wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/arginine repetitive matrix protein 1 (Plenty-of-prolines 101) (Q52KI8)
Organism: Mus musculus (Mouse)
Function: Part of pre- and post-splicing multiprotein mRNP complexes. Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by bridging together sequence-specific (SR family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA 3'-end cleavage independently of the formation of an exon junction complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with low sequence specificity and has similar preference for either double- or single-stranded nucleic acid substrates.
Subcellular location: Nucleus matrix {ECO:0000255|PROSITE-ProRule:PRU00627}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00627}.
Interaction partners:
- Serine/arginine repetitive matrix protein 2
- RNA-binding protein 25
- RNA-binding protein with serine-rich domain 1
- Regulator of nonsense transcripts 2
- Spliceosome RNA helicase Ddx39b
- Regulator of nonsense transcripts 1
- Transcription elongation regulator 1
- UPF3 regulator of nonsense transcripts homolog B
- WW domain-binding protein 11
- Pre-mRNA-splicing factor 38A
Sequence:
MDAGFFRGTSAEQDNRFSNKQKKLLKQLKFAECLEKKVDMSKVNLEVIKPWITKRVTEILGFEDDVVIEFIFNQLEVKNPDSKMMQINLTGFLNGKNAREFMGELWPLLLSAQENIAGIPSAFLELKKEEIKQRQIEQEKLASLKKQDEDKDKRDKEEKESSREKRERSRSPRRRKSRSPSPRRRSSPVRRERKRSHSRSPRHRTKSRSPSPAPEKKEKSPELPEPSVRMKDSSVQEATSTSDILKAPKPEPVPEPKEPSPEKNSKKEKEKTRPRSRSRSKSRSRTRSRSPSHTRPRRRHRSRSRSYSPRRRPSPRRRPSPRRRTPPRRMPPPPRHRRSRSPGRRRRRSSASLSGSSSSSSSSRSRSPPKKPPKRTSSPPRKTRRLSPSASPPRRRHRPSSPATPPPKTRHSPTPQQSNRTRKSRVSVSPGRTSGKVTKHKGTEKRESPSPAPKPRKVELSESEEDKGSKMAAADSVQQRRQYRRQNQQSSSDSGSSSTSEDERPKRSHVKNGEVGRRRRHSPSRSASPSPRKRQKETSPRMQMGKRWQSPVTKSSRRRRSPSPPPARRRRSPSPAPPPPPPPPPPRRRRSPTPPPRRRTPSPPPRRRSPSPRRYSPPIQRRYSPSPPPKRRTASPPPPPKRRASPSPPPKRRVSHSPPPKQRSPTVTKRRSPSLSSKHRKGSSPGRSTREARSPQPNKRHSPSPRPRAPQTSSPPPVRRGASASPQGRQSPSPSTRPIRRVSRTPEPKKIKKTAMATQRNIRRVSKSPKADSLSRAASPSPQSVRRVSSSRSVSGSPEPAAKKPPAPPSPVQSQSPSTNWSPAVPAKKAKSPTPSLSPARNSDQEGGGKKKKKKKDKKHKKDKKHKKHKKHKKEKAVTIATPATAAPAAVSAATTTSAQEEPAAAPEPRKETESEAEDDNLDDLERHLREKALRSMRKAQVSPQS
Protein: Rho guanine nucleotide exchange factor 26 (D3YYY8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
- Rho-related GTP-binding protein RhoG
Sequence:
MDGESEVDFSSNGVTPLWRRRSTPPLQLLSRSKPRPQSYQSPSGLLITDFPVEELAALPTPQTPVRVPADPDDRTVSRSPQLLSAHRRPVTNGRTVSPDYRAASPRLRRPKSPLVSYAASGGSPKSTSNGTVASPAALLSRASRTPDTPASCATDEDCTGVTASKVSSPIANGLAHKTDSSGPVSQTGQPAGDLELAPSRLSPALPHKSSEQKLPLQRLPSQGNELPNPSVVLSTNSPAALKMGKQQIIPKSLASEIKLSKSNSQNVESHRRLLKVRSMVEGLGAPLGHEGEEGEVDNDMDSPGSLRRGLRSTSYRRAVVSGFDFDSPTSSKKKNRMSQPVLKAVMEDKEKFSSLGRIKKKILKGQGTFDGEENAVLYQNYKEKALDIDSDEEPEAKEQKAEERIVIHHKPLRSTWSQLSAVKRNGLSQTVSQEERKRQEAIFEVISSEHSYLLSLEILIRMFKNSKELTDTMTKTERHHLFSNITDVWEASKKFFTELEARHQNNIFIEDISDIVEKHTASTFDPYVKYCTNEVYQQRTLQKLLATNPSFKEVLSRIESHEDCRNLPMISFLILPMQRVTRLPLLMDTICQKTPKDSPKYEVCKRALKEVSKLVRLCNEGARKMERTEMMYTINSQLEFKIKPFPLVSSSRWLVKRGELTAYVEDTVLFSKRMSKQQVYFFLFNDVLIITKKKSEESYNVNDYSLRDQLLVESCDNEELNSSPGKNPSTMLYSRQSSATHLFTLTVLSNHASEKVDMLLGAETQSERARWITALGHSSGKQPPDRTTLTQVEIIRSFTAKQPDELSLQVADVVLIYQRVGDGWYEGERLRDGERGWFPMECAKEITCQATIDKNVERMGRLLGLETNV
Protein: Fimbrin-2 (AtFIM2) (Fimbrin2) (O50064)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cross-links actin filaments (F-actin). Stabilizes and prevents F-actin depolymerization mediated by profilin. May regulate actin cytoarchitecture, cell cycle, cell division, cell elongation and cytoplasmic tractus.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q7G188}.
Interaction partners:
- At5g11810
- At2g35730
- ER membrane protein, putative
- F-actin-capping protein subunit beta
- Probable protein phosphatase 2C 40
- Leucine-rich repeat receptor-like tyrosine-protein kinase PXC3
- Villin-1
- At5g47730
- Classical arabinogalactan protein 7
- Terminal EAR1-like 1
Sequence:
MSGFVGILVSDPWLQNQFTQVELRSLKSHFTSMKRESGKLTVSDLASRMGKSKVVGDQNLSNEERATLIQNFHPNLNDEVDFEFYLRIYLNLQAHVNAIIGSGVKNSSAFLKAATTTLLHTISDSEKSSYVAHINNYLSGDEFLNKCLPINPSSNDLFEVAKDGVLLCKLINVAVPGTIDERAINTKSMLNPWERNENHTLCLNSAKAIGCTVVNIGTQDIIEGRRHLVLGVISQIIKIQLLADLNLKKTPQLVELVGDSKDVEELMSLPPEKILLRWMNFQLRKTEYKKTVTNFSSDVKDAEAYTNLLNVLAPEHKNPSHLAVKSSFERAKLVLEHADKMGCRRYLTAKDIVEGSPNLNLAFVAHIFQHRNGLSTQTKQISFLENLADDIQISREEKAFRFWINSFDGSVYINNVFEDLRDGWILLQTLDKVSPGIVNWKVSSKPPIKLPFKKVENCNQVVKLGKQLKFSLVNIAGNDIVQGNKKLILAYLWQLMRYNILQLLKNLRLHSNGKEITDADILEWANAKVRNNGCKTRMYSFRDKSLSDGVFFLELLSSVQPRSVNWSLVTNGVTDEEKKMNATYVISIARKLGCSIFLLPEDIIEVNQKMMLTLTASIMYWTLKQPLHLNKPIGSPDSHNGSLLDDSTSDSSIE
Protein: BEACH domain-containing protein C1 (BEACH-domain homolog C1) (F4JD14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a negative factor in protein storage vacuole (PSV) trafficking regulation and plant effector triggered immunity (ETI). Negatively regulated upon interaction with GSF12, and also probably by BCHB. Required for ETI, but not for cell death.
Interaction partners:
Sequence:
MNGKESRGPACSFEFVGESSGLLGPGESRWPFTNGYAFATWIYIESFADTLDASTAAAAIAAASAAKSGKISNAAPANVHTGEGTAHMPRLFSFLTPDNQGIEAYFYAQFLVVESGSGKGSKTSLHFTHAFKPQCWYFIGLEHTCNQGLLGNSDSELRLYIDGSLYETRPFDYPRISKPLSFCCIGSNPPSTTAGLQRRRRQCALFAEMGPVYIFKEPIGPERMTRLATRGGDVLPCFGNGAGLPWLATNDHVRNVAEESSLSDAELGGYIHLLYHPCLLSGRFCPDASLSGAAGDEKTPYSFSAVVFALCYLVFPYFGRPMSLLPLTVSSVHKDNLEPCSRNVPSSLTTYSLAAPIFRMISFAIKHPGNNEELSRTRGPEILATVLGYLLHSLASFDIKHDRVGDEELVAAIVSLCQSQKINHALKVQLFCTLLLDLKIWSVCSYRLQKKLLSSLQDMVFTEATAMRNADAIQVLLDGCRRYFWTIQEKDSVNTFSLDGDARQVGEVNALVDELLVIIELLMGAASPSFAADDLHRLLGFIIESPQPNQVARVLHLMFRLVVQPNAAKAQTFAEAFITSGGIETLLVLIANRVNTMGLETESFQQVKVHGSETVICETGSVTLSSSVNADRISSVSETPFNNNARNNVDDRDRVMVGIIRLIGALISKGHLKFSVGAKSDVMSNLMGSEFRENGGTMFDYKVALLLFALLKAFQAAPNRLMTDNVYTTLLGASVNASSTEDGLNFCDLGHRFEHPQLLLILLRSLPFASKALQNRALQDILFLACTHPEKRSSLTKMEEWPEWILEILISNYEKDAGKQSASPGSAEEEDLIHNFLIIMLEHSMRQKDGWKDIEATIHCAEWLTFVGGSSTGEKRIRREESLPIFKRRLLGGLLDFAASELQAQTQVIAAASAGFAAESLTPKDAKAGVENAALLSVFLVENTVVILMLVEDHLRLQSKQNCAASAVDVSPSPLSLVYPPNYRSHTLPTVGESSEVSSSCASVSSDSGGVHLDILASMADASGQISTAVMERLAAAAAAEPYESVSCAFVSYGSCTRDLADAWKYRSRLWYGVGLPSKTSCFGGGGSGWDSWKHALQKDAQGNWIELPLVKKSVSMLQALLLDESGLGGGLGIGGGSGTGMGGMSGLYQLLDSDQPFLCMLRMVLLSLREEDHGEDSLLMKNLSSEDGITGGLQCPLGNSASVDISSQLSMRQSPSALLWSVLSPVLNMPISDSKRQRVLVTTCVLYSEVWNAVSKDKRPLRKQYLEAILPPFVAILRRWRPLLAGIHELSTGDGVNPLVVDTRALAADALPIEAALSMISPEWAAAFASPPSAMALAMIAAGAAGWEAPAHPAPPAPPPLRRDSSLLERKSTKLQTFSSFQKPLEAPNDDTPGRARDKAAANIDSHLLIQPLTRLTGVFWKLDSMESSSRMRQCLRRNYSGTGHLETTRNYGDQTYLMNNHDSPVLAVEAISKEIMYEDDEHGDADDLEIEGNVGERKGENEERRSGSLEDAITLSTGINDHRPLSEQNMVQNSTEVKDLSELKERIVLEISSTMVRPLGVVKGTFQITTRRINFIVDIREDQHLDEKSDGSKSRDEERDRSWLMSSLHQIYSRRYLLKKSALELFMVDRSNFFFDFGNTEGRRNACRAIVQARPPHLKNIYSATQPEQVSRRTQLMERWARWEISNFEYLMQLNTLAGRSYNDITQYPIFPWILCDYVSEILDLSNPSNYRDLSKVPIGALNPERLKKFQEKHSSFEDPVIPKFHYGSHYSSAGAVLHYLARVEPFTTLSIQLQGRKFDRADQIFSDIAATWKGVLQDMNNVKELNTTDPNTHMVSSFSNPTTSETEPDSDMNIVSTPSNATTNQIDTESSEAANYENSNSSIKTSKNTSKITKLTPTSKRSLTSSKDNAAQKSSTKPKLLSKAEIIKVDVYSYIMSL
Protein: Larval cuticle protein 1 (Larval cuticle protein I) (P02839)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the larval cuticle.
Interaction partners:
Sequence:
MFKFVMICAVLGLAVANPPVPHSLGRSEDVHADVLSQSDDVRADGFDSSLHTSNGIEQAASGDAHGNIHGNFGWISPEGEHVEVKYVANENGYQPSGAWIPTPPPIPEAIARAVAWLESHPPAPEHPRHH
Protein: High-affinity nitrate transporter 2.1 (OsNRT2.1) (P0DKG9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in nitrate transport, but does not seem to be able to mediate transport by its own. Acts as a dual component transporter with NAR2.1. Imports nitrate with high affinity when expressed with NAR2.1 in a heterologous system (Xenopus oocytes).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- High-affinity nitrate transporter-activating protein 2.1
- Nitrate reductase 1
- Nitrate reductase
- Nitrate reductase
- Os02g0765900 protein
- Ferredoxin--nitrite reductase, chloroplastic
- Os11g0242400 protein
- Probable high-affinity nitrate transporter 2.4
- High-affinity nitrate transporter 2.3
- Plastocyanin
Sequence:
MDSSTVGAPGSSLHGVTGREPAFAFSTEVGGEDAAAASKFDLPVDSEHKAKTIRLLSFANPHMRTFHLSWISFFSCFVSTFAAAPLVPIIRDNLNLTKADIGNAGVASVSGSIFSRLAMGAICDMLGPRYGCAFLIMLAAPTVFCMSLIDSAAGYIAVRFLIGFSLATFVSCQYWMSTMFNSKIIGLVNGLAAGWGNMGGGATQLIMPLVYDVIRKCGATPFTAWRLAYFVPGTLHVVMGVLVLTLGQDLPDGNLRSLQKKGDVNRDSFSRVLWYAVTNYRTWIFVLLYGYSMGVELTTDNVIAEYFYDRFDLDLRVAGIIAASFGMANIVARPTGGLLSDLGARYFGMRARLWNIWILQTAGGAFCLLLGRASTLPTSVVCMVLFSFCAQAACGAIFGVIPFVSRRSLGIISGMTGAGGNFGAGLTQLLFFTSSRYSTGTGLEYMGIMIMACTLPVVLVHFPQWGSMFLPPNAGAEEEHYYGSEWSEQEKSKGLHGASLKFAENSRSERGRRNVINAAAAAATPPNNSPEHA
Protein: Eukaryotic translation elongation factor 1 epsilon-1 (Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3) (Elongation factor p18) (Multisynthase complex auxiliary component p18) (O43324)
Organism: Homo sapiens (Human)
Function: Positive modulator of ATM response to DNA damage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15680327}. Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}. Nucleus {ECO:0000269|PubMed:15680327}. Note=Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes (S phase) and following DNA damage.
Interaction partners:
- Aspartate--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Bifunctional glutamate/proline--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Glutamine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, cytoplasmic
Sequence:
MAAAAELSLLEKSLGLSKGNKYSAQGERQIPVLQTNNGPSLTGLTTIAAHLVKQANKEYLLGSTAEEKAIVQQWLEYRVTQVDGHSSKNDIHTLLKDLNSYLEDKVYLTGYNFTLADILLYYGLHRFIVDLTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRLYTNSH
Protein: Thymine DNA glycosylase (B4E127)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIERNMDVQEVQYTFDLQLAQEDAKKMAVKEEKYDPGYEAAYGGAYGENPCSSEPCGFSSNGLIESVELRGESAFSGIPNGQWMTQSFTDQIPSFSNHCGTQEQEEESHA
Protein: AarF domain-containing protein kinase 1 (EC 2.7.-.-) (Q9D0L4)
Organism: Mus musculus (Mouse)
Function: Appears to be essential for maintaining mitochondrial cristae formation and mitochondrial function by acting via YME1L1 in a kinase-independent manner to regulate essential mitochondrial structural proteins OPA1 and IMMT (By similarity). The action of this enzyme is not yet clear. It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr) (Probable).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q86TW2}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
Sequence:
MARKALKLASWTSVALAASGVYLYSNNYLDPNDFGAVRVGRAVATTAVISYDYLTSLRSVPYGSEEYLQRRSQVHLRSARRLFELCCANRGTFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEVRQVIREDLGKEIHDLFLSFDDTPLGAASLAQVHKAVLHDGRTVAVKVQHPKVQAQSSKDILLMEVLVLAVKQLFPDFEFMWLVDEAKKNLPLELDFLNEGRNAEKVAHMLRHFDFLKVPQIHWELSTKRVLLMEFVEGGQVNDRAYMEKNQIDVNEISCHLGKMYSEMIFVNGFVHCDPHPGNVLVRKRPDTGKAEIVLLDHGLYQVLTEEFRLDYCHLWQSLIWTDMDGLKQYSQRLGAADLYPLFACMLTARSWDSVKQGIGQAPVSATEDSEIRNNAACYLPEISQLLNHVPRQMLLILKTNDLLRSIETTLGTRSSASSFLNMSRCCIRALAEHKKRDAGSFFRRTQISFSEAFSLWQINLHELLLRVRALRLACWVSALLGWLTRAPHRM
Protein: Aconitate hydratase, mitochondrial (Aconitase) (EC 4.2.1.3) (Q8T4D6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|RuleBase:RU362107}.
Interaction partners:
- Isocitrate dehydrogenase
- Citrate synthase
- Probable citrate synthase, mitochondrial
- ATP-citrate synthase
- isocitrate dehydrogenase
- 2-oxoglutarate dehydrogenase, mitochondrial
- Probable isocitrate dehydrogenase subunit alpha, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Malate dehydrogenase
- Superoxide dismutase, mitochondrial
Sequence:
MAQRTHRYICLAGSMVRNFHTARFPRCDKVAMSNFDTGIPLPYKKLRENLDCIKGRLGGPLTLSEKVLYSHLDQPDSQEIERGKSYLRLRPDRVALQDATAQMTLLQFISSGLKKVAVPSTVHCDHLIEAQISGDKDLARAKDLNKEVYDFLSSACAKYNLGFWKPGSGIIHQIILENYAFPGLLMIGTDSHTPNGGGLGCLCVGVGGADAVDVMANIPWELKCPTVIGCHLTGKISGWTSPKDVILKVAEILTVKGGTGAIVEYHGPGVESISCTGMATITNMGAEIGATTSIFPFNERMVTYLRATGRGAIADEATKNKDLLVPDEGCKYDKVIEINLDTLEPLVNGPFTPDLAHPISKLGQNSEKNGYPMEIKVSLIGSCTNSSYEDMGRCASIANDALGHGLKSCVPFNVTPGSEQVRATIARDGIIDVLEKFGGTVLANACGPCIGQWDRKDVKMGEKNTIVTSYNRNFTGRNDANPATHCFVTSPEMATALAIAGRLDFNPMTDELTGTDGKTFKLKEPHGEELPSKGFDPGEDTYQAPPAKADDIKVNVDPKSDRLQLLEPFEKWDGKDYIDLMVLIKIKGKCTTDHISAAGPWLKYRGHLDNISNNMFIGATNAENNEMNKVKNQKTGSFDAVPAVARDYKANKIKWCAVGEENYGEGSSREHAALEPRHLGGVAIIVKSFARIHETNLKKQGMLALTFANPGDYDKVQPSSKISILNLKDLAPGKPVDAEIKNNGSSDKIQLNHTLNELQIQWFQAGSALNLMKELAAKGGDKK
Protein: Transcriptional elongation regulator MINIYO (Q8GYU3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Positive regulator of transcriptional elongation that is essential for cells to initiate differentiation. Interacts with RNA polymerase II and the Elongator complex and is required to sustain global levels of transcriptional elongation activity, specifically in differentiating tissues.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21620701}. Nucleus {ECO:0000269|PubMed:21620701}. Note=Cytoplasmic in undifferentiated cells (meristem core) and nuclear in differentiating cells. {ECO:0000269|PubMed:21620701}.
Interaction partners:
- GPN-loop GTPase QQT1
- GPN-loop GTPase QQT2
- DNA-directed RNA polymerases II, IV and V subunit 3
- GPN-loop GTPase 3
- Putative U3 small nucleolar ribonucleoprotein
Sequence:
MEQSSGRVNPEQPNNVLASLVGSIVEKGISENKPPSKPLPPRPSLLSFPVARHRSHGPHLAPVGSSIAQPKDYNDDQEEEEAEERFMNADSIAAFAKPLQRKEKKDMDLGRWKDMVSGDDPASTHVPQQSRKLKIIETRPPYVASADAATTSSNTLLAARASDQREFVSDKAPFIKNLGTKERVPLNASPPLAVSNGLGTRHASSSLESDIDVENHAKLQTMSPDEIAEAQAELLDKMDPALLSILKKRGEAKLKKRKHSVQGVSITDETAKNSRTEGHFVTPKVMAIPKEKSVVQKPGIAQGFVWDAWTERVEAARDLRFSFDGNVVEEDVVSPAETGGKWSGVESAAERDFLRTEGDPGAAGYTIKEAIALARSVIPGQRCLALHLLASVLDKALNKLCQSRIGYAREEKDKSTDWEAIWAYALGPEPELVLALRMALDDNHASVVIACVKVIQCLLSCSLNENFFNILENMGPHGKDIFTASVFRSKPEIDLGFLRGCYWKYSAKPSNIVAFREEILDDGTEDTDTIQKDVFVAGQDVAAGLVRMDILPRIYHLLETEPTAALEDSIISVTIAIARHSPKCTTAILKYPKFVQTIVKRFQLNKRMDVLSSQINSVRLLKVLARYDQSTCMEFVKNGTFNAVTWHLFQFTSSLDSWVKLGKQNCKLSSTLMVEQLRFWKVCIHSGCCVSRFPELFPALCLWLSCPSFEKLREKNLISEFTSVSNEAYLVLEAFAETLPNMYSQNIPRNESGTWDWSYVSPMIDSALSWITLAPQLLKWEKGIESVSVSTTTLLWLYSGVMRTISKVLEKISAEGEEEPLPWLPEFVPKIGLAIIKHKLLSFSVADVSRFGKDSSRCSSFMEYLCFLRERSQDDELALASVNCLHGLTRTIVSIQNLIESARSKMKAPHQVSISTGDESVLANGILAESLAELTSVSCSFRDSVSSEWPIVQSIELHKRGGLAPGVGLGWGASGGGFWSTRVLLAQAGAGLLSLFLNISLSDSQNDQGSVGFMDKVNSALAMCLIAGPRDYLLVERAFEYVLRPHALEHLACCIKSNKKNISFEWECSEGDYHRMSSMLASHFRHRWLQQKGRSIAEEGVSGVRKGTVGLETIHEDGEMSNSSTQDKKSDSSTIEWAHQRMPLPPHWFLSAISAVHSGKTSTGPPESTELLEVAKAGVFFLAGLESSSGFGSLPSPVVSVPLVWKFHALSTVLLVGMDIIEDKNTRNLYNYLQELYGQFLDEARLNHRDTELLRFKSDIHENYSTFLEMVVEQYAAVSYGDVVYGRQVSVYLHQCVEHSVRLSAWTVLSNARVLELLPSLDKCLGEADGYLEPVEENEAVLEAYLKSWTCGALDRAATRGSVAYTLVVHHFSSLVFCNQAKDKVSLRNKIVKTLVRDLSRKRHREGMMLDLLRYKKGSANAMEEEVIAAETEKRMEVLKEGCEGNSTLLLELEKLKSAALCGRR
Protein: Inner kinetochore subunit mhf2 (CENP-X homolog) (Constitutive centromere-associated network protein mhf2) (MHF histone-fold complex subunit 2) (O74896)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of a FANCM-MHF complex that promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork (Probable). FANCM-MHF promotes non-crossover recombination.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Inner kinetochore subunit mhf1
- Inner kinetochore subunit cnp20
- ATP-dependent DNA helicase fml1
- Histone H3-like centromeric protein cnp1
- Inner kinetochore subunit wip1
- Inner kinetochore subunit fta1
- Replication factor A protein 3
- Uncharacterized protein C16C6.03c
Sequence:
MEQESELLSLNTLARILTLYFSSEKGTKITPSALELITQYLRIYSKEAVCRAYEEKKNSIMSSSENEDIVLELEDLENGIAAQLALDFS
Protein: Nucleolar and spindle-associated protein 1 (NuSAP) (A1L2F3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Microtubule-associated protein with the capacity to bundle and stabilize microtubules. May associate with chromosomes and promote the organization of mitotic spindle microtubules around them (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Associates with mitotic spindle microtubules, particularly in the vicinity of chromosomes. {ECO:0000250}.
Interaction partners:
- Kinesin family member 11
- Discs, large
- Borealin
- BUB1 mitotic checkpoint serine/threonine kinase
- Protein regulator of cytokinesis 1b.
- Lymphokine-activated killer T-cell-originated protein kinase homolog
- Ubiquitin-conjugating enzyme E2 C
- Kinetochore protein NDC80 homolog
- TPX2 microtubule nucleation factor
- Cell division cycle 20 homolog
Sequence:
MDLDSLKYAELQRLAKEVGLKANMKAERLLKALKEHFSQQQLSENGNDAAASDAHDSVPPVDAHAATYVTERRGKGRTAKRKLSEPTPIISPTEEKTPQDEGRRGSKRRKVSSAKDTQTPVPAEAFAKENTMEKESGDLNPDSESGPTETGVKGRRTVGKIPRHKGLMKRKPAMRPTTPNFKKLHEAHFKKMESIDSYVQRKNKQMEVLRNSVKELKTLSEKTLKKPEAKAQTKVPSSRASLFSPAVQKTAVPERRRLTQQPVSKSALKDTATFRPTVLTTNKINVRFSQATQDNEYKRSLVKTPARMSPHMPLTSTPGRKSDVRSKAELNRSASTITKTPGATPFVFNGNNSISTTPGTTKKNTFDLKASLSRPLTYKPHKGKLKPFGDAQENTALNKSQTVPSHQKNYKQHQVQTREERRVKHTEDRKQKKEKMLGARRGLVMA
Protein: Quinic acid utilization activator (P10563)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Transcription activation of genes for enzymes and proteins of quinate metabolism by binding to a 16 base-pair sequence (consensus 5'-GGATAANNNNTTATCC-3') in front of each qut gene.
Subcellular location: Nucleus.
Interaction partners:
- Quinate repressor protein
- Quinate dehydrogenase
- Pentafunctional AROM polypeptide
- Quinate permease
Sequence:
MSSDTRQTSGGNARSKRRLTDAVDEDGRPTATAEDPTSNPKRQRVSRACDSCRSKKDKCDGAQPICSTCASLSRPCTYRANPKKRGLPTGYIRTLELLWGLVFNKIQGSEEVVRTLLRAANIPSHLATMGKESEGSDTLLSSWKNSIVLKEIERLLTFLEQPEGDQERSARGEIDSPADAEESSVLSPETLEWQLPDSIAVASQSPLASGPSPVRLPRPSTTRLVRDSGTQTIPLGEIEDLTTNGSSHDRPVIASNSAREEHRLPPNPWPLLDIYFSYTQCWFPILEKHDILRTAFRQGDDDQYNSPSAAGDNAALWAVLALASIQQTSISTTRQLSDLPEDRPDPDQLYAKARSLIPTESGTYQLGHIQALLILSLIKLGQQDCAAAWMLVGQAVRSAQSLGLNDPSDATGVEKTAGRSKHVFLGCFVLETLVAAKLGLLPSLRKTDLTKVGLINEDGLEEWHPWEDQTGLRPIESSRSFQRGPLHALSTFNRLLSLMCILNELCCVRQTPANSMSYLGTLERQLQLWVSALPTSYRIDLQTVSTKPASPHIFGLEMMYEAVATAISLQLAVQKNERNGLRRASEGSKRLVSLLQAYMETYSLSATCPTFGIALTLGLPLPCMKKTAPWAFEASHGINHKLQSFSAHLATVWIHNTGSQRRPRHATQQGTHPRSPMAISLPGNNMRLTNLIEESRTGNLSTTDSYLSPTWMRTSNDENAVLSLPTPASSLNIASGVETNPTSQQITHQHRSSVVGKPNSALIMSDLTTPFPASGHHYQQTYDDASLHFNSLADIESTSSAQRPRIAPDLDALFDELASLDGTDR
Protein: APOBEC1 complementation factor (APOBEC1-stimulating protein) (Q923K9)
Organism: Rattus norvegicus (Rat)
Function: Essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. The complex also seems to protect the edited APOB mRNA from nonsense-mediated decay (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11870221}. Endoplasmic reticulum {ECO:0000269|PubMed:11870221}. Cytoplasm {ECO:0000269|PubMed:11870221}. Note=Predominantly nuclear where it localizes to heterochromatin. Also cytoplasmic where it is found at the outer surface of the endoplasmic reticulum. Shuttles between the nucleus and cytoplasm. May be transported into the nucleus by the nuclear import protein TNPO2/TRN2 or by APOBEC1.
Interaction partners:
- C->U-editing enzyme APOBEC-1
- Putative C->U-editing enzyme APOBEC-4
- Apolipoprotein B-100
- Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2.
- Cytidine deaminase
- Vir like m6A methyltransferase associated
- RNA-binding protein 15
- Similar to KIAA1627 protein
- Putative RNA-binding protein 15B
- mRNA m
Sequence:
MESNHKSGDGLSGTQKEAALRALVQRTGYSLVQENGQRKYGGPPPGWDTTPPERGCEIFIGKLPRDLFEDELIPLCEKIGKIYEMRMMMDFNGNNRGYAFVTFSNKQEAKNAIKQLNNYEIRNGRLLGVCASVDNCRLFVGGIPKTKKREEILSEMKKVTEGVVDVIVYPSAADKTKNRGFAFVEYESHRAAAMARRRLLPGRIQLWGHPIAVDWAEPEVEVDEDTMSSVKILYVRNLMLSTSEEMIEKEFNSIKPGAVERVKKIRDYAFVHFSNREDAVEAMKALNGKVLDGSPIEVTLAKPVDKDSYVRYTRGTGGRNTMLQEYTYPLSHVYDPTTTYLGAPVFYTPQAYAAIPSLHFPATKGHLSNRALIRTPSVREIYMNVPVGAAGVRGLGGRGYLAYTGLGRGYQVKGDKRQDKLYDLLPGMELTPMNTISLKPQGVKLAPQILEEICQKNNWGQPVYQLHSAIGQDQRQLFLYKVTIPALASQNPAIHPFTPPKLSAYVDEAKRYAAEHTLQTLGIPTEGGDAGTTAPTATSATVFPGYAVPSATAPVSTAQLKQAVTLGQDLAAYTTYEVYPTFAVTTRGDGYGTF
Protein: Transmembrane protein 59-like (Brain-specific membrane-anchored protein) (Q7TNI2)
Organism: Mus musculus (Mouse)
Function: Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of APP. Inhibits APP transport to the cell surface and further shedding (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Mitochondrial disaggregase
Sequence:
MAAVALPLLLLLASLVTPTPARDPFAPQLGDTQRCQQRCRQHHPGSPPAQPEPEGPSESPNNKAILISACERGCRLFSICRFVAKSSRPNATETECEAACTEAYVKAAEQRACSEGCWGQIPEPETQLEQKDLALDPPRGRLSLRYLFSMLCSDLMSSAQGFLSSSWTYSLQTDNRKVVVFQTQPVAENFAFQGSHLQRVEVTWRRSHPKALELHMDPVGPLDKVRKAKPRVKTSKAKVESEDQQESDFLSCMSRRSGLPRWVLFCCLFLSILIMLWLSCCTLVTTPGQHLKFQPLTAEQHKGLLVESDWPLYPPLPPPAYEDSTPPYKLKLDLTTL
Protein: ST13 protein (Q3KNR6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDPRKVNELRAFVKMCKQDPSVLHTEEMRFLREWVESMGGKVPPATQKAKSEENTKEEKPDSKKVEEDLKADEPSSEESDLEIDKEGVIEPDTDAPQEMGDENAEITEEMMDQANDKKVAAIEALNDGELQKAIDLFTDAIKLNPRLAILYAKRASVFVKLQKPNAAIRDCDRAIEINPDSAQPYKWRGKAHRLLGHWEEAAHDLALAWTQ
Protein: Multiplexin, isoform G (E1JID9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRVLQGVMFALAMICTLLVPVLGSFELVGQSIKDALAEYTLTDIMNNNQFAGIEFGEAEDGFPAFRFLQTADVKSPYRMLLPEKLYEFAILITFRQSSLKGGYLFSVVNPLDTVVQLGVHLSPVVKNSYNVSLVYTQADQNIGRKLASFGVAHVPDKWNSIALQVLSDKVSFYYDCELRNTTLVTREPIELVFDSASTLYIGQAGSIIGGKFEGYLEKINVYGNPDAINVTCMPPPKATIAPTTADDGSIFYEGSGENILFEDSTEANILSDDFWNTGDEATDIFDASGMQPPGQTQYTHERPYRGIKGEKGERGPKGDSIRGPPGPPGPPGPKGETAPYPPFVETTSAGAKYTGECTCNASDILEAIKDNESLRESLRGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGLPGVMGPPGPPGPPGLPENYDINWNPTRTFKESLMVNSMGAFRGTTQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPGGLDGLASANGTKGEKGEKGEKGMRGRRGGTGATGPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSGGREGLKGDKGDRGQDGRDGLPGPPGLPSTGGGDGDSGGVQYIPMPGPPGPPGPPGLPGLSISGPKGEPGVDSRSSFFGDASYYGRPEPPRQPGHSHKHEETLGLVDGEEPYFSASSSNMNMKIVPGAVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVPIATPAPPTTVAPSMRFDLQSKNLLNSPPPLLNTPTWYPRMLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRDLPVVNTRGDVLFNSWKGIFNGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDSKLIILCVEALSQDRKRKKREIGDGSSHGESESREFKTADEYAAHLENLLL
Protein: Ankyrin repeat domain-containing protein 37 (Low-density lipoprotein receptor-related protein 2-binding protein) (hLrp2bp) (Q7Z713)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:15809689}. Cytoplasm {ECO:0000269|PubMed:15809689}.
Interaction partners:
- Protein fem-1 homolog B
Sequence:
MLLLDCNPEVDGLKHLLETGASVNAPPDPCKQSPVHLAAGSGLACFLLWQLQTGADLNQQDVLGEAPLHKAAKVGSLECLSLLVASDAQIDLCNKNGQTAEDLAWSCGFPDCAKFLTTIKCMQTIKASEHPDRNDCVAVLRQKRSLGSVENTSGKRKC