWADRFEDLPLYFMTFHGQQSIRSVIDTMQHAVYVYDVCHVVIDNLQFMMGHEQLSSDRIAAQDYIVGAFRKFATDNSCHVTLVIHPRKEDDDKELQTASIFGSAKASQEADNVLILQDRKLVTGPGKRYLQVSKNRFDGDVGVFPLEFNKNSLTFSIPPKSKARLKKIKDDNGLVAKKSSSGKKGAAHQNPEICLGQDPSPAQPDTSKSSG
Protein: Mago-binding protein, putative (Q8I5V8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- RNA-binding protein 8A, putative
- Mago nashi protein homologue, putative
Sequence:
MQKKPSTGFKLENTYRALFDNDDNNEKSYIREVVTPLGDVYIINEKTQEKFIKGTQRSDGTFRKNIRVKTDYMPQEENCAYQVKGKLLEEQNRLLTKNTSPNVNINVNTNHNTFSHVNINRHVNLNNQQKKIPGWNPINDDQDEKLNSSKKKKKKKKKKPNKEIAEM
Protein: Cation/H(+) antiporter 20 (Protein CATION/H+ EXCHANGER 20) (AtCHX20) (Q9M353)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Operates as a K(+)/H(+) antiporter that maintains K(+) homeostasis in guard cells and could regulate pH. Plays a critical role in osmoregulation through the control of stomates opening.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:17337534}; Multi-pass membrane protein {ECO:0000269|PubMed:17337534}.
Interaction partners:
- F-actin-capping protein subunit alpha
- GDSL esterase/lipase At1g33811
- GDSL esterase/lipase At5g18430
- Sodium/hydrogen exchanger 4
Sequence:
MPFNITSVKTSSNGVWQGDNPLNFAFPLLIVQTALIIAVSRFLAVLFKPLRQPKVIAEIVGGILLGPSALGRNMAYMDRIFPKWSMPILESVASIGLLFFLFLVGLELDLSSIRRSGKRAFGIAVAGITLPFIAGVGVAFVIRNTLYTAADKPGYAEFLVFMGVALSITAFPVLARILAELKLLTTQIGETAMAAAAFNDVAAWILLALAVALAGNGGEGGGEKKSPLVSLWVLLSGAGFVVFMLVVIRPGMKWVAKRGSPENDVVRESYVCLTLAGVMVSGFATDLIGIHSIFGAFVFGLTIPKDGEFGQRLIERIEDFVSGLLLPLYFATSGLKTDVAKIRGAESWGMLGLVVVTACAGKIVGTFVVAVMVKVPAREALTLGFLMNTKGLVELIVLNIGKEKKVLNDETFAILVLMALFTTFITTPTVMAIYKPARGTHRKLKDLSASQDSTKEELRILACLHGPANVSSLISLVESIRTTKILRLKLFVMHLMELTERSSSIIMVQRARKNGLPFVHRYRHGERHSNVIGGFEAYRQLGRVAVRPITAVSPLPTMHEDICHMADTKRVTMIILPFHKRWNADHGHSHHHQDGGGDGNVPENVGHGWRLVNQRVLKNAPCSVAVLVDRGLGSIEAQTLSLDGSNVVERVCVIFFGGPDDRESIELGGRMAEHPAVKVTVIRFLVRETLRSTAVTLRPAPSKGKEKNYAFLTTNVDPEKEKELDEGALEDFKSKWKEMVEYKEKEPNNIIEEILSIGQSKDFDLIVVGRGRIPSAEVAALAERQAEHPELGPIGDVLASSINHIIPSILVVQQHNKAHVEDITVSKIVSESSLSINGDTNV
Protein: Possible osmoprotectant (Glycine betaine/carnitine/choline/L-proline) transport ATP-binding protein ABC transporter ProV (O69724)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible osmoprotectant binding lipoprotein ProX
- Possible osmoprotectant transport integral membrane protein ABC transporter ProZ
- Possible osmoprotectant transport integral membrane protein ABC transporter ProW
- Probable lipoprotein LpqZ
- Conserved protein
- Uncharacterized membrane protein Rv3760
Sequence:
MICFDDVSKVYAHGATAVDRLTLEVPNGMLTVFVGPSGCGKTTALRMINRMVDPTSGTITVDGTDVSTVNAVKLRLGIGYVIQNAGLMPHQRVIDNVATVPVLKGQPRRAARKAGYEVLERVGLDPKVATRYPAQLSGGEQQRVGVARALAADPPILLMDEPFSAVDPVVRHELQNEILRLQAELHKTIVFVTHDIDEALKLADLVAVFAPGGALAQYDETARLLSSPANDFVSKFIGLGRGYRWLQLFDAAGLPVRDIEQVSVNGLSDARDRQVRDGWVLVVDGAGAPLGWIDADGRRRHRGGAALSDAMTVGGSVFRPNGNLSQALDAALSSPSGVGVAVDGGGKVIGGILAADVLAEFQKGKKAGGGAKPCTT
Protein: FI03643p (B7FNJ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
QNLWHFVWRLIIGYLDFNCNKNRDNTMLSRKRRASSISSRQDEDPLQLDDSTPEQSPVQQTTTQSARKKRRLDPTELCQQLYDSIRNIKKEDGSMLCDTFIRVPKRRQEPSYYDVVVNPIDLLKVQQKLKTDSYDDLDDLMADLELLIGNAKAFYIPGSSEHQDAVSLWQHIHSQRQRIMEANGLAEEEPRARRMSRQVRRMTSSTEPGGDGATDDEYNQYEELFASVMTATDPVGDRLMHRMFQLLPSKKIYPDYYDVIEHPIDLRLIATKIQMNAYSSLAEMERDLLQMTKNACLFNEPGSQIYKDAKSLKRIFTQRRIELEMGKGKLAKRVKSLSSAAIAALKEEVDSSDDEETSKKGEGPMWALFDHLYNAPGTSEHPGVTGPPLGNSLWKLPVRRFHPEYFELIKRPISMSQIHTKLKKGDYANISDLTADLYLMLDNAKKAFPTSHRTHKDALKMLKLMNAKLVEESLEEGSDLDDEDAEEMDTEVFTVSTQPEKRKPGRPRINSNSNSNASHTPNNSNSPKSNRIAINAAIKKKILSIQKYLVDYSLGNRRPIEMFMEKPPRKIYPDYYDIIQNPIDMNTIEHNIRTDRYAAVEDVVSDYRLMFSNCRQYNEEGSNIYEDANILERALNEKLKEFPGLTEGKKSQQKYSKVGRKLKTAVITERLWQFYETVKEYQEPKGKRQLSLIFTKLPSKSEYPDYYDIIREPIDMDRIAQKLKQGAYDTLDDLAADFLLMLENACKYNEPDSQIYKDALVLQQLTLQLKQQLRTERDSLPDVPLAVQELFLTLFTTIYNHQDEEGRCYSDSLAELPEYDEIGEGPKVRGISLDLVKRRLDKGAYKRLDVYQEDIFACLERARKLSRTDSDIFQDSIELQTYFIRKRDELCKDTLSSSALNFSLERLMADVELCRQQKMQQEEQDQEQDKEKDEFNAAKGESMTINQQVFSPGDYVYVQMPENKIPSICCIERLWTSPTNEKLMQASIFVRPHETYHVTTRKFLEKEVFKSSLSQTISMDKVQGMCYVMNIKDYIKMRPENLPEKDVYVCESRYNIQGRWFKKLKSWPPVREGSSVKFVPREQPLELKRVMSVFKERLEKHKGELEELKLQETLVEKEKPNVSCDPPPNAEVGSTYYQQYNTICSGAIKTGDFVYVATQTGKQSVAQVQQIWEQNGKSYFKGPWLLPPSETTPGLGKQFYRQELLLSTVEEVSPVVGIVGRCAVLEYSEFISSRPTEISESDVYICESVYDELKKALRKLVTGNMRKFQHSPSVTEDEIFYFKTPIKPSKDFKNELNELGMLEDSMDGDTPSLSSDIAAMSSPAPSVNSTPLTSKVKAAKSAKKCLTGYILYSSEVRKSICQSNPDATFGDISRMVGTEWKNLPSSVKQSWEDRASRQNEETAALRRELDDVQNSASPSSQVSQDVFGQVLTFECQWDKCDFQFEELSDCTEHCMSDSTGHIQRHPQAGVETEYVCLWRNCPRVKKSVQAFPNVLRLIKHVREVHLSKCGKTISAADRSKNFVPRRQKHAQLATTVPIPPSLAQSPRAPSNLEAVQLQQQQHPQQNMHQLQQQQTIVLGPPPEPLFVTVPPRTTRVIHSEAYIKYIESLQTGSHLNVVTCNNNWRRALTHITPAQVVAKTALPEKWIGPNLRDQGNVVQALCHLRNFMVDDILQIRRSCN
Protein: Uncharacterized protein (Q35962)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MTRDRMRQSIKGRALCRAFSSRSAGGVIFKVVLKSLQERKKRISSEISSTIYFYMLCIPYLIFFLKISILVFLVFYRIVLPIVQMFSLLTCCSFLITLPPEVQDPQALAHLEGLNFYLSLYEQDPEWVAFIQQELNHNTPLEDIPGRLRLFLMEERTSNVRMDLIQEFLALYARNGAVLPVEPYLLEGALRSYLDSIRATDDFSILQAAYQDLRDHEEGSFFFRDVVSHNRDFLEAQSAKRTWIEVERNSLYSKIERAQARLERTEFQHTLLIFQLEDRKRGGE
Protein: 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial (AKB ligase) (EC 2.3.1.29) (Aminoacetone synthase) (Glycine acetyltransferase) (O88986)
Organism: Mus musculus (Mouse)
Function: Pyridoxal phosphate (PLP) dependent enzyme, which catalyzes the cleavage of 2-amino-3-oxobutanoate to glycine and acetyl-CoA. Catalyzes the second reaction step on the main metabolic degradation pathway for L-threonine.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q0P5L8}. Nucleus {ECO:0000250|UniProtKB:O75600}. Note=Translocates to the nucleus upon cold and osmotic stress. {ECO:0000250|UniProtKB:O75600}.
Interaction partners:
- L-threonine 3-dehydrogenase, mitochondrial
- Glycine dehydrogenase
- Serine hydroxymethyltransferase, mitochondrial
- L-threonine aldolase
- Sarcosine dehydrogenase, mitochondrial
- Glycine N-methyltransferase
- Serine hydroxymethyltransferase, cytosolic
- Peroxisomal sarcosine oxidase
- Alanine--glyoxylate aminotransferase
- D-amino-acid oxidase
Sequence:
MWASFMWHGALSPGRRAHSALAQLRCILDSELEGIRGAGTWKSERVITSRQGPSIRVDGISGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEAQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICPVMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
Protein: SVF1-like protein YDR222W (Q04925)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Note=Punctate pattern.
Interaction partners:
- Uncharacterized vacuolar protein YLR297W
Sequence:
MLESSSDKIKFAPIKEVDYKKPVSKSKNYTLINDIQPLEWYCHNDSETGYQHTISNKTDGGRGLFRVMKKSMETRVETQTLYFTDLHTGLCGFVQLLYSTVMGGIYKGFQLNFKVFGSESNNTDYDVWESFKLDDIAEFQPLKFVSRNVIFEFLSNKNEKLGSIGQLSIKCDLPTCNNTIQNLKIDLLVDLFQGFKMNPNGCNYYFDKQISMSDEFVSSDKMIRHVFVPRGKCNGNISYDKKLNSGDFQNKNISLTDVPVVYLDAVQGLLPNKAASKWNFLCFQSENYSVLAIEFTTPRDHDNVTVTVWSITEKNKLISIGSSVQSPKRHVRFRATSTDKESGWVYPTSIKFPGGFSEHDLRLVNRYDVLGELPSMVRSLAQKIVSIKPFIYQYCQPSKYKHEKGISIVESTFIS
Protein: Unconventional myosin-Va (Dilute myosin heavy chain, non-muscle) (Q99104)
Organism: Mus musculus (Mouse)
Function: Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.
Interaction partners:
- Melanophilin
- Ras-related protein Rab-27A
- Calmodulin-1
- Rab effector MyRIP
- RILP-like protein 2
- Ras-related protein Rab-11A
- Protein spire homolog 2
- Glutamate receptor 1
- Ras-related protein Rab-3A
- Ras-related protein Rab-8A
Sequence:
MAASELYTKFARVWIPDPEEVWKSAELLKDYKPGDKVLLLHLEEGKDLEYRLDPKTGELPHLRNPDILVGENDLTALSYLHEPAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTRVPVKPTKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLGDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKRYLCMQRAAITVQRYVRGYQARCYAKFLRRTKAATTIQKYWRMYVVRRRYKIRRAATIVIQSYLRGYLTRNRYRKILREYKAVIIQKRVRGWLARTHYKRTMKAIVYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSETEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQETDQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMERKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMLNVPKPGHKRTDSTHSSNESEYTFSSEFAETEDIAPRTEEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEEERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEELYADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRPVNIPRKEKDFQGMLEYKREDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFIRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFIARV
Protein: O-GlcNAcase NagJ (EC 3.2.1.169) (Beta-N-acetylglucosaminidase) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (GH84C) (Hexosaminidase B) (N-acetyl-beta-D-glucosaminidase) (Q0TR53)
Organism: Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
Function: Binds carbohydrates. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can bind and deglycosylate O-glycosylated peptides from mammals.
Interaction partners:
- Hyaluronoglucosaminidase
- exo-alpha-sialidase
- PTS system, N-acetylglucosamine-specific IIBC component
- PTS system, N-acetylglucosamine-specific IIBC component
Sequence:
MKRKMLKRLLTSAFACMFIANGLITTTVRAVGPKTGEENQVLVPNLNPTPENLEVVGDGFKITSSINLVGEEEADENAVNALREFLTANNIEINSENDPNSTTLIIGEVDDDIPELDEALNGTTAENLKEEGYALVSNDGKIAIEGKDGDGTFYGVQTFKQLVKESNIPEVNITDYPTVSARGIVEGFYGTPWTHQDRLDQIKFYGENKLNTYIYAPKDDPYHREKWREPYPESEMQRMQELINASAENKVDFVFGISPGIDIRFDGDAGEEDFNHLITKAESLYDMGVRSFAIYWDDIQDKSAAKHAQVLNRFNEEFVKAKGDVKPLITVPTEYDTGAMVSNGQPRAYTRIFAETVDPSIEVMWTGPGVVTNEIPLSDAQLISGIYNRNMAVWWNYPVTDYFKGKLALGPMHGLDKGLNQYVDFFTVNPMEHAELSKISIHTAADYSWNMDNYDYDKAWNRAIDMLYGDLAEDMKVFANHSTRMDNKTWAKSGREDAPELRAKMDELWNKLSSKEDASALIEELYGEFARMEEACNNLKANLPEVALEECSRQLDELITLAQGDKASLDMIVAQLNEDTEAYESAKEIAQNKLNTALSSFAVISEKVAQSFIQEALSFDLTLINPRTVKITASSEETSGENAPASFASDGDMNTFWHSKWSSPAHEGPHHLTLELDNVYEINKVKYAPRQDSKNGRITGYKVSVSLDGENFTEVKTGTLEDNAAIKFIEFDSVDAKYVRLDVTDSVSDQANGRGKFATAAEVNVHGKLKENAEVTGSVSLEALEEVQVGENLEVGVGIDELVNAEAFAYDFTLNYDENAFEYVEAISDDGVFVNAKKIEDGKVRVLVSSLTGEPLPAKEVLAKVVLRAEAKAEGSNLSVTNSSVGDGEGLVHEIAGTEKTVNIIEGTSPEIVVNPVRDFKASEINKKNVTVTWTEPETTEGLEGYILYKDGKKVAEIGKDETSYTFKKLNRHTIYNFKIAAKYSNGEVSSKESLTLRTAR
Protein: C2H2-type domain-containing protein (O18068)
Organism: Caenorhabditis elegans
Interaction partners:
- Sun domain-containing protein 1
- Zygote defective protein 12
- HORMA domain-containing protein
- HORMA domain-containing protein
- DNA repair protein RAD51 homolog
- Serine/threonine-protein kinase chk-2
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Meiotic recombination protein spo-11
- HORMA domain-containing protein
- Cyclin N-terminal domain-containing protein
Sequence:
MNGNSLNSFVNIRIYGKTLENLKHYGLIEYLNEFAGGSSFVSLTESTSISSINTATVDTPRFSTPIVPNVGLYQKFTLNLSEKISEIGPNDENEDLKESYDQEPEEELNSSHESNNSVEKVMDMIIEDVVSNHTTNIADGDDINSPIVSSGQSEFLQDGVDNDGNIDDYEEYQSLPPNDDVIMNETELMDVDRTTVMTPLRSPTFFDYHNESGDEDQLNENEMKSPDSKNDEINKDEIHNIQCHFPNCNRAIAWKRKYGKLRLIDHALVHCDKNFLKCKKCKHTCHTIRQMRYHYRIFHSTSKMEGFGVSGLPTKNKGFQKIMNACFADQLVEMNKRKNPPKSQNGSRRSRVKSKSKRSGI
Protein: Uncharacterized protein CPT2R1.03 (P0CS85)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP-dependent DNA helicase tlh2
- Histidine biosynthesis bifunctional protein his7
Sequence:
MSIEFDDSSRHNMNMTQLMQLGAFDRRSGDDFMVQDFKNGIRDCSGIPVNNRNLAFKAYDAVKQKYDSSIKVFNIQDITIKGATWQHHNCQSTGKWYSQLYDYQNTFIGKQEYNILFDCYSYLKYNLNG
Protein: Sterile alpha motif domain-containing protein 7 (SAM domain-containing protein 7) (Q7Z3H4)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of gene expression in the retina. It functions as a negative regulator of CRX-controlled genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:38272031}. Cytoplasm {ECO:0000250|UniProtKB:Q8C8Y5}. Note=Co-localizes with PHC2 and RNF2 in nuclear polycomb bodies. {ECO:0000250|UniProtKB:Q8C8Y5}.
Interaction partners:
Sequence:
MAVNPLLTPTGQQTIPLIPSPFGPPTVDRDVLPSTVAPTDPRQFCVPSQFGSSVLPNTNMANVLSSRIYPGWGILPPESIKAVARRNEMIQRHHTARTEMEMYAIYQQRRMEKINPKGLAGLGIPFLYGSSVPAAPAAYHGRSMLPAGDLHFHRSTLRNLQGNPMLAATAPHFEESWGQRCRRLRKNTGNQKALDSDAESSKSQAEEKILGQTHAVPYEEDHYAKDPDIEAPSNQKSSETNEKPTTALANTCGELEPTHRKPWGSHTTTLKAKAWDDGKEEASEQIFATCDEKNGVCPPVPRPSLPGTHALVTIGGNLSLDEDIQKWTVDDVHSFIRSLPGCSDYAQVFKDHAIDGETLPLLTEEHLRGTMGLKLGPALKIQSQVSQHVGSMFYKKTLSFPIRQAFDQPADTSPLLDPNSWSDTMNIFCPQDTIIPKGIERGSMRN
Protein: NHL repeat-containing protein 3 (Q5JS37)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MARFWVCVAGAGFFLAFLVLHSRFCGSPVLRNFTFAVSWRTEKILYRLDVGWPKHPEYFTGTTFCVAVDSLNGLVYIGQRGDNIPKILVFTEDGYFLRAWNYTVDTPHGIFAASTLYEQSVWITDVGSGFFGHTVKKYSSFGDLVQVLGTPGKKGTSLNPLQFDNPAELYVEDTGDIYIVDGDGGLNNRLIKLSQDFMILWLHGENGTGPAKFNIPHSVTLDSAGRVWVADRGNKRIQVFDKDTGEWLGAWNNCFTEEGPSSVRFTPDGKYLIVAQLNLSRLSVVAAPPVGSIGECSVISTIQLADQVLPHLLEVDRKTGAVYVAEIGAKQVQKYVPLNSYVPSFGS
Protein: F-box domain-containing protein (Q583X7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDSQARAGKSILHKGIPRYRQAAHVRRGDEEALGHVAGSGAKVPLRTHTITSGRLRIKTYQDTQSMREAFERLKQICGAFSLDEDEEISCMIPRVCDSGNPAPAQLNRMPGHLIVHCFSFCDLSSLGQLSRVSRRLAAFANAHHIWVEHAKRLNKPVRGPETARADLRFEVCGRWDAEIQEHEQAYEDLQRRLQERAAAERAAVLDVEGVLNENRRNVRGGDILRSRGSNNSNIYSVADVQALQAKVEQLEAVKLELLRSVRDLGDILAQQQAQIQDMQNRLAVRVTAEGDVVTTTSSCNTVDGTATHVSPPELTLHELTNFERRMCRLVLGTIPDLSVVLRRGVDDFGTMEMLVQHSGGELESGIRKRWQAFKSFFPPLSNDYSKARFYLLSGESAQSERRNESITRCSAIVRRLMKMSDSEITDIVMQSGSS
Protein: Pathogenesis associated protein Cap20, putative (AFU_orthologue AFUA_1G06350) (C8V4B0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MPHFENGAMGENAVNGERAQSQFLEHLTSYPVVSDSISFYKGNKYGAKSLEFADQGYGFAKPYLSYLSKPYGYVAPYVTRADSLGDKGLQKVDATFPIIKEDTKTLKNTIYDTAYFPLRLFGDAKSHVFSTYGDEYKKCGGDGVVASGKAIITTSLVLSQESLAFISSLLQKKKAQVKDLVNEQAQE
Protein: Pyruvate kinase 2 (PK 2) (EC 2.7.1.40) (Q6FV12)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Enolase 2
- Enolase 1
- Malic enzyme
- Glucose-6-phosphate isomerase
- Pyruvate dehydrogenase E1 component subunit beta
- L-lactate dehydrogenase
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Pyruvate carboxylase
- Pyruvate decarboxylase
Sequence:
MDSRLHRLINLEVTPGKDVRKTAIIGTIGPKTNNVDTLVALRKAGLNIVRMNFSHGSYEYHQSVIDNARKSEQVYPGRPLAIALDTKGPEIRTGTNVDDVDYPIPPNHEMIFTTDDKYAKACDDKIMYVDYKNITKVIQPGKVIYVDDGVLSFEVLEVVDDKTLKVKSLNAGKISSHKGVNLPGTDVDLPALSEKDKEDLRFGVKNGVHMIFASFIRTAQDVLTIREVLGEEGKDIKVIVKIENQQGVNNFDEILEVAHGVMVARGDLGIEIPAPQVLAVQKKLIAKCNLAGKPVICATQMLESMTFNPRPTRAEVSDVGNAILDGADCVMLSGETAKGNYPINAVTTMAETAIIAERAIAYMPLYDDLRNCTPKPTSTTETVAASAVAAVQEQGAKLILVLSTSGNTARLVSKYRPQCPIVLVTRNPRTARFSHLFRGVFPFVYEKEPLDDWSEDTHARLRFGVDMAKEYGFVKNGDAVISIQGFKGGVGHSNTMRVSIVGGEKEDI
Protein: Rrp4, isoform A (Rrp4, isoform B) (Q9W1M9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ribosomal RNA-processing protein 42
- FI06805p
- Exosome complex component 10 homolog
- FI07225p
- Nuclear nucleic acid-binding protein C1D
- FI01414p
- Csl4
- Exosome complex component RRP45
- Exosome complex exonuclease RRP44
- RNA helicase
Sequence:
MSTNAAIDLALDRVDWRDLAAQTEEQPRVYTPGEVLMPEAGFMRGHGTFVEDENIKSSVAGVIQKVNKLISVRPLKSRYVGEIGDVVVARVSEVQQKRWRVDTNSRLDSILLLSSVNLPGGELRRRSAEDEQMMRRYLDEGDLISAEVQNIFEEGSLSLYTRSLKYGKLSQGILVKVFPALVKRRKMHFHNLPCGASVILGNNGYIWISPTKGQEEEGGEGGFAQNLNEHVPRADREVIARLRNSILALAKCKLMIYDTSIQYAYEESLRYEAHELLQQNAIYDIGQQTQARLRDADE
Protein: Glycine N-methyltransferase (EC 2.1.1.20) (Q14749)
Organism: Homo sapiens (Human)
Function: Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy), a reaction regulated by the binding of 5-methyltetrahydrofolate. Plays an important role in the regulation of methyl group metabolism by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P13255}.
Interaction partners:
- Sarcosine dehydrogenase, mitochondrial
- Dimethylglycine dehydrogenase, mitochondrial
- Peroxisomal sarcosine oxidase
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Alanine--glyoxylate aminotransferase
- Glycine amidinotransferase, mitochondrial
- Glycine dehydrogenase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- D-amino-acid oxidase
Sequence:
MVDSVYRTRSLGVAAEGLPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCQRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRHEPAFDKWVIEEANWMTLDKDVPQSAEGGFDAVICLGNSFAHLPDCKGDQSEHRLALKNIASMVRAGGLLVIDHRNYDHILSTGCAPPGKNIYYKSDLTKDVTTSVLIVNNKAHMVTLDYTVQVPGAGQDGSPGLSKFRLSYYPHCLASFTELLQAAFGGKCQHSVLGDFKPYKPGQTYIPCYFIHVLKRTD
Protein: Kelch-like protein 20 (Kelch-like ECT2-interacting protein) (Kelch-like protein X) (Q9Y2M5)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis. The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination. Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking. Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11. In case of tumor, the BCR(KLHL20) E3 ubiquitin ligase complex is involved in tumor hypoxia: following hypoxia, the BCR(KLHL20)complex mediates ubiquitination and degradation of PML, potentiating HIF-1 signaling and cancer progression.
Subcellular location: Cytoplasm, perinuclear region. Nucleus. Golgi apparatus, trans-Golgi network. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes in the perinuclear region in normal conditions. Following IFN-alpha or IFN-gamma treatment, it is relocalized and sequestrated to the PML nuclear bodies, preventing DAPK1 ubiquitination (PubMed:20389280). {ECO:0000269|PubMed:20389280}.
Interaction partners:
- Cullin-3
- E3 ubiquitin-protein ligase RBX1
- Death-associated protein kinase 1
- Kelch-like protein 22
- Kelch-like protein 42
- Speckle-type POZ protein
- Kelch-like protein 9
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2
- Kelch repeat and BTB domain-containing protein 8
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
Sequence:
MEGKPMRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEFLKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVKYSIQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVLFAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTSTCRTSVGVAVLGGFLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERYNPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVGGFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW