wanglab/gogpt-training-data huggingface dataset:
Protein: C2H2-type zinc finger family protein (Putative zinc finger transcription factor) (Q84K31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- C2H2 and C2HC zinc fingers superfamily protein
- C2H2-type zinc finger family protein
- HAT family dimerization domain-containing protein
- Ac-like transposase
- Mitochondrial import receptor subunit TOM9-2
Sequence:
MEAFEEATKEQSLILKGKRTKRQRPQSPIPFSISPPIVSTPENNMEEEYTDLDSKDNALGNDEGNHKKDGVITSSSSSASWSSQNNHTLKAAEDEEDQDIANCLILLAQGHSLPHNNHHLPNSNNNNTYRFTSRRFLETSSSNSGGKAGYYVYQCKTCDRTFPSFQALGGHRASHKKPKAASFYSNLDLKKNTYANDAVSLVHTTTTVFKNNNSRSLVVYGKASKNKVHECGICGAEFTSGQALGGHMRRHRGAVVVPAVIAPTVTVATAAANTELSLSSMSFDQISDGHQDHLAMPAKKKARTVVSLDLDLNLPAPEDENRVNGFSFASKQNHEQEHQQKKQREEPKSLVLSAPTLVDCHY
Protein: Nickel ABC transporter, permease protein, putative (Q48JD2)
Organism: Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6))
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}.
Interaction partners:
Sequence:
MTIFDNRLARLTRLVDSSQSLSGKTAPAAQWRRRSNLSRAVEAAKPLLRRPGFLLAVAMVAFALLAALAPNLLSSYAPYATSPSDKLTAPNAAHWFGTDELGRDLYTRVVHGSSLSVQAALLAVGIAMAGGLSLGVISGFAGGRIDAVIMRLIDVLLALPGLLLALAIVTAIGFGTIPVAIAVGVGIIPGFARTTRAEVLRVKTLPYVEAARLGGASWTRTLLRHILPNAWGPVAVLATLDFGAAILATAGLSFLGFGAEPPAAEWGTLIANGRHFLMTAPWVSLLPGLFVVGVVFSFNHIARTLEETQR
Protein: Protein yippee-like At4g27740 (Q2V3E2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Heavy metal-associated isoprenylated plant protein 2
- Heavy metal-associated isoprenylated plant protein 25
- Zinc transporter 3
- Probable zinc transporter 10
- GDSL esterase/lipase At2g19010
- At2g19160
- DUF630 family protein
- GDSL esterase/lipase At2g19060
- Protein RALF-like 13
- Zinc transporter 9
Sequence:
MAANKTLPTYFCRNCENPLALGEDLISKKFVGASGPAFMFSHAMNVVVGPKIGRKLITGSYVVADVMCSKCGETLGWKYVETFDLKQRYKEGMFVIEKLKLTKRY
Protein: carbonyl reductase (NADPH) (EC 1.1.1.184) (Q9PT36)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- dihydrofolate reductase
- 6-pyruvoyl tetrahydrobiopterin synthase
- L-xylulose reductase
- Prostaglandin E synthase 3
- Prostaglandin E synthase 3
- Prostaglandin E synthase 3
- Prostaglandin E synthase 3
- Cytochrome P450 1A
- Prostaglandin E synthase
- Glutathione S-transferase omega
Sequence:
MSKKVAVVTGANKGIGLAIVRELCKAKFTGDVILTARNEKLGNEAVKMLKSEGFEVSYHHLDICDQGSAKQLSNFLQKTYGGLDVLINNAGMAFKNDATETFGEQAEVTMRTNFWGTLWVCHALLPLLRPNARVVNVSSFVSKKALDTCSPQLQAKFRDTELSEEELCLLMGQFVIAAQQGNHQAQGWPNTAYGTTKIGVTVLSRIQAHYLTKTRAADGILLNACCPGWVRTDMAGSKAPKSPEEGAQTPTYLALLPEGAKEPHGQLVWDKTVQEW
Protein: Methylosome protein WDR77 (Methylosome protein 50) (WD repeat-containing protein 77) (H0Y711)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XCAAPNEGFCSAGVQTEAGVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLSSYRAHAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIGCSAPGYLPTSLAWHPQQSEVFVFGDENGTVSLVDTKSTSCVLSSAVHSQCVTGLVFSPHRLDLSQPSPPSDSVPFLASLSEDCSLAVLDSSLSELFRSQAHRDFVRDATWSPLNHSLLTTVGWDHQVVHHVVPTEPLPAPGPASVTE
Protein: Acyl-protein thioesterase 1 homolog 2 (EC 3.1.2.-) (Palmitoyl-protein hydrolase) (EC 3.1.2.22) (Q55FK4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins with a strong preference for palmitoylated G-alpha proteins over other acyl substrates. Mediates the deacylation of G-alpha proteins such as GPA1 in vivo, but has weak or no activity toward palmitoylated Ras proteins. Has weak lysophospholipase activity in vitro; however such activity may not exist in vivo.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q12354}. Nucleus {ECO:0000250|UniProtKB:Q12354}.
Interaction partners:
- Acyl-protein thioesterase 1 homolog 1
- NADPH--cytochrome P450 reductase
Sequence:
MSNLIEIKSKSTHTATVIFLHGLMDTGKGWETRMENIISMGGLDHIKFVLPTAPTIPISINFGNKGTAWCNVTAFYPGSEEDLIGLEKSMKLVEALIEEEIKNGIPAERIILSGFSQGGALTLYTGYQSKHKLAALITLSGFSPSLSLPSKIKPENKDIPLTMFHGTDDKVVNCKWGELSHKSYLKVGIKNSQFISITNLDHSSNEFELKQVHDLIEKYLPK
Protein: Aryl hydrocarbon receptor nuclear translocator-like 2 (Aryl hydrocarbon receptor nuclear translocator-like protein 2) (A0A0R4IH97)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cryptochrome circadian regulator 3a.
- Cryptochrome-1
- Cryptochrome circadian regulator 1b.
- Cryptochrome 3
- Cryptochrome circadian regulator 3b.
- Circadian locomoter output cycles protein kaput
- Cryptochrome circadian regulator 4
- Cryptochrome circadian regulator 5
- Cryptochrome DASH
- Circadian locomoter output cycles protein kaput
Sequence:
MSSRNTAAGGGDGATGENTGDVLEEEPQGLSASLSGLMTPTSASSLMELPRKRKGSMDNLEMKSASNLDEDMEDDAGRSEDDQHLKIKCIREPHSQIEKRRRDKMNNLIDELAAMIPTCNPMSRKLDKLTVLRMAVQHLKSLKGATSSFAEANYKPAFLPDDELKHLVLRAADGFLFVVGCDRGKIVFVSESVSKTLNYSRTELIGQSLFDYVHPKDIGKVKEQLSASELYPRERLIDAKTGLQVQAELPVGSARLCSGARRSFFCRMKYNKITVKEEKDFQAGASKKKESQRYCTVHCTGYMRTWPTRQLATEGEAEADKESSHFSCLVAMGRVHPHTLPQANGEIKVKPTEFVTRYAMDGKFTFVDQRATTILGYLPQELLGTSCYEYFHLDDLPHLAERHRKVLRSKEKIETNCYKFKTKSGSFVNLQSQWFSFINPWTKEVEYIVSTNTVVSGKSNPGGSGDKAEQPSSSKASEDDAKKSQQVPIIPGISSASGMIYAGCIGTQIANEIMDFNRMNSSPSSGNTSPFSLLQDKSPLALAQASSNVPNGEATDVEMPGKSSSEEEARGGPFSTGDNLMEASSQLDLEGVPGLGALSTDEAAMAVIMSLLETDANLGEAVNFDEMHWSL
Protein: Squalene synthase 13 (PgSS13) (SQS 13) (EC 2.5.1.21) (FPP:FPP farnesyltransferase SS13) (Farnesyl-diphosphate farnesyltransferase SS13) (A0A1P7Y0D0)
Organism: Panax ginseng (Korean ginseng)
Function: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways. Catalyzes the biosynthesis of squalene (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53799}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGSLGAILKHPDDFYPLLKLKIAARHAEKQIPSEPHWAFCYSMLHKVSRSFGLVIQQLGPQLRDAVCIFYLVLRALDTVEDDTSISTEVKVPIVMAFHCHIYDNDWHFSCGTKEYKVLMDEFHHVSNAFLDLGSSYKEAIEDITMRMGAGMAKFICKEVETIDDYDEYCHYVAGLVGLGLSKLFHASGAEDLATDSLSNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPRQIWSKYVDKLEDLKYEENSAKAVQCLNDMVTDALVHAEDCLKYMSDLRGPAIFRFCAIPQIMAIGTLALCFNNTQVFRGVVKMRRGLTAKVIDQTKTMSDVYGAFFDFSCLLKSKVDNNDPNATKTLSRLEAIQKTCKESGTLSKRKSYIIESESGHNSALIAIIFIILAILYAYLSSNLLLNKQ
Protein: Cleavage stimulation factor subunit 2 (A0A0G2K6F9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAGLPVRDPAVDRSLRSVFVGNIPYEATEEQLKDIFSEVGPVVSFRLVYDRETGKPKGYGFCEYQDQETALSAMRNLNGREFSGRALRVDNAASEKNKEELKSLGTGAPVIESPYGESISPEDAPESISKAVASLPPEQMFELMKQMKLCVQNSPQEARNMLLQNPQLAYALLQAQVVMRIVDPEIALKILHRQTNIPTLISGNPQPVHVAGPGSGPNVSMNQQNPQAPQAQSLSGMHVNGAPPMMQASMPGGVPAPVQMAAAVAGPGPGSLAPAGVMQAQVGMQGAGPVPMERGQVPMQDPRAAMQRGALPANVPTPRGLLGDAPNDPRGGTLMTVTGEVEPRAYLGPPPPPHQGPPMHHVPGHEGRGPPPVIDERRCGRDPRGLDARGMEARAMEARGLEARAMEARAMEARAMEARAMEARAMEARAMEARGMDTRGPVPGPRGPIPSGIQGPNPMNMGAVVPQGSRQVMLVAYT
Protein: Anoctamin (A0A8I5Y1S2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU280814}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU280814}.
Interaction partners:
Sequence:
MTWSRSDACCRQAWDSGDVPDSRRPFLAPHTPLPSGLVLENFDQTIVCSTFGSLESQEDFRTPEFEEFNGKPDSLFFTDGQRRIDFVLVYEDESKKENNKKGTNEKQKRKRQAYESNLISHGLQLEATRSVSDDKLVFVKVHAPWEVLCTYAEIMHIKLPLKPNDLKTRSTFDTFNWFTKVLRVNESVIKPEQEFFTAPFEKSRMNDFYILDRDSFFNPATRSRIVYFILSRVKYQVMNNVNKFGINRLVSSGIYKAAFPLHDCKFNYKSEDPNCPSERYLLYREWAHPRSIYKKQPLDLIRKYYGEKIGIYFAWLGYYTQMLLLAAVVGVACFLYGYLNQDNCTWSKEVCDPDIGGQILMCPQCDRLCPFWRLNITCESSKKLCIFDSFGTLIFAVFMGVWVTLFLEFWKRRQAELEYEWDTVELQQEEQPRPEYEAQCNHVVINEITQEEERIPFTTCGKCIRITLCASAVFFWILLIIASVIGIIVYRLSVFIVFSTTLPKNPNGTDPIQKYLTPQMATSITASIISFIIIMILNTIYEKVAIMITNFELPRTQTDYENSLTMKMFLFQFVNYYSSCFYIAFFKGKFVGYPGDPVYWLGKYRNEECDPGGCLLELTTQLTIIMGGKAIWNNIQEVLLPWVMNLIGRYKRVSGSEKITPRWEQDYHLQPMGRLGLFYEYLEMIIQFGFVTLFVASFPLAPLLALVNNILEIRVDAWKLTTQFRRMVPEKAQDIGAWQPIMQGIAILAVVTNAMIIAFTSDMIPRLVYYWSFSIPPYGDHTYYTMDGYINNTLSVFNITDFKNTDKENPYIGLGNYTLCRYRDFRNPPGHPQEYKHNIYYWHVIAAKLAFIIVMEHVIYSVKFFISYAIPDVSKITKSKIKREKYLTQKLLHESHLKDLTKNMGLIAERIGGVADSSVRPKLE
Protein: Vesicular-fusion protein SEC18 (P18759)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
Subcellular location: Cytoplasm.
Interaction partners:
- Alpha-soluble NSF attachment protein
- t-SNARE VTI1
- Syntaxin VAM3
- Synaptobrevin homolog YKT6
- Vacuolar v-SNARE NYV1
- Vacuolar morphogenesis protein 7
- Protein SSO1
- Protein SLY1
- Protein transport protein SEC22
- Protein transport protein SEC1
Sequence:
MFKIPGFGKAAANHTPPDMTNMDTRTRHLKVSNCPNNSYALANVAAVSPNDFPNNIYIIIDNLFVFTTRHSNDIPPGTIGFNGNQRTWGGWSLNQDVQAKAFDLFKYSGKQSYLGSIDIDISFRARGKAVSTVFDQDELAKQFVRCYESQIFSPTQYLIMEFQGHFFDLKIRNVQAIDLGDIEPTSAVATGIETKGILTKQTQINFFKGRDGLVNLKSSNSLRPRSNAVIRPDFKFEDLGVGGLDKEFTKIFRRAFASRIFPPSVIEKLGISHVKGLLLYGPPGTGKTLIARKIGTMLNAKEPKIVNGPEILSKYVGSSEENIRNLFKDAEAEYRAKGEESSLHIIIFDELDSVFKQRGSRGDGTGVGDNVVNQLLAKMDGVDQLNNILVIGMTNRKDLIDSALLRPGRFEVQVEIHLPDEKGRLQIFDIQTKKMRENNMMSDDVNLAELAALTKNFSGAEIEGLVKSASSFAINKTVNIGKGATKLNTKDIAKLKVTREDFLNALNDVTPAFGISEEDLKTCVEGGMMLYSERVNSILKNGARYVRQVRESDKSRLVSLLIHGPAGSGKTALAAEIALKSGFPFIRLISPNELSGMSESAKIAYIDNTFRDAYKSPLNILVIDSLETLVDWVPIGPRFSNNILQMLKVALKRKPPQDRRLLIMTTTSAYSVLQQMDILSCFDNEIAVPNMTNLDELNNVMIESNFLDDAGRVKVINELSRSCPNFNVGIKKTLTNIETARHDEDPVNELVELMTQSA
Protein: E3 ubiquitin-protein ligase MIB2 (EC 2.3.2.27) (Dystrophin-like protein) (Dyslike) (Mind bomb homolog 2) (Mind bomb-2) (RING-type E3 ubiquitin transferase MIB2) (Skeletrophin) (Q8R516)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15824097}. Endosome {ECO:0000269|PubMed:15824097}. Note=Colocalizes with endosomal compartments.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin carboxyl-terminal hydrolase CYLD
- TNF receptor-associated factor 2
- Receptor-interacting serine/threonine-protein kinase 1
- E3 ubiquitin-protein ligase NEURL1
- B-cell lymphoma/leukemia 10
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- CASP8 and FADD-like apoptosis regulator
- E3 ubiquitin-protein ligase NEURL1B
- Tumor necrosis factor
Sequence:
MDLDPHAGVQVGMRVVRGMDWKWGQQDGGEGGVGTVVELGRHGSPSTPDRTVVVQWDQGTRTNYRAGYQGAHDLLLYDNAQIGIRHPNIICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHAFERYETSHSRPVTLSPRQGLPRIPLRGIFQGAKVVRGPDWEWGSQDGGEGKTGRVVDIRGWDVETGRSVASVTWADGTTNVYRVGHKGKVDLRCVGEAAGGFYYKEHLPKLGKPAELQRRVSADGQPFQRGDKVKCLLDTDVLRDMQEGHGGWNPRMAEFIGQMGTVHRITDRGDVRVQFNHETRWTFHPGALTKHNSFWVGDVVRVIGDLDTVKRLQAGHGEWTDDMAPALGRVGKVVKVFGDGNLRVAVGGQRWTFSPSCLVAYRPEEDANLDVAERARENKSAASVSVAGSLSVALDKLRTQKSDPEHPGRLVVEAALGNVARALDLLRRHPEQASYHPALVVDTKNQGRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEVPGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQLVDAKKEDGFTALHLAALNNHREVAQVLIREGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQRHQLLPLVADRAGGDPGPLQLLSRLQASGLPGCTELTVGAAVACFLALEGADVSYANHRGRSPLDLATEGRVLKALQGCAQRFRERQAGGGGGVPPGPRHVLSTPNTVTNLHVSGTAGPEAAECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQVVISKKLRPDGSEVVNAIQVPGPPRQLVEELQSRYRQMEERITCPICIDSHIRLVFQCGHGACAPCGAALNACPICRQPIRDRIQIFV
Protein: UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase (EC 2.4.1.285) (Neomycin biosynthesis protein 15) (Neo-15) (Neomycin biosynthesis protein K) (Q53U11)
Organism: Streptomyces fradiae (Streptomyces roseoflavus)
Function: Glycosyltransferase involved in the biosynthesis of neomycin by mediating glycosylation of ribostamycin with UDP-GlcNAc as a sugar donor to generate 2'''-acetyl-6'''-hydroxyneomycin C.
Interaction partners:
Sequence:
MAEAPAGRALFEIYDEGFDSPSWGGVETALWHLSRSLREAGTEAEFYRSSEGADLDALAARVERDRVDAVFPLVESDLFEGAAWRRLPALHARTVRVWHDVSRLSADLSAPPPCPVHARVPALPGAPVAEGCPARGAHPEGPMREVFLGEWPWTRCFPRRSVIPWAADHVPAKDLCDPSGPVVLQLGKIDTVDAERCLRRLTGAGVALRVVFATWSRRGREARELVRAHQGAGRRVEVLDAYDIRTDWERVFGGASLFLLPSVFHETYNFAAAEAVQLGVPVAALGEGGNLPRFASLTAPTPDALVDRLLAGGGAVAPRPRPAAGWRDVAARYAEVIREHPAAGAGPAVPAGAGEGRGGREEEHGG
Protein: Leucine-rich repeat protein (LRRP) (Q38B07)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTSNIAPEDPGDVPLEVENPLTYEVVKESLSALSSNADGWLVYAQAKLCSLSLTSIDLLSSYVHLQRLSLDDNRLVTLKPLRSLCCLIHFSAAGNALTNDVFDDLASSSVTLERLNLDRNALTSLGGLSKLPFLMDFSAAENGITELHADDFSLLHSLTRLNLKLNKISRVNLDTFSKCLTVRALNLSYNSIVDKRFVVHLAGNLESLNLEHNAVEGFSDFDVLHSLVFLFLSNNNIQNWDGLEGLSKLKNIRVLTLEGNPVLRSHDGTTSGNSSSLSYEAHVQQDVDFAACRSLNVSTQKEGMPLPTVSSALLTSLTAPQVRSIIHHLPAAPYGDVQWEVDGNHELSQLPYEEQCRFRVISMMPQLQVLDSTEVHAGEIPRAMRLFCKEMKSAEVLADARNFPSGSGLKAIGLHRLKSGSKYMT
Protein: Transcription factor MYB3R-2 (Myb-related protein MYB3R-2) (OsMYB3R-2) (Q0JHU7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription factor involved in abiotic stress responses. May play a regulatory role in tolerance to salt, cold, and drought stresses. Transcriptional activator that binds specifically to a mitosis-specific activator cis-element 5'-(T/C)C(T/C)AACGG(T/C)(T/C)A-3', found in promoters of cyclin genes such as CYCB1-1 and KNOLLE (AC Q84R43). Positively regulates a subset of G2/M phase-specific genes, including CYCB1-1, CYCB2-1, CYCB2-2, and CDC20.1 in response to cold treatment.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:17293435}.
Interaction partners:
Sequence:
MGAMAMVEQEGCVENRQPLAASSSSVSDGSSYGGGGGGLAQMSPPVSSSANSISGLRRTSGPIRRAKGGWTPEEDETLRKAVEAYKGRNWKKIAECFPYRTEVQCLHRWQKVLNPELIKGPWTQEEDDQIIDLVKKYGPTKWSVIAKALPGRIGKQCRERWHNHLNPEIRKDAWTTEEEQALINAHRIYGNKWAEIAKVLPGRTDNSIKNHWNSSLRKKQDMYNTSNNMVVPKLLVHDKFKDKPKLMAMEGHLDLNKAPIINSKDQPGTAHRSNCSGFLSRSSLPTAQPLTSREASVVDGSAVTLVAQALESDSVRGKGLEIDSVHEKGLEVNSAPDHTGNSWTIQLEAAPSKGEAELSLKNEARSLGPLCYQIPNMEDVVPVSSSLFSDHLTGNHTSEHCGDDILSPAGCTTPPPTKGKLTSQLSVDSILKSAANSFPGTPSILKRRKRDKSTPVSASEMKISGSNTDRFYTPMGMEPATATPESFKTTSFLSLGSLDGSVKSFDVSPQYRARSKRMALTKTVEKQLDFSSDGLDTCGSEILNSSCNNSQSTLSITEAPKLKEKEHAVQLENLTKNFAHTTNLDVT
Protein: Crossover junction endonuclease MUS81 (EC 3.1.22.-) (Protein MMS AND UV SENSITIVE 81) (AtMUS81) (Q5W9E7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks, nicked Holliday junctions and also intact Holliday junctions with a reduced efficiency. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. Plays a role in DNA repair and in genotoxic stress-induced homologous recombination (HR) in somatic cells. Mediates a subset of meiotic recombination events that are insensitive to crossover interference. Together with SEND1, essential for the resolution of toxic replication structures to ensure genome stability, and to maintain telomere integrity and replication.
Subcellular location: Nucleus {ECO:0000269|PubMed:18182028}. Nucleus, nucleolus {ECO:0000269|PubMed:18182028}.
Interaction partners:
- DNA excision repair protein ERCC-1
- DNA repair endonuclease UVH1
- DNA topoisomerase 3-alpha
- DEAD-box ATP-dependent RNA helicase FANCM
- DNA repair protein UVH3
- ATP-dependent DNA helicase Q-like 4A
- DNA mismatch repair protein MSH4
- Exonuclease 1
- AT5G19950 protein
- ATP-dependent DNA helicase Q-like 4B
Sequence:
MDDERRVLCPENRGLAAYVLQKKQEYAEKPKGLSENLERTFVKGYRSVCDAKDPINTLKDLSQIKGFGKWMVKLMKGYFDTAVESSEQEDLPDNRAGKKANGKKRYIPQRNSVGYALLITLHRRTTNGKEFMRKQELIDAADANGLSHAPVGPEKGKGKAGLGHSKREWYSGWSCMTTLIQKGLVVKSSNPAKYMLTVEGREVANECILRSGLPDSVDILSVDEMDPTPQAKKTPNQNPTCSFTMREELPYVDPRCRAQSAIPSDILEKFTPFGYSKEQVVAAFREVSDGSGDKDPSTLWLSVMCHLRQAEVYNSCPDSRNSKKDSSGPFKSQIRQVDLEGSRAKKFRSCNDGSTLNPCSSGSSHAVKACSSSLASDGTKGITNIPRLPPLQFGETFEEAYDVILILDDREKFATKGSRSRNIVENICSEFNIKIEVRRLPVGDCIWIARHKYLETEYVLDFIAERKNVDDMRSSIRDNRYRDQKLRLQRSGFKKLIYILEGDPNHSDAAESIKTACFTTEILEGFDVLRTHGLGETLRKYGYLTKSIYQYYKLRVNDNDQSKGAASCPSFDSFVKRCQDLDKMTISDVFAIQLMQVPQVTEEIAIAVLDMYPTLLSLASAYSHLEADVSAQEEMLRNRSNNVICASASKNIFKLVWGE
Protein: DNA replication licensing factor mcm5-A (xMCM5-A) (EC 3.6.4.12) (CDC46 homolog A) (xCDC46-A) (CDC46p) (p92) (P55862)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}. Chromosome {ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}.
Interaction partners:
Sequence:
MSGFDDLGVYYSDSFGGEQQVGDDGQAKKSQLKKRFREFLRQYRIGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEDLADYLYKQPTEHLQLLEEAAQEVADEVTRPRPAGEETIQEIQVMLRSDANPANIRSLKSEQMSHLVKIPGIIIAATAVRAKATKISIQCRSCRNTIGNIAVRPGLEGYAMPRKCNTEQAGRPNCPLDPYFIIPDKCKCVDFQTLKLQESPDAVPHGELPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIRKSGKTSTKGRDRVGVGIRSSYIRVVGIQVDTEGTGRSAAGAITPQEEEEFRRLAAKPDIYETVAKSIAPSIYGSSDIKKAIACLLFGGSRKRLPDGLTRRGDVNLLMLGDPGTAKSQLLKFVERCSPIGVYTSGKGSSAAGLTASVMRDPVSRNFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVYGRWDDTKGEENIDFMPTILSRFDMIFIVKDEHNEQRDMTLAKHVMNVHLSARTQSSSVEGEVDLNTLKKYIAYCRAKCGPRLSAEAAEKLKNRYILMRSGAREHERETEKRSSIPITVRQLEAIVRISESLGKMKLQPFATETDVEEALRLFQVSTLDAAMSGSLSGVEGFTTQEDQEMLSRIEKQMKKRFAIGSQVSEHSIIQDFLKQKYPEHAIHKVLSLMMRRGEIQHRLQRKVLYRIK
Protein: Derlin-2 (Degradation in endoplasmic reticulum protein 2) (Der1-like protein 2) (F-LANa) (Q8BNI4)
Organism: Mus musculus (Mouse)
Function: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins. May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9GZP9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9GZP9}.
Interaction partners:
- Protein sel-1 homolog 1
- Derlin-1
- E3 ubiquitin-protein ligase synoviolin
- Protein OS-9
- Lipid droplet-regulating VLDL assembly factor AUP1
- Derlin-3
- Transitional endoplasmic reticulum ATPase
- FAS-associated factor 2
- E3 ubiquitin-protein ligase AMFR
- Ubiquitin recognition factor in ER-associated degradation protein 1
Sequence:
MAYQSLRLEYLQIPPVSRAYTTACVLTTAAVQLELITPFQLYFNPELIFKHFQIWRLITNFLFFGPVGFNFLFNMIFLYRYCRMLEEGSFRGRTADFVFMFLFGGFLMTLFGLFVSLVFLGQAFTIMLVYVWSRRNPYVRMNFFGLLNFQAPFLPWVLMGFSLLLGNSIIVDLLGIAVGHIYFFLEDIFPNQPGGIRILKTPSILRTIFDTPDEDPNYNPLPEERPGGFAWGEGQRLGG
Protein: Transmembrane protein 203 (Q969S6)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of cellular calcium homeotasis. Required for spermatogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25996873}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q8R235}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R235}; Multi-pass membrane protein {ECO:0000255}. Note=Co-localizes with STING1 in the lysosome membrane, mediates lysosomal localization of STING1. {ECO:0000250|UniProtKB:Q8R235}.
Interaction partners:
Sequence:
MLFSLRELVQWLGFATFEIFVHLLALLVFSVLLALRVDGLVPGLSWWNVFVPFFAADGLSTYFTTIVSVRLFQDGEKRLAVLRLFWVLTVLSLKFVFEMLLCQKLAEQTRELWFGLITSPLFILLQLLMIRACRVN
Protein: PDZ and LIM domain protein 2 (PDZ-LIM protein mystique) (Q96JY6)
Organism: Homo sapiens (Human)
Function: Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15659642}. Nucleus {ECO:0000269|PubMed:15659642}. Note=May be partially nuclear.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton. Note=Colocalizes with beta-1 integrin (ITGB1) and alpha-actinin but not with paxillin (PXN).; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus.
Interaction partners:
- Alpha-actinin-4
- Unconventional myosin-VI
- Alpha-actinin-1
- PDZ and LIM domain protein 7
- PDZ and LIM domain 5
Sequence:
MALTVDVAGPAPWGFRITGGRDFHTPIMVTKVAERGKAKDADLRPGDIIVAINGESAEGMLHAEAQSKIRQSPSPLRLQLDRSQATSPGQTNGDSSLEVLATRFQGSVRTYTESQSSLRSSYSSPTSLSPRAGSPFSPPPSSSSLTGEAAISRSFQSLACSPGLPAADRLSYSGRPGSRQAGLGRAGDSAVLVLPPSPGPRSSRPSMDSEGGSLLLDEDSEVFKMLQENREGRAAPRQSSSFRLLQEALEAEERGGTPAFLPSSLSPQSSLPASRALATPPKLHTCEKCSTSIANQAVRIQEGRYRHPGCYTCADCGLNLKMRGHFWVGDELYCEKHARQRYSAPATLSSRA
Protein: Endonuclease III-like protein 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase) (O35980)
Organism: Mus musculus (Mouse)
Function: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:12531031}.
Interaction partners:
- DNA repair nuclease/redox regulator APEX1
- Endonuclease 8-like 3
- N-glycosylase/DNA lyase
- DNA repair protein XRCC1
- Endonuclease 8-like 1 lyase Neil1)
- Endonuclease 8-like 2 lyase Neil2)
- Adenine DNA glycosylase
- Flap endonuclease 1
- Uracil-DNA glycosylase
- G/T mismatch-specific thymine DNA glycosylase
Sequence:
MNSGVRMVTRSRSRATRIASEGCREELAPREAAAEGRKSHRPVRHPRRTQKTHVAYEAANGEEGEDAEPLKVPVWEPQNWQQQLANIRIMRSKKDAPVDQLGAEHCYDASASPKVRRYQVLLSLMLSSQTKDQVTAGAMQRLRARGLTVESILQTDDDTLGRLIYPVGFWRNKVKYIKQTTAILQQRYEGDIPASVAELVALPGVGPKMAHLAMAVAWGTISGIAVDTHVHRIANRLRWTKKMTKTPEETRKNLEEWLPRVLWSEVNGLLVGFGQQICLPVHPRCQACLNKALCPAAQDL