wanglab/gogpt-training-data huggingface dataset:
Protein: Bifunctional peptidase and arginyl-hydroxylase JMJD5 (EC 1.14.11.73) (EC 3.4.-.-) (JmjC domain-containing protein 5) (Jumonji C domain-containing protein 5) (L-arginine (3R)-hydroxylase KDM8) (Q8N371)
Organism: Homo sapiens (Human)
Function: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-terminal tail of histone H3 at monomethylated lysine residues, preferably at monomethylated 'Lys-9' (H3K9me1). The histone variant H3F3A is the major target for cleavage. Additionnally, acts as Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (R)-stereospecific hydroxylation at C-3 of 'Arg-137' of RPS6 and 'Arg-141' of RCCD1, but the biological significance of this activity remains to be established. Regulates mitosis through different mechanisms: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with RCCD1. Possibly together with RCCD1, is involved in proper mitotic spindle organization and chromosome segregation. Negatively regulates cell cycle repressor CDKN1A/p21, which controls G1/S phase transition. Required for G2/M phase cell cycle progression. Regulates expression of CCNA1/cyclin-A1, leading to cancer cell proliferation. Also, plays a role in regulating alpha-tubulin acetylation and cytoskeletal microtubule stability involved in epithelial to mesenchymal transition. Regulates the circadian gene expression in the liver (By similarity). Represses the transcriptional activator activity of the CLOCK-BMAL1 heterodimer in a catalytically-independent manner. Negatively regulates the protein stability and function of CRY1; required for AMPK-FBXL3-induced CRY1 degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:20457893, ECO:0000269|PubMed:28982940}. Chromosome {ECO:0000269|PubMed:24981860}. Note=Colocalizes with trimethylated 'Lys-9' of histone H3 (H3K9me3). {ECO:0000269|PubMed:24981860}.
Interaction partners:
- RCC1 domain-containing protein 1
- Small ribosomal subunit protein eS6
- Pyruvate kinase PKM
- Probable splicing factor YJU2B
- RecQ-like DNA helicase BLM
Sequence:
MAGDTHCPAEPLAREGTLWEALRALLPHSKEDLKLDLGEKVERSVVTLLQRATELFYEGRRDECLQSSEVILDYSWEKLNTGTWQDVDKDWRRVYAIGCLLKALCLCQAPEDANTVAAALRVCDMGLLMGAAILGDILLKVAAILQTHLPGKRPARGSLPEQPCTKKARADHGLIPDVKLEKTVPRLHRPSLQHFREQFLVPGRPVILKGVADHWPCMQKWSLEYIQEIAGCRTVPVEVGSRYTDEEWSQTLMTVNEFISKYIVNEPRDVGYLAQHQLFDQIPELKQDISIPDYCSLGDGEEEEITINAWFGPQGTISPLHQDPQQNFLVQVMGRKYIRLYSPQESGALYPHDTHLLHNTSQVDVENPDLEKFPKFAKAPFLSCILSPGEILFIPVKYWHYVRALDLSFSVSFWWS
Protein: Hemin import ATP-binding protein HmuV (EC 7.6.2.-) (Q56993)
Organism: Yersinia pestis
Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system (Probable).
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01718}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01718}.
Interaction partners:
- Hemin transport system permease protein HmuU
- Hemin-binding periplasmic protein HmuT
- Hemin transport protein HmuS
- FecCD transport family protein
- Hemin receptor
- Putative FecCD-family membrane transport protein
- Putative iron-siderophore transport system,transmembrane component
- Vitamin B12 import system permease protein BtuC
- Putative iron-siderophore transport system,membrane permease component
- Similar to Escherichia coli ferrichrome transport system permease protein FhuB SW:FHUB_ECOLI
Sequence:
MVDMAVTPVALLEASHLHYHVQQQALINDVSLHIASGEMVAIIGPNGAGKSTLLRLLTGYLSPSHGECHLLGQNLNSWQPKALARTRAVMRQYSELAFPFSVSEVIQMGRAPYGGSQDRQALQQVMAQTDCLALAQRDYRVLSGGEQQRVQLARVLAQLWQPQPTPRWLFLDEPTSALDLYHQQHTLRLLRQLTRQEPLAVCCVLHDLNLAALYADRIMLLAQGKLVACGTPEEVLNAETLTQWYQADLGVSRHPESALPQIYLRQ
Protein: Probable conserved transmembrane protein (O06252)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible conserved transmembrane protein
- Bifunctional NAD
- Methyltransferase domain-containing protein
- Protein-glutamine gamma-glutamyltransferase-like C-terminal domain-containing protein
- Probable conserved transmembrane protein
- Uncharacterized protein Rv2067c
- Tat
- PE-PGRS family protein PE_PGRS42
- Uncharacterized protein Rv0048c
Sequence:
MGRILRVVVGLVLVIAAYVTVIALYHSTGLGRPHEVAHGRPTADGTTVTLHVEQLQTIKGVLVANLAVSPGTELLDSQTQGLKDDLTVTVTSVVTPTKRTWSSGSLPGVFPVPLTISGDPANWPFDHYRSGPITVQLYRGAAHAPERVSVTFVDRLPGWNVDISGVGDANVPAPYRVGLHRSPSSVAFGTVIVGVLIALAGVGLFVAVQTARGRRQFQPPMTTWYAAMLFAVIPLRNALPDAPPIGFWIDVTVVLWVVVALVTSMVLYILCWWWHLKPDVDETM
Protein: Probable alginate O-acetylase AlgJ (EC 2.3.1.-) (Alginate biosynthesis protein AlgJ) (Q51393)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Together with AlgI and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases resistance to opsonic killing in the host.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:12003941}; Peripheral membrane protein {ECO:0000269|PubMed:12003941}; Periplasmic side {ECO:0000269|PubMed:12003941}. Periplasm {ECO:0000269|PubMed:12003941}.
Interaction partners:
- Alginate biosynthesis protein AlgK
- Mannuronan C5-epimerase
- Probable alginate O-acetylase AlgI
- Alginate lyase
- Mannuronan synthase
- Alginate biosynthesis protein AlgF
- Alginate biosynthesis protein AlgA
- Mannuronan synthase
- Alginate production protein AlgE
- GDP-mannose 6-dehydrogenase
Sequence:
MTQSISRPLQYAYIAAFGGLLLGLAGWSLKSVPGFSAAADTPLLNGKLAHAFEAHYDKEFPIKRLGTNLWAALDYTLFHEGRPGVVIGKDGWLFTDEEFKPAPSGQQLEDNWALVRGVQRELNRRGVKLVLAVIPAKARLYPEHIGREQPAALHDSLYQDFLARARAAGIDSPDLLGSLRQAKDNGAVFLRTDTHWSPLGAETVAQRLGAEIRETHLLDVPAQNFVTRVGEERTHKGDLLSFLPLDPLFDELLPRPEQLQQRTTEAAPALPGGQQSGAGDDLFGDSQQPRLALVGTSYSANPRWNFEGALKQALSADLINYAKEGKGPLEPMLELLQDEGFRKDPPQLLVWEFPERYLPMASDLSQFDADWVAQLKASGGRDERLAASRND
Protein: Transmembrane protein 59 (Thymic dendritic cell-derived factor 1) (Q9QY73)
Organism: Mus musculus (Mouse)
Function: Acts as a regulator of autophagy in response to S.aureus infection by promoting activation of LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C). Acts by interacting with ATG16L1, leading to promote a functional complex between LC3 and ATG16L1 and promoting LC3 lipidation and subsequent activation of autophagy. Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of several proteins such as APP, BACE1, SEAP or PRNP. Inhibits APP transport to the cell surface and further shedding.
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q9BXS4}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9BXS4}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9BXS4}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9BXS4}; Single-pass type I membrane protein {ECO:0000255}. Note=Mainly localizes to late endosomes/lysosomes. Probably first exported to the cell surface and then actively endocytosed to transiently localize in early endosomes on its way to the late endosomal/lysosomal compartment where it becomes quickly degraded. {ECO:0000250|UniProtKB:Q9BXS4}.
Interaction partners:
- Mitochondrial disaggregase
- Autophagy-related protein 16-1
- Constitutive coactivator of PPAR-gamma-like protein 2
Sequence:
MAAPKGKLWVQAQLGLPPLLLLTMALAGGSGTAAAEAFDSVLGDTASCHRACQLTYPLHTYPKEEELYACQRGCRLFSICQFVDDGLDLNRTKLECESACTEAYSQPDEQYACHLGCQDQLPFAELRQEQLMSLMPRMHLLFPLTLVRSFWSDMMDSAQSFITSSWTFYLQADDGKIVIFQSKPEIQYAPQLEQEPTNLRESSLSKMSYLQMRNSQAHRNYLEEEESDGFLRCLSLNSGWILTTTLVLSVMVLLWICCAAVATAVEQYVPPEKLSIYGDLEFMNEQKLSRYPAPSLVIVRSQTEEHEEAGPLPTKVNLAHSEI
Protein: Peroxidase 32 (Atperox P32) (EC 1.11.1.7) (ATP16a) (PRXR3) (Q9LHB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000305}. Vacuole {ECO:0000305}. Note=Carboxy-terminal extension appears to target the protein to vacuoles.
Interaction partners:
- Transducin family protein / WD-40 repeat family protein
- Beta-glucosidase 32
- Heavy metal-associated isoprenylated plant protein 4
Sequence:
MNFSYSSLSTWTTLMTLGCLLLHSSISSAQLTPTFYDNTCPSVFTIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAAPNANSARGFPVIDRMKAAVETACPRTVSCADILTIAAQQAVNLAGGPSWRVPLGRRDSLQAFFALANTNLPAPFFTLPQLKASFQNVGLDRPSDLVALSGGHTFGKNQCQFIMDRLYNFSNTGLPDPTLNTTYLQTLRGQCPRNGNQTVLVDFDLRTPTVFDNKYYVNLKELKGLIQTDQELFSSPNATDTIPLVREYADGTQKFFNAFVEAMNRMGNITPLTGTQGQIRQNCRVVNSNSLLHDVVEIVDFVSSM
Protein: Probable methyltransferase PMT3 (EC 2.1.1.-) (Q93YV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Fasciclin-like arabinogalactan protein 2
Sequence:
MKGRSDGGQKKRVIALVCVAAVVLVFVYLFYGSSDHRASAIEYGRKLGLGGDDDDTKQDDTSSSFGVDDGFTPRSFPVCDDRHSELIPCLDRNLIYQMRLKLDLSLMEHYERHCPPPERRFNCLIPPPNGYKVPIKWPKSRDEVWKVNIPHTHLAHEKSDQNWMVVKGDKINFPGGGTHFHYGADKYIASMANMLNYPNNVLNNGGRLRTVFDVGCGVASFGGYLLSSDILTMSLAPNDVHQNQIQFALERGIPASLGVLGTKRLPYPSRSFELSHCSRCRIDWLQRDGILLLELDRVLRPGGYFAYSSPEAYAQDEEDLRIWREMSALVERMCWKIAAKRNQTVIWQKPLTNDCYLEREPGTQPPLCRSDNDPDAVWGVNMEACITSYSDHDHKTKGSGLAPWPARLTSPPPRLADFGYSTGMFEKDTELWRQRVDTYWDLLSPRIESDTVRNIMDMKASMGSFAAALKEKDVWVMNVVPEDGPNTLKLIYDRGLMGAVHSWCEAFSTYPRTYDLLHAWDIISDIKKKGCSEVDLLLEMDRILRPSGFIIIRDKQRVVDFVKKYLKALHWEEVGTKTDSDSDQDSDNVVFIVQKKLWLTSESLRDME
Protein: U7 snRNA-associated Sm-like protein LSm10 (Q8QZX5)
Organism: Mus musculus (Mouse)
Function: Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing (By similarity). Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed (By similarity). Required for cell cycle progression from G1 to S phases (By similarity). Binds specifically to U7 snRNA (By similarity). Binds specifically to U7 snRNA (By similarity). Binds to the downstream cleavage product (DCP) of histone pre-mRNA.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- U7 snRNA-associated Sm-like protein LSm11
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D2
- Nuclear cap-binding protein subunit 2
- Cleavage and polyadenylation specificity factor subunit 3
- Histone RNA hairpin-binding protein
- U6 snRNA-associated Sm-like protein LSm4
Sequence:
MALSHSVKERTISENSLIILLQGLQGQITTVDLRDESVARGRIDNVDAFMNIRLANVTYTDRWGHQVELDDLFVTGRNVRYVHIPDGVDITATIEQQLQIIHRVRNFGGKGQGRREFPSKRP
Protein: Acetyl-CoA C-acyltransferase (G8BEF7)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase
- Acyl-coenzyme A oxidase
- Citrate synthase
- Succinyl-CoA:3-ketoacid-coenzyme A transferase
- Acetyl-coenzyme A synthetase
- Acetyl-coenzyme A synthetase
- Malate synthase
- methylmalonate-semialdehyde dehydrogenase
- Peroxin-7
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MFKKAAKDIVVLSALRTAVTKSVKGGLAQLYPEELLYQVLRGSISKSNVDPNLVDDVLVGTVLQTLGGQKASSLAVKKAGFPIKTTVNTINRQCASSAQAITYSAGSILSGENKFTIAAGVESMTHDYFPHRGIPQRIYQPFFEDASEEAKNVLTPMGITSESVAEKFGIGRQSQDEFAVQSHLKAAKATESGHFAKEIIPIEARNEAGEAKLVEKDDGIRPGSTYEKLSTLKPVFKENGVTTAGNSSQISDGASAVILTTRENAEKHGYKPIARFVGSSVAGVPSGLMGIGPSEGIPLLLERFGLTNMDIGIFELNEAFASQSIYCIEKLGLDYDKVNPYGGAIAIGHPLGATGGRVVSTLLNGLKAQNKELGVVSMCTSTGQGYAGLFINED
Protein: AT09010p (Q5BHV4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
RFLDMLIEPTLNRDLGSLTVANSGLSAAHWKMEPHPQRITSLAPHASSVAAASVAAAAAAAAAAAAAAAAGAGSGAVAGGGGATSTSPTSVQIPPGFGGGGSTGGIPPGAGGPTGSTLNTLMSQHRLLEFSRFGGLRGYDIAQHMLTQQGAVSKLLGSLRPPGLIGGSKPKVATPTVVSKIEQYKRENPTIFAWEIRERLISEGVCTNATAPSVSSINRILRNRAAERVATEFARTAAYGLYPPPPHPYGSFTWHPAGNVPGGQGVPPPPPPSALWSVAAPTLANLPPSAASAVPVSTCGSLSSAHLMAGGAGGTPTNRAISPGSGSHDTLESADENRHIDSDYLDDDDEPKFRRNRTTFSPEQLEELEKEFDKSHYPCVSTRERLSSRTSLSEARVQVWFSNRRAKWRRHQRMNLLKRQRSSPANPLHSQQSNDAPASSPTPSNHSSASTSAPVAPVPPPQQPLPLCGDHSPQGPPPSVLLHPLHGPPGGHHHHHPLHLPTHPAALHLLSHYHQQQQQQQQQQHQQQQQQHHQQQQQLSPSGCNPAANHLSMGGERSAFRSLVSSPSAAAFLGLARQYAVAASLTVAEEQRSRLHYSAGGLGSGGEGTGPNTNTTQSGGSTMTVDNSSSDSDEEINVHDDSDGEIESSAATAAKVAHLSSSDAPATLQFLKHDR
Protein: Indoleamine 2,3-dioxygenase (EC 1.13.11.52) (Q2UJE7)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Kynureninase 1
- Kynureninase 2
- Indoleamine 2,3-dioxygenase
- aromatic-amino-acid transaminase
- aromatic-amino-acid transaminase
- Indoleamine 2,3-dioxygenase
- Aromatic-L-amino-acid/L-histidine decarboxylase
- Amine oxidase
- Amine oxidase
- Amine oxidase
Sequence:
MRYTPEVSLDEYGVSLQNGFLPHSPPLKTMESPYYWPWEHIVSDLPDHIRFRTIRQAVETLPVLSTSKLQGEPEWRRAYLLLAYLTHAYIWGGEKPKDVLPPAISSPFLEVSSHLELPPCATYAALNLWNYATSDPNADLTDPDLLSVTASFTGTKDEEWFLMISVALEAKGAQLIPLMLDTIHAVSIDDAQLACDSLLALSEGLKELRKLLERMYEKNRPSVFYHQLRPLLAGSKNMASAGLPNGVFYDIGDGQGQWHQYSGGSNAQSSLIQTFDIFLGVEHIATGGMKTNDAVQPRAKNGFMQEMRNYMPGPHRRFLEMLTRVSNVRAYALSHKANSPIRDAYNAAVMSLGVFRDSHIQIVTRYIIMAAKAKPPTNESTQVNLATSTTTHMRDKNEKLTGGIHGTGGTDLIPFLKQTRDTTKATASYD
Protein: Putative ATP-dependent RNA helicase BoYb (EC 3.6.4.13) (Brother of Yb) (Q9VNP5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in primary piRNA biogenesis in germline cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21863019}. Note=Localizes to Yb bodies.
Interaction partners:
- Protein vreteno
- Probable ATP-dependent RNA helicase spindle-E
- Tudor domain-containing protein krimp
- Qin
- Inactive peptidyl-prolyl cis-trans isomerase shutdown
- Mitochondrial cardiolipin hydrolase
- Splicing factor 3B subunit 4
- Splicing factor 3A subunit 2
- Probable RNA helicase armi
- PHD finger-like domain-containing protein 5A
Sequence:
MIKISDEKTWQSSRDSVYEVGDSYSGQNANRPLVATNCSEYAVAHANCQLRPVRRFAEVSLLPDILETMRNLGLNRLLRLQSYTWPHLAGGSGHGAMIVGSPASGRTFAYIPPVCHAVSRALMDFTGQCEDVEHDISQPDRYGPIALILVPDLRRVHQVSAMCLALLRKAHKNDSVTLALNVSSTKSSQFFLKLLNGVGCLVATPAQLVWFWQEAPGLMRFPCLQFLVYDDVDLMSREQLQDVQQVLQEILPLSHSPQVVMVSKSYCHTLMSKLRAVNDKPALVFGDILEAALYGGTRIRISIMRSEAKANAVVQMLQQCSPEEFRTVIFCSDDGDMQCLVAALEVQHYSCLPYYQTADLEVRQQVHSWQARSNGVILLCTDNCPELDIRDAHTIIHHSMSHSWSKFKLRHLKISDNLCNMVKPTASIVKKPLYSLVLLDDNNHRQLPRLVDFLQLHQKVDHRLVEVAKRIRQELGKARNDQHQLCDQILVLGKCYDPVCESRHRLSHIDRRPDYLPASGDVKVQLVKVYSPTHFCVRLLEHLPPKGTWRMMEYSAVQEFRMQLTQIKEPRRYWPPVAGAICMYHTTFTKERVRVLKVAAIKNTNIVQSDLTVKLQALDVDTRIFSTNCGKLFECPEALQQEAPLACDLRLPGWVPYFGERSWTEENIRNVNLILTQLPKDHFLQAKILFVAAGTLFVQDLVAIMYADQFKAHVRHLSLARRLVEATLVKRSENAAEMIREFFAEVIIEDDIDENVQDSKEKANSKPHEKMKGKMTDQPAKLQSQPPLSGRCLRLANMAHESVKENQLHQELQERRYETPEIPHQSNESDIPQSNEDRFSQLYECIMNCASLQLEDESKPAKHPDHVLSESVEFHKIMTNEDATPDHTQEKTALLLLPNNVARPSVTYYQTMTTLEFQVFLPEDDHDYKALLLGAQLFFRAISKSSDLILQFIMTLRFPYSSMSHNIRGRTVYISVKKLLALIDPLAFREYRFLKPNHDLFDKVDKQLQETQNRLVRFLEDMNYVKRNFEGQEKRETSEDEEVNVEGIERPDCHKIWDL
Protein: Pentatricopeptide repeat-containing protein At2g15630, mitochondrial (Q9ZQF1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
Sequence:
MRRFTVPCILRHRISILSGAGYSPAAARLSSLAQTSTPESVLPPITSEILLESIRSSQWHIVEHVADKLTPSLVSTTLLSLVKTPNLAFNFVNHIDLYRLDFQTQCLAIAVISKLSSPKPVTQLLKEVVTSRKNSIRNLFDELVLAHDRLETKSTILFDLLVRCCCQLRMVDEAIECFYLMKEKGFYPKTETCNHILTLLSRLNRIENAWVFYADMYRMEIKSNVYTFNIMINVLCKEGKLKKAKGFLGIMEVFGIKPTIVTYNTLVQGFSLRGRIEGARLIISEMKSKGFQPDMQTYNPILSWMCNEGRASEVLREMKEIGLVPDSVSYNILIRGCSNNGDLEMAFAYRDEMVKQGMVPTFYTYNTLIHGLFMENKIEAAEILIREIREKGIVLDSVTYNILINGYCQHGDAKKAFALHDEMMTDGIQPTQFTYTSLIYVLCRKNKTREADELFEKVVGKGMKPDLVMMNTLMDGHCAIGNMDRAFSLLKEMDMMSINPDDVTYNCLMRGLCGEGKFEEARELMGEMKRRGIKPDHISYNTLISGYSKKGDTKHAFMVRDEMLSLGFNPTLLTYNALLKGLSKNQEGELAEELLREMKSEGIVPNDSSFCSVIEAMSNLDAKKSDS
Protein: Reticulon-like protein 2 (Q12443)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Reticulon-like protein 1
- Protein YOP1
- Meiotic sister chromatid recombination protein 1
- Protein SEY1
- Catalase T
- Inactive diphosphatase DCS2
- Phosphate metabolism protein 7
- Endoplasmic reticulum junction formation protein lunapark
- Protein HBT1
- Aldehyde dehydrogenase [NAD
Sequence:
MNRNTTTNKNANLNNSRNANAPGEAGHQNKTGLIYWTNPSKSGASFAATLVSLLILRNVNVISVLLKIGYMVLFTSFAVELSTKVLFDKGVVSRFGMQESPDLVGVLKPHIDRELDRLPALEDRIRKLVFAHRTRNNFTIGVSLYFLHGLFAIFSMNTVLIMTTIFLYTVPLIYDRKQARIDRAIDRMKDLVIHRFHKNYNKVVEKTEPYIDKIIPPQTDEGSYSTSISNENKSSTSQRNKSGLSSSEFDNMNDTSASKSGKDSYSTSQYNRAEYPVSQNENIGTLKSGKQEIPTEKDFNNRHENFSKPDVKTYDPRTVDIEEELAAHQRELEQNLKDGDYNLVGSKEIPDPITVPAPTRHTTKPAESQSIPIKNNETLHKTTHGLKQKLQHA
Protein: Mitochondrial fission regulator (B4DRE5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004570}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004570}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004570}.
Interaction partners:
Sequence:
MKESRLPPPGAAQWLPCPSSAGAGSNVRNGSHCAVSVSLLQTIPIWQNKPHGAARSVVRRIGTNLPLKPCARASFETLPNISDLCLRDVPPVPTLADIAWIAADEEETYARVRSDTRPLRHTWKPSPLIVMQRNASVPNLRGSEERLLALKKPALPALSRTTELQDELSHLRSQIAKIVAADAASASLTPDFLSPGSSNVSSPLPCFGSSFHSTTSFVISDITEETEVEVPELPSVPLPCSASPECCKPEHKAACSSSEEDDCVSLSKASSFADMMGILKDFHRMKQSQDLNRSLLKEEDPAVLISEVLRRKFALKEEDISRKGN
Protein: Moira, isoform B (A0A0B4JDA0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNTLGPKKDGSPNIDFFQSPETLQGFESIRQWLQKNCKKYLAHSSEPITKESLAQLLIHFLQYVEAKLGKNSADPPATRIPMRCFLDFKSGGGLCIIFSTMFRFRAEQRGKKFDFSIGKNPTRKDPNIQLLIEIEQALVEADLYRIPYIYIRPEIEKGFEGKLREILDNRRVEIVSDEEDATHIVYPVVDPHPDEYARPIFKRGGHVMLHWYYFPESYDSWAVNNFDLPDHIPENPESPAERWRVSASWIVDLEQYNEWMAEEDYEVDEQGKKKTHKQRMSIDDIMSFGDEKKKPAASSGGGKQKRRRSPSPASSASTSKPGKRKRSPAVVHKKSRNDDDDEDLTRDLDDPPAEPNVQEVHKANAALQSTASPAPGGKSRGDNDMMPIKGGTMTDLDDEMTGGSAAQAMSTGDGENSQTGKTSDNSNTQEFSSSAKEDMEDNVTEQTHHIIVPSYSAWFDYNSIHVIEKRAMPEFFNSKNKSKTPEIYMAYRNFMIDTYRLNPTEYLTSTACRRNLAGDVCAIMRVHAFLEQWGLINYQIDADVRPTPMGPPPTSHFHILSDTPSGLQSINPQKTQQPSAAKTLLDLDKKPLGKDGGLELGDKSGLTGIKTEALENGAAGGLSSGVSQFGLKLDQYAKKPAAMRNRTAASMAREWTDQETLLLLEGLEMHKDDWNKVCEHVGSRTQDECILHFLRLPIEDPYLEDDGGFLGPLACQPIPFSKSGNPIMSTVAFLASVVDPRVAAAAAKAAMEEFAAIKDEVPATIMDNHLKNVEKASAGGKFNPNFGLANSGIAGTGNDKDDEEGKEGGASASAGGSDEEMKDLSKKDETAAAASGGEVDIKTEDSSGDGETKDGTEAKEGTGTGTGPLAVPKEGTFSENNMQTAAAAALASAAVKAKHLAALEERKIKSLVALLVETQMKKLEIKLRHFEELEATMEREREGLEYQRQQLITERQQFHLEQLKAAEFRARQQAHHRLQQELQGQAAAGSMILPQQQQLPQAQQPQQQQQTLPPHPHLAQQQQLPPHPHQLPPQSQPLAGPTAQHQPLPPHVVSSPNGAPFAAPPISLTGGLPPGAPTAIVTNPSDQTGPVAAGAAQSQAPTPMDTTPPSSGPVSDANAPPGSAMPPGGIPPANTAPIAGVAPSS
Protein: Molybdate-anion transporter (Major facilitator superfamily domain-containing protein 5) (Molybdate transporter 2 homolog) (Q9C5R0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Alpha/beta-Hydrolases superfamily protein
- At2g41640/T32G6.16
- Xyloglucan endotransglucosylase/hydrolase protein 31
- Autophagy-related protein 9
Sequence:
MEIFYYLVFGVLGLVVAALELSKNNKDRINTSSAFNSFKNNYLLVYSLMMAGDWLQGPYVYYLYSTYGFGKGDIGQLFIAGFGSSMLFGTIVGSLADKQGRKRACVTYCITYILSCITKHSPQYKVLMVGRVLGGIATSLLFSSFESWLVAEHNKRGFEQQWLSVTFSKAVFFGNGLVAIIAGLFGNLLVDTFSLGPVAPFDAAACFLTIGMAVILSSWTENYGDPSENKDLLTQFRGAAVAIASDEKIALLGAIQSLFEGSMYTFVFLWTPALSPNDEEIPHGFIFATFMLASMLGSSLASRLLSRSTPKVESYMQIVFLVSGAALLLPILMTLFIAPSKVKGGGISFSGCFQLLGFCIFEACVGLFWPSIMKMRSQYIPEEARSTIMNFFRIPLNIFVCVVLYNVNAFPITVMFGMCSIFLFVASLLQRRLMMIVDKPKTNDWTPLEERNTEEDPLNI
Protein: Myosin phosphatase DMBS-S (Q86R99)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSLDARNNSAMMKRAEQLKRWEESDTNRAAPTPRHEHGRRIKFSSGCVFLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLAIDVQHMAMIDYMEKMVQELNINVDEARKAEELAMLNDAKKWLRSDAAEVDRPHPKTGATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVADRKIVKFLEELRANKRNKRRPSSQIRISDAMENHVEKTPTKLVRVEVRTDATKDAENVKPNQQIHAVEHPVEEEAPWRRKLPRTPSDSPTNNQVPDRELGTNSSETANDVILRRTQSFENDQKKPTVTIATPTSTAATAINSPSTTVQTPPIRRSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEELVKKKNMGMANNNNNNNISTTTTNTISNSGFKLEDITSGGTYPPNNSTIIPSAPAVMAAANLSTTTGVQRRISSGPIALNASNQSLNSVGRPVSAPSEGTNNSAYVTPSARKFETNATSTGATTAATTTSNSTSNSVSATSANHTTATAPNATSNHDDKDNDKENDNRTQTVIQRRRKPKRRSTGVVHIDMDELDPERQNESSNNDNEEKEKESGSERTSRSRLGSTASTATTSESKSSSSNDKTENGDGIDYKALWEAEKLENDKLRQMLKQKDDEAVQTRATLERFANAQLDAYKSDNHRLKEENAALIRVISKLSK
Protein: Ras-related protein Rab-37 (EC 3.6.5.2) (Q96AX2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9JKM7}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9JKM7}. Note=Secretory granules. Located mainly in the connecting cilia between the outer segment and inner segment and also observed in the outer plexiform layer, inner plexiform layer, and ganglion cell layer of the retinas. {ECO:0000250|UniProtKB:Q9JKM7}.
Interaction partners:
Sequence:
MTGTPGAVATRDGEAPERSPPCSPSYDLTGKVMLLGDTGVGKTCFLIQFKDGAFLSGTFIATVGIDFRNKVVTVDGVRVKLQIWDTAGQERFRSVTHAYYRDAQALLLLYDITNKSSFDNIRAWLTEIHEYAQRDVVIMLLGNKADMSSERVIRSEDGETLAREYGVPFLETSAKTGMNVELAFLAIAKELKYRAGHQADEPSFQIRDYVESQKKRSSCCSFM
Protein: Uncharacterized kinase C3H5.11 (EC 2.7.1.-) (Q6LA56)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- Putative glutamine-dependent NAD
- NAD-dependent histone deacetylase sir2
- NAD-dependent protein deacetylase hst4
- Uncharacterized kinase C24B10.02c
- NAD-dependent protein deacetylase hst2
- NAD-capped RNA hydrolase
- Putative nicotinamide mononucleotide adenylyltransferase
Sequence:
MAEFDDSCLPTNPTTENDYHGSFPYCSVHAQLYPYVSDCMVMHRKAPINEQEALRDVVWETRTINKKLHVTPIKPNITSILLVSKPGDEEVEEKLKEFVYWLISLDNITVFIQKSMEDLFEKTEKIQYWTTLLCTKHSQLFDLVLTLGGDGTVLYTSRLFQRTVPPIMPFAMGTLGFLTHFDVKKYKTSILEICNEMYVHLRTRFECRVMKKKNRTQWINIDEHLSQSLHATDTETHTFTDSLVVLNEVVIDRGPNTAMSDIMLYVDSKYLTTVKADGLCISTPTGSTAYSLAAGGSLCHPDISVMIVSPICAHSLSLRPIHVPDSMALHVVIPQDAQQSSWISFDGRNRTELLPGDYLTVRISRYPFPTVHSTEEDADWFESIKRTLMWNQN