wanglab/gogpt-training-data huggingface dataset:
Protein: RNA-binding protein RMD9, mitochondrial (Dodecamer binding protein) (DBP) (Required for meiotic nuclear division protein 9) (P53140)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds the RNA motif 5'-AAUAA[U/C]AUUCUU-3' in the 3'-UTR of mitochondrial mRNAs. Involved in the processing or stability of mitochondrial mRNAs.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10441495, ECO:0000269|PubMed:10905425, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:17194786, ECO:0000269|PubMed:17194787}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:17194786, ECO:0000269|PubMed:17194787}; Matrix side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:17194786, ECO:0000269|PubMed:17194787}.
Interaction partners:
- ATPase expression protein 3
- Small ribosomal subunit protein mS46
- Mitochondrial COX1 translation regulator PET309
- Mitochondrial translation factor ATP22
- mRNA-binding protein PUF3
- Protein PET111
Sequence:
MMLRRNAVRSLKTMEISVSNVVNSGSIAMLRGKLANVVLSDRTYHSSPIFHKNVPKGVLDKKNGREQRKTEQNVFNVDPASPWRHELLSFDECVSSALKYSTTPLQNTYKRIGNNQLNKNPSFAMFWDSMGRAMELYYSLRESPDFNAYRVSRLIHLLHNGLRSTRDQLVKLSRKPDYDSQSFHKEMMNFLCNSLKDISDDILIGKVSVSGYGATHLLTSFKELSFDDDCIRIWEASKNLSDETTSQAFQEPKVVGFMLPLLYAKTRSLTEPNELYNQIIQSKEFIHPNLYSGLIKVFIKAEDYEKALSLFGQLCEKAEVRNYGYLIETHLSFIGDSKNLTLAESFFDKIINDEMPYKIILQVSTVNSFLQNIWKAQNDFDHVYRIWEKAVKFYGNTVNPGILSSLNNTFFTIFFENYINDNINGFRKLQEIITFYSGVKKIDEPFFNVMLTRASIWHERSIIDFIDKNYTLYHIPRTIISYRILLKSLGSIDNTNNEEILDRWLELVKKLNELGQQYIANADLSALRDATVVWSQSKRDEKVFSAKAKGTPATTTTTEDDIKVPKPLENLKNEDSTSNSEDRIELYLKILKRYTPYFRATKQVYRYTTGCAESYPILNEYLSGYSDLSAEDIPVPQLHSFIAKEQ
Protein: Brivido-2, isoform B (M9PFT4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNLSSISRKDLTCFGVTTCVVMVCFVLVSIFSGFMHEPQRFKTMLSIDYATWPQEDPPYRAEEGGPTMDHIGYLKIRLRSLRSELLISEGHTNEMLNQKYKHIAGDLLLYGSYFIALMLMVVLQEDHTNYYNTNNMQRLFWDNTSVTFGLSQVYFIYQVHSYMKITLVEAFYAQKTNGYEGWWAMEQWQKIGVVRLRQMRPVDCHIGLGKPEWDKKTYAPEWRLPYHRMHYTEKFWRIYDPFVPAEFEPSFLNGLLLNYDHYGYLLNYPEVAGYVVLMMSTKINCLKQIEYLRDYSWLDKNTSALFIDLTMYNADANLFTLITLRVENSPFGIQLPRVHVDSVSMLGNVETRSNSELLILFVYTVLVILFARGVFTKIWHHPAAAHEAWTMVDLAIYILNVFLTVLAIMRDIETDALLQIIETATKGQYLDFQRPLRLHQMLFIVKGFLVCITTLRLWKVLQFASVFQHFTQTLFSAWRAVASLGVIILVVLMAIGITLAVPNGNNAVVFSHMVQSVVTCMWYSMGFNGDIHPADFFHGGRILGILLYLALVFLLAIILMNVFASVIYDYFNETSRILKEHSNRSSITFLEFLHVEYADLFGDAFRCLRKTYESRGHTVAENVELELNRRELIKFKRDLIKSPQELKRALLTEEQRSADYRLRGEKLFKLMAILNLQVEILERMVLGDKDGKLPTPPASDSDPDDMPEMYRKRR
Protein: Glutenin, high molecular weight subunit DX5 (P10388)
Organism: Triticum aestivum (Wheat)
Function: Glutenins are high-molecular weight seed storage proteins of wheat endosperm. Thought to be responsible for the visco-elastic property of wheat dough.
Interaction partners:
- Cyclin-dependent kinase E-1
- Cyclin-dependent kinase E-1
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 23
- Mediator complex subunit 23
- Mediator complex subunit 23
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 31
- Uncharacterized protein
Sequence:
MAKRLVLFVAVVVALVALTVAEGEASEQLQCERELQELQERELKACQQVMDQQLRDISPECHPVVVSPVAGQYEQQIVVPPKGGSFYPGETTPPQQLQQRIFWGIPALLKRYYPSVTCPQQVSYYPGQASPQRPGQGQQPGQGQQGYYPTSPQQPGQWQQPEQGQPRYYPTSPQQSGQLQQPAQGQQPGQGQQGQQPGQGQPGYYPTSSQLQPGQLQQPAQGQQGQQPGQAQQGQQPGQGQQPGQGQQGQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPAQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQSQQPGQGQQGQQVGQGQQAQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYLTSPQQSGQGQQPGQLQQSAQGQKGQQPGQGQQPGQGQQGQQPGQGQQGQQPGQGQPGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSPLQPGQGQPGYDPTSPQQPGQGQQPGQLQQPAQGQQGQQLAQGQQGQQPAQVQQGQRPAQGQQGQQPGQGQQGQQLGQGQQGQQPGQGQQGQQPAQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPWYYPTSPQESGQGQQPGQWQQPGQGQPGYYLTSPLQLGQGQQGYYPTSLQQPGQGQQPGQWQQSGQGQHWYYPTSPQLSGQGQRPGQWLQPGQGQQGYYPTSPQQPGQGQQLGQWLQPGQGQQGYYPTSLQQTGQGQQSGQGQQGYYSSYHVSVEHQAASLKVAKAQQLAAQLPAMCRLEGGDALSASQ
Protein: Large ribosomal subunit protein eL32 (60S ribosomal protein L32) (Q6FS03)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- 60S ribosomal protein L6
- 40S ribosomal protein S30
- Large ribosomal subunit protein eL38
- 60S ribosomal protein L8
- Large ribosomal subunit protein eL31
- S16a
- Ribosomal protein L37
- 40S ribosomal protein S26
- Candida glabrata strain CBS138 chromosome F complete sequence
- 60S ribosomal protein L29
Sequence:
MAASLPHPKIVKKHTKKFKRHHSDRYHRVSENWRKQKGIDSVVRRRFRGNISEPTIGYGSNKKTKFMSPSGHKVVLVSNLKDLETLTMHTKSYAAEIAHNVSSKNRVTLLARAKALGVKVTNAKGRLALEA
Protein: Glycosylation-dependent cell adhesion molecule 1 (GlyCAM-1) (Endothelial ligand FOR L-selectin) (SGP50) (Sulfated 50 kDa glycoprotein) (Q04807)
Organism: Rattus norvegicus (Rat)
Function: Adhesion molecule that accomplishes cell binding by presenting carbohydrate(s) to the lectin domain of L-selectin.
Subcellular location: Cell membrane.
Interaction partners:
- L-selectin
- Alpha-S2-casein-like B
- Beta-casein
- E-selectin
- Alpha-lactalbumin
- Podocalyxin
- Alpha-S1-casein
- Endomucin
Sequence:
MKFFTVLLFASLAATSLAAVPGSKDELHLRTQPTDAIPASQFTPSSHISKESTSSKDLSKESFIFNEELVSEDNVGTESTKPQSQEAQDGLRSGSSQQEETTSAATSEGKLTMLSQAVQKELGKVIEGFISGVEDIISGASGTVRP
Protein: Hemoglobin subunit beta-1 (Beta-1-globin) (Hemoglobin beta chain, major-form) (Hemoglobin beta-1 chain) (P02091)
Organism: Rattus norvegicus (Rat)
Function: Involved in oxygen transport from the lung to the various peripheral tissues.
Interaction partners:
- Hemoglobin subunit alpha-1/2
- Globin c1
- Hemoglobin alpha, adult chain 2
- Globin b1
- Epsilon 3 globin
- Haptoglobin
- Hemoglobin subunit zeta
- Alpha-hemoglobin-stabilizing protein
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
Sequence:
MVHLTDAEKAAVNGLWGKVNPDDVGGEALGRLLVVYPWTQRYFDSFGDLSSASAIMGNPKVKAHGKKVINAFNDGLKHLDNLKGTFAHLSELHCDKLHVDPENFRLLGNMIVIVLGHHLGKEFTPCAQAAFQKVVAGVASALAHKYH
Protein: LIM domain binding 1 (D3ZT89)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKEAFHSNFVSLDCDQGSMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPARQQPSKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNNSPALGANSPWNSKPPSSQESKSENPTSQASQ
Protein: Necdin (P25233)
Organism: Mus musculus (Mouse)
Function: Growth suppressor that facilitates the entry of the cell into cell cycle arrest. Functionally similar to the retinoblastoma protein it binds to and represses the activity of cell-cycle-promoting proteins such as SV40 large T antigen, adenovirus E1A, and the transcription factor E2F. Necdin also interacts with p53 and works in an additive manner to inhibit cell growth. Also functions as a transcription factor and directly binds to specific guanosine-rich DNA sequences.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10965153}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10965153}. Nucleus matrix {ECO:0000269|PubMed:10965153}. Note=Mainly cytoplasmic. Translocates to the nucleus where it is found associated with the nuclear matrix.
Interaction partners:
- Cellular tumor antigen p53
- Transcription factor E2F1
- Tumor necrosis factor receptor superfamily member 16
- NAD-dependent protein deacetylase sirtuin-1
- Small nuclear ribonucleoprotein-associated protein N
- EP300-interacting inhibitor of differentiation 1
- Hypoxia-inducible factor 1-alpha
- Ubiquitin-protein ligase E3A
- Heterogeneous nuclear ribonucleoprotein U
- FRAT3
Sequence:
MSEQSKDLSDPNFAAEVPDCEMQDSDAVPVGIPPPASLAANLAGPPCAPEGPMAAQQASPPPEERIEDVDPKILQQAAEEGRAHQPQSPARPIPAPPAPAQLVQKAHELMWYVLVKDQKRMVLWFPDMVKEVMGSYKKWCRSILRRTSVILARVFGLHLRLTNLHTMEFALVKALSPEELDRVALNNRMPMTGLLLMILSLIYVKGRGAREGAVWNVLRILGLRPWKKHSTFGDVRKIITEEFVQQNYLKYQRVPHIEPPEYEFFWGSRANREITKMQIMEFLARVFKKDPQAWPSRYREALEQARALREANLAAQAPRSSVSED
Protein: Heat shock protein 83 (HSP 82) (Q9VAY2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Hsp90 co-chaperone Cdc37
- DnaJ-like-2, isoform A
- Endoplasmic reticulum chaperone BiP
- Hsc70Cb, isoform G
- Calreticulin
- Hypoxia up-regulated protein 1
- Protein disulfide-isomerase A6 homolog
- DnaJ homolog shv
- LD43819p
- 10 kDa heat shock protein, mitochondrial
Sequence:
MKYFLLVGLLLLAGINQIAADDEAATTETIDLDLGSFKEGSRTDAETLKREEEAIQLDGLNVAQLKEIREKAKKFTFQTEVNRMMKLIINSLYRNKEIFLRELISNASDAIDKIRLLALSNSKELETNPELHIRIKADKENKALHIMDSGIGMTHQDLINNLGTIAKSGTADFLAKMQDPSKSEGLDMNDMIGQFGVGFYSAFLVADRVVVTTKHNDDKQYIWESDANSFSITEDPRGDTLKRGSVISLYLKEEAQDFLEEDTVRELIRKYSQFINFPIRMWSSKTVEEEVPVEEEAKPEKSEDDVEDEDAKVEEAEDEKPKTKKVSKTTWDWTLINDSKPIWTRKPAEVTEDEYTSFYKSLTKDSSEPLTQTHFIAEGEVTFKSLLYVPKVQPSESFNRYGTKSDNIKLYVRRVFITDEFNDMMPNYLSFIRGVVDSDDLPLNVSRETLQQHKLIKVIKKKLVRKVLDMLKKIDKEAYEKFWKEFSTNIKLGVMEDPSNRSRLAKLLRFQTSNGKGVTSLAEYKERMKAKQEHIYYIAGANRAEVEKSPFVERLLSKGYEVLYLVEAVDEYCISALPEFDGKKFQNVAKEGFQLNESEKSKKNFESLKSTFEPLVKWLNDVALKDQISKAQVSERLSNSPCALVAGVFGWTGNMERLAMSNAHQKSDDPQRTYYLNQKKTLEINPRHPLMRELLRRVEADEADDTAKDMAVMMFRTATLRSGYMLQETSQFADSIEQMMRQTLGVSQDEQVEFDEEEEDDAEETATGSQESGNADDEEEEQQHDEL
Protein: Diphthamide synthesis protein (Q386P7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DPH-type MB domain-containing protein
- Elongation factor 2
Sequence:
MYHDAPPKPVATVMCRRQPKPREGIRSQYKLDSVASFILTGSSLSSSTSTQALASPFLRVALQFPDDLLDDAVAVVETLKGILLSDPRCVGGVYGVTPSPDVGEDCCCSNNDGRIRFFVVADNTFGSCCPDEITAQHYCSDCLIHFGESCMSRSTRIPVFYVQESFQFTATARQVTQQQEEQVRQKDLSARLVLGAVELLQKYLVGRVRSLVREKDAEATVNLVVVGCHRSRNVVEDAERRWRERHQAGTPVPDFVTLIDGSSVSWCSYELVQSTTNPEQPSTSGSVVNVHAAIPHSWSPSSGECSSWVINGVRFPRAGTKELQYFLFVGPSSAFLPLHILNVHQHNLYHYSQELREVAFEANESPPALIIMDESFGLTGDGGNLLSPLNDTARGDIDDATLETVLSTCSSGDGHSIAADIFSGDTCFRNAGYAKLQMVVDKRSKQRAFNIELIRATSAVGIVVASLSIAGYYETTMLLHKLLRAHGKRSYIIYIGHLNEFKIANFVDTVDCFVTIACPNSREGHFPEKKDGFPKPIVSPVEVLLALRAEDVDSPLYGHPAVFSTTFDSILPLLRNEVEEATGSQKRKEELRGDCTTLIRTMAGTVMTHDGGGSALDRLYQRTYVGLEPRTGQTPVQTQIEKGRHGIARGYATEKEQ
Protein: Possible glycosyl hydrolase (O53444)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Beta-D-galactosidase Rv1717
- Pre-mycofactocin glycosyltransferase
- Secreted protein
- Probable membrane protein
- Probable conserved proline rich membrane protein
Sequence:
MPKRPDNQTWRYWRTVTGVVVAGAVLVVGGLSGRVTRAENLSCSVIKCVALTFDDGPGPYTDRLLHILTDNDAKATFFLIGNKVAANPAGARRIADAGMEIGSHTWEHPNMTTIPPEDIPGQFSRANDVIAAATGRTPTLYRPAGGLSNDAVRQAAAKVGQAEILWDVIPFDWINDSNTAATRHMLMTQIKPGSVVLFHDTYSSTVDVVYQFIPVLKANGYRLVTVSELLGPRAPGSSYGSRENGPPVNELRDIPASEIPPLPNTSSPKPMPNFPITDIAGQNSGGPNNGA
Protein: Ribonucleases P/MRP protein subunit POP1 (EC 3.1.26.5) (RNA-processing protein POP1) (RNases P/MRP 100.4 kDa subunit) (P41812)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for processing of 5.8S rRNA (short form) at site A3 and for 5' and 3' processing of pre-tRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribonuclease P/MRP protein subunit RPP1
- Ribonucleases P/MRP protein subunit POP8
- RNases MRP/P 32.9 kDa subunit
- Ribonuclease MRP protein subunit SNM1
- Ribonuclease P/MRP protein subunit POP5
- Ribonucleases P/MRP protein subunit POP3
- Ribonucleases P/MRP protein subunit POP6
- Ribonuclease P protein subunit RPR2
- Ribonuclease MRP protein subunit RMP1
- Ribonucleases P/MRP protein subunit POP7
Sequence:
MSGSLSRGNGGKKVLNKNQLLKRNRIRNARSIRAEAVAASSTKTGTPSDLSESGSKLNVDQFISSRQFEVKQLQLAMHNSKAASSTRIFQALPRKLRRRTASHNVRRIPKRMRNRALREMRKSDQQDVLKGSSASSRKAHGLNAKQLYKARMSIKLLRLASKSTSMKLSMPPEVTSSNCHVRQKIKTLKRMIKESSTANPNIKLLNNRMGSYDCTGVNELAPIPKGRVKYTKRQKHFAWLPTHIWNAKRSHMMKRWGYQMVWAPTQKCFKLTHRLGGDTCSSDGALCMDSSYIGTIIVKDKSNDSEGDFLKSIIGKLTAERANLRKYREGQVLFQGLIYSFNEENGEDSTKPLGPCDVFWVQKDTAIIRLHPSIYTQVFNILLQHKEKLTVQDCRYSLASVTLKGAKALESLASCLRSTEYSKSFEQFKMVSMITDHNALPQRCTFAFEAIDPRHLAAPKKLNDSQRKTVNSDDILSLHENYPQDEINAVFNELCDPESRTQSYNNQNTLKEISARRYKLLTATPNSINKTTVPFKESDDPSIPLVIIRRLKTRDWIVVLPWFWLLPLWHLLNRIPRMYHIGLRQFQQIQYENKQLYFPDDYPFTQLGYIENSFYKKEASKTKWDRKPMGKRINFEKIKDIHNTKLPAYSGEIGDFFSSDWRFLQILRNGIDYLQRNDKTLELMDSKKTGQFNAQGVRDINCVNDVLEFCKDYEAKTKAMSLSIEENIPVALCKNRKCQFRTPDSISVNSSSFSLTFFPRCIIAVSCTLLERGHPKDNARIYQVPEKDLEHWLQLAKGVYRPNGRKDHDLKIPLPEVHDLIGFITSGTYHLNCGNGMGIGFIDHHAAIRQPTRYVLIRNVGTNTYRLGEWSKISV
Protein: Osmotically-inducible putative lipoprotein OsmE (Activator of ntr-like gene protein) (P0ADB1)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Peroxiredoxin OsmC
- Osmotically-inducible protein Y
- Uncharacterized protein YgaM
- Protein ElaB
- Potassium binding protein Kbp
- Uncharacterized protein YqjD
- NAD
- Uncharacterized lipoprotein YbaY
- UPF0410 protein YeaQ
- Serine/threonine kinase YeaG
Sequence:
MNKNMAGILSAAAVLTMLAGCTAYDRTKDQFVQPVVKDVKKGMSRAQVAQIAGKPSSEVSMIHARGTCQTYILGQRDGKAETYFVALDDTGHVINSGYQTCAEYDTDPQAAK
Protein: Protein phosphatase 2C homolog 4 (PP2C-4) (EC 3.1.3.16) (P38089)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Polyamine N-acetyltransferase 1
- Serine/threonine-protein kinase VHS1
- Protein phosphatase 2C homolog 7, mitochondrial
- SRP-independent targeting protein 1
- Mitogen-activated protein kinase SLT2/MPK1
Sequence:
MGQLLSHPLTEKTIEYNEYKNNQASTGIVPRFYNCVGSMQGYRLTQEDAHLIRNENSVVYVRFFNPFIDKYETLSLNVFAVFDGHGGDDCSKFLSGGRHHRDGNGSSNGNGEPNAGLIKWIAYSFENHHYTSTTNNDSSKFKRSFNTLEGLVSQIFKDAFILQDEELYRHFANSSCGSTAVVACIINEESLYVANCGDSRCILSSKSNGIKTMSFDHKPQHIGELIRINDNGGTVSLGRVGGVLALSRAFSDFQFKRGVTYPHRRTKLTNITQNLTYGTPPQEAQVTVEPDVLMHKIDYSKDEFLVLACDGIWDIYNNKQLIHFIKYHLVSGTKLDTIITKLLDHGIAQANSNTGVGFDNMTAIIVVLNRKGETLQDWFNKMKTRLERERGLV
Protein: MutL homolog 3 (G3V419)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIKCLSVEVQAKLRSGLAISSLGQCVEELALNSIDAEAKCVAVRVNMETFQVQVIDNGFGMGSDDVEKVGNRYFTSKCHSVQDLENPRFYGFRGEALANIADMASAVEISSKKNRTMKTFVKLFQSGKALKACEADVTRASAGTTVTVYNLFYQLPVRRKCMDPRLEFEKVRQRIEALSLMHPSISFSLRNDVSGSMVLQLPKTKDVCSRFCQIYGLGKSQKLREISFKYKEFELSGYISSEAHYNKNMQFLFVNKRLVLRTKLHKLIDFLLRKESIICKPKNGPTSRQMNSSLRHRSTPELYGIYVINVQCQFCEYDVCMEPAKTLIEFQNWDTLLFCIQEGVKMFLKQEKLFVELSGEDIKEFSEDNGFSLFDATLQKRVTSDERSNFQEACNNILDSYEMFNLQSKAVKRKTTAENVNTQSSRDSEATRKNTNDAFLYIYESGGPGHSKMTEPSLQNKDSSCSESKMLEQETIVASEAGENEKHKKSFLEHSSLENPCGTSLEMFLSPFQTPCHFEESGQDLEIWKESTTVNGMAANILKNNRIQNQPKRFKDATEVGCQPLPFATTLWGVHSAQTEKEKKKESSNCGRRNVFSYGRVKLCSTGFITHVVQNEKTKSTETEHSFKNYVRPGPTRAQETFGNRTRHSVETPDIKDLASTLSKESGQLPNKKNCRTNISYGLENEPTATYTMFSAFQEGSKKSQTDCILSDTSPSFPWYRHVSNDSRKTDKLIGFSKPIVRKKLSLSSQLGSLEKFKRQYGKVENPLDTEVEESNGVTTNLSLQVEPDILLKDKNRLENSDVCKITTMEHSDSDSSCQPASHILNSEKFPFSKDEDCLEQQMPSLRESPMTLKELSLFNRKPLDLEKSSESLASKLSRLKGSERETQTMGMMSRFNELPNSDSSRKDSKLCSVLTQDFCMLFNNKHEKTENGVIPTSDSATQDNSFNKNSKTHSNSNTTENCVISETPLVLPYNNSKVTGKDSDVLIRASEQQIGSLDSPSGMLMNPVEDATGDQNGICFQSEESKARACSETEESNTCCSDWQRHFDVALGRMVYVNKMTGLSTFIAPTEDIQAACTKDLTTVAVDVVLENGYLFRCYHKNLEDLGLEFVFPDTSDSLVLVGKVPLCFVEREANELRRGRSTVTKSIVEEFIREQLELLQTTGGIQGTLPLTVQKVLASQACHGAIKFNDGLSLQESCRLIEALSSCQLPFQCAHGRPSMLPLADIDHLEQEKQIKPNLTKLRKMAQAWRLFGKAECDTRQSLQQSMPPCEPP
Protein: Uncharacterized WD repeat-containing protein C4F10.18 (O36030)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Nucleoporin nup120
- Nucleoporin nup189
- Nucleoporin nup107
- Nucleoporin nup85
- Nucleoporin seh1
- Protein transport protein sec13
- Nucleoporin nup131
- Nucleoporin nup132
- Probable nucleoporin C890.06
- Nucleoporin nsp1
Sequence:
MTLSSNQYQLPLNVRPYTTTWCSQSPSCSNLLAIGHDTGITIYCASEEQTPGSTGLTLQELFTIQTGLPTLHLSFSSSCSYSENLHDGDGNVNSSPVYSLFLACVCQDNTVRLIITKNETIITQHVLGGKSGHHNFVNDIDIADVYSADNRLAEQVIASVGDDCTLIIWRLTDEGPILAGYPLSSPGISVQFRPSNPNQLIVGERNGNIRIFDWTLNLSAEENSQTELVKNPWLLTLNTLPLVNTCHSSGIASSLANVRWIGSDGSGILAMCKSGAWLRWNLFANNDYNEISDSTMKLGPKNLLPNVQGISLFPSLLGACPHPRYMDYFATAHSQHGLIQLINTYEKDSNSIPIQLGMPIVDFCWHQDGSHLAIATEGSVLLTRLMGFTRL
Protein: Glucomannan 4-beta-mannosyltransferase 2 (EC 2.4.1.32) (Cellulose synthase-like protein A2) (AtCslA2) (Glucomannan synthase) (Mannan synthase 2) (Q9FNI7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses glucomannan synthase and mannan synthase activities in vitro. Mannan synthase consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cellulose synthase-like protein D2
- Protein MANNAN SYNTHESIS-RELATED 1
- UDP-rhamnose/UDP-galactose transporter 2
- Cellulose synthase A catalytic subunit 5
- Pectinesterase inhibitor 6
- Cellulose synthase-like protein D5
- Cellulose synthase A catalytic subunit 1
- Peroxidase 36
- Cellulose synthase A catalytic subunit 6
- Xylan glycosyltransferase MUCI21
Sequence:
MDGVSPKFVLPETFDGVRMEITGQLGMIWELVKAPVIVPLLQLAVYICLLMSVMLLCERVYMGIVIVLVKLFWKKPDKRYKFEPIHDDEELGSSNFPVVLVQIPMFNEREVYKLSIGAACGLSWPSDRLVIQVLDDSTDPTVKQMVEVECQRWASKGINIRYQIRENRVGYKAGALKEGLKRSYVKHCEYVVIFDADFQPEPDFLRRSIPFLMHNPNIALVQARWRFVNSDECLLTRMQEMSLDYHFTVEQEVGSSTHAFFGFNGTAGIWRIAAINEAGGWKDRTTVEDMDLAVRASLRGWKFLYLGDLQVKSELPSTFRAFRFQQHRWSCGPANLFRKMVMEIVRNKKVRFWKKVYVIYSFFFVRKIIAHWVTFCFYCVVLPLTILVPEVKVPIWGSVYIPSIITILNSVGTPRSIHLLFYWILFENVMSLHRTKATLIGLFEAGRANEWVVTAKLGSGQSAKGNTKGIKRFPRIFKLPDRLNTLELGFAAFLFVCGCYDFVHGKNNYFIYLFLQTMSFFISGLGWIGTYVPS
Protein: Protein high chlorophyll fluorescent 107 (Q8RWG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved, directly or indirectly, in the processing of chloroplast encoded mRNAs. Exhibits sequence-specific RNA binding and RNA remodeling activities, probably leading to the activation of translation of the target gene cluster psbB-psbT-psbH-petB-petD. Blocks 5'-3' and 3'-5' exoribonucleases (e.g. polynucleotide phosphorylase (PNPase), RNase R) in vitro. Necessary for intercistronic RNA processing of the psbH 5' untranslated region or the stabilization of 5' processed psbH RNAs. Also required for the synthesis of psbB.
Subcellular location: Plastid, chloroplast {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000269|PubMed:15918885}; Peripheral membrane protein {ECO:0000269|PubMed:15918885}; Stromal side {ECO:0000269|PubMed:15918885}. Plastid, chloroplast stroma {ECO:0000269|PubMed:15918885}.
Interaction partners:
- Photosystem II reaction center protein H
- Pentatricopeptide repeat-containing protein At3g09650, chloroplastic
- Pentatricopeptide repeat-containing protein At5g42310, chloroplastic
- Photosystem II CP47 reaction center protein
- Protein HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 173
- Pentatricopeptide repeat-containing protein MRL1, chloroplastic
- Cytochrome b6-f complex subunit 4
- Cytochrome b6
- Protein MID1-COMPLEMENTING ACTIVITY 1
- Protein MULTIPLE CHLOROPLAST DIVISION SITE 1
Sequence:
MHFFFVPNSSSSSPSPANTSSFSLSFLTPQIPENLCKSPTKIHIGTHGISGQSFLSHPTFSSKNTYLYAVVDRSSSGVFSPQKESANGEGEESNTEEGVLVVRRPLLENSDKESSEEEGKKYPARIDAGLSNIAKKMPIFEPERSESSSSSSAAAAARAQERPLAVNLDLSLYKAKVLARNFRYKDAEKILEKCIAYWPEDGRPYVALGKILSKQSKLAEARILYEKGCQSTQGENSYIWQCWAVLENRLGNVRRARELFDAATVADKKHVAAWHGWANLEIKQGNISKARNLLAKGLKFCGRNEYIYQTLALLEAKAGRYEQARYLFKQATICNSRSCASWLAWAQLEIQQERYPAARKLFEKAVQASPKNRFAWHVWGVFEAGVGNVERGRKLLKIGHALNPRDPVLLQSLGLLEYKHSSANLARALLRRASELDPRHQPVWIAWGWMEWKEGNTTTARELYQRALSIDANTESASRCLQAWGVLEQRAGNLSAARRLFRSSLNINSQSYVTWMTWAQLEEDQGDTERAEEIRNLYFQQRTEVVDDASWVTGFLDIIDPALDTVKRLLNFGQNNDNNRLTTTLRNMNRTKDSQSNQQPESSAGREDIETGSGFNLDVFLRSKLSLDPLKLDVNLDSKRLERFTRGRINGA
Protein: Open reading frame X (Q1HAH9)
Organism: Staphylococcus aureus
Interaction partners:
Sequence:
AEYEKRLGPYTKIDIIEVPDEKAPENMSDKEIEQVKEKEGQRILAKIKPQSTVITLEIQGKMLSSEGLAQELNQRMTQGQSDFVFVIGGSNGLHKDVLQRSNYALSFSKMTFPHQMMRVVLIEQVYRAFKIMRGEAYHK
Protein: SUZ12 polycomb repressive complex 2 subunit (A0A0G2K2I0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- [histone H3]-lysine
- Polycomb protein EED
- RB-binding protein 4, chromatin-remodeling factor.
- Histone-lysine N-methyltransferase EZH2
- Zinc finger protein AEBP2
- Protein Jumonji
- Histone-binding protein RBBP7
- Metal-response element-binding transcription factor 2
- PHD finger protein 19
- E3 ubiquitin-protein ligase RING2
Sequence:
MAPQKHGGGGGGGSGPSAGSGGGGFGGSAAAVAAAVASGGKSGGGGCGGGGGYSASSSSAAAAGAAVLPVKKPKMEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSQNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDGSAVKSSDCSSRGPEFNSLMKIRGSSYDTVAEETVLIIAVHSTRSFHKSNREKAISPAQETLTTEMQTRKEKDTSNETRQKLRIFYQKIHFLYFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLESEDGEVEQQRTYSSGHNRLYFHSDTCLPLRPQEMEVDSEDEKDPEWLREKTITQIEEFSDVNEGEKEVMKLWNLHVMKHGFIADNQMNHACMLFVENYGQKIIKKNLCRNFMLHLVSMHDFNLISIMSIDKAVTKLREMQQKLEKGESAAPANEDIAEEQNGTANGFSETNSKEKALETDGVSGVPKQSKKQKL
Protein: DNA polymerase eta (EC 2.7.7.7) (RAD30 homolog A) (Xeroderma pigmentosum variant type protein homolog) (Q9JJN0)
Organism: Mus musculus (Mouse)
Function: DNA polymerase specifically involved in the DNA repair by translesion synthesis (TLS). Due to low processivity on both damaged and normal DNA, cooperates with the heterotetrameric (REV3L, REV7, POLD2 and POLD3) POLZ complex for complete bypass of DNA lesions. Inserts one or 2 nucleotide(s) opposite the lesion, the primer is further extended by the tetrameric POLZ complex. In the case of 1,2-intrastrand d(GpG)-cisplatin cross-link, inserts dCTP opposite the 3' guanine (By similarity). Particularly important for the repair of UV-induced pyrimidine dimers. Although inserts the correct base, may cause base transitions and transversions depending upon the context. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have any lyase activity, preventing the release of the 5'-deoxyribose phosphate (5'-dRP) residue. This covalent trapping of the enzyme by the 5'-dRP residue inhibits its DNA synthetic activity during base excision repair, thereby avoiding high incidence of mutagenesis. Targets POLI to replication foci (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y253}. Note=Binding to ubiquitinated PCNA mediates colocalization to replication foci during DNA replication and persists at sites of stalled replication forks following UV irradiation. After UV irradiation, recruited to DNA damage sites within 1 hour, to a maximum of about 80%; this recruitment may not be not restricted to cells active in DNA replication. Colocalizes with TRAIP to nuclear foci. {ECO:0000250|UniProtKB:Q9Y253}.
Interaction partners:
- Proliferating cell nuclear antigen
- DNA repair protein REV1
- DNA polymerase zeta catalytic subunit
- E3 ubiquitin-protein ligase RAD18
- RING finger and CHY zinc finger domain-containing protein 1
- DNA polymerase delta catalytic subunit
- Mitotic spindle assembly checkpoint protein MAD2B
- DNA polymerase epsilon catalytic subunit A
- DNA repair protein RAD51 homolog 1
- DNA polymerase delta subunit 3
Sequence:
MAPGQNRVVALVDMDCFFVQVEQRQNPHLRNKPCAVVQYKSWKGGGIIAVSYEARAFGVTRNMWADDAKKLCPDLLLAQVRESRGKANLTKYREASVEVMEIMSYFAVIERASIDEAYIDLTSAVQERLQKLQGQPISADLLPSTYIEGLPRGPTVEETVQKEAIRKQGLLQWLDSLQSDDPTSPDLRLTVGAMIVEEMRAAIESKTGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASVIEVLGIEYMGDLTQFTESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATREQVQWWLLQLALELEERLTKDRNDNDRVATQLVVSIRFQGDRRLSSLRRCCALPRYDAHKMSQDAFAAIRNCNTSGIQTEWSPPLTMLFLCATKFSAAAPPACTDITAFLSSDSSCQPKVPIASSETRTQGSGPAVPTSKEAATSLASFFQKAAKKQRMKETSFVPLNTATEKLSSKPSLVFQSSQTTGSQSFFKQKSLLLQHTQLSNSAAPDPPQASPAAQPSCLPAECVDSGPDDGAVKPVSSKAVSTEMNVAGDSPNVLDSPAYNSQEVTQRATEDQVLCEKCDSLVPVWDMPEHTDYHFALELQKSFLQPCTSKPQAIPAVSPQGKRNPKSPSASSSKRLRPHGMQTLESFFKPLTH