wanglab/gogpt-training-data huggingface dataset:
Protein: Germinal center kinase 1 (EC 2.7.11.1) (H2L099)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase which is required for normal oogenesis and suppression of germline cell apoptosis. Inhibits phosphorylation and thus probably activation of mpk-1 during pachytene stage. Involved in excretory canal elongation during postembryonic development, probably acting downstream of ccm-3.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25743393}. Apical cell membrane {ECO:0000269|PubMed:25743393}; Peripheral membrane protein {ECO:0000269|PubMed:25743393}. Note=Co-localizes with ccm-3 in the apical membrane of the excretory canals. {ECO:0000269|PubMed:25743393}.
Interaction partners:
- Programmed cell death protein 10 homolog
- Striatin N-terminal domain-containing protein
- DUF3402 domain-containing protein
- Cortactin-binding protein-2 N-terminal domain-containing protein
- MOB-like protein phocein
- Serine/threonine-protein phosphatase 2A catalytic subunit
- Mps one binder kinase activator-like 2
- Mob1/phocein
- MOB kinase activator-like 3
- MO25-like protein 2
Sequence:
MTTTSSDELPRQADDDSMKWDRIYIQKLDPEVIFTKQERIGRGSFGEVYKGIDNRTGRVVAIKIIDLEQAEDEIEDIQQEIQVLSQCDSQYVTKYFGSFLKGSKLWIIMEYLGGGSALDLTKSGKLDESHIAVILREILKGLEYLHSERKIHRDIKAANVLVSEHGDVKVADFGVAGQLTETVKKRITFVGSPFWMAPELIKQSSYDYKADIWSLGITAIELANGEPPHSDLHPMRVLFLIPKNPPPVLQGSQWSKPFKEFVEMCLNKDPENRPSASTLLKHQFIKRAKKNSILVDLIERAAEYRLRTGVSSDSDLDEDSDGGGGTSKWDYPTVRGPRVSADDDGTVRQRTDRPRAQVDRRSPSGSPGGTIVRGSPQVAAVAEQLRNSSVGSSGYGSGGNSASSQYATSSLPQSHTASSGGATTITLGSPNGSPTSSLARTQSMVSPSGQRSGSAQSWELERGNRPMSERVSSQVSPSKYNQHRTSSSNGVQGGSGGRREYINGSGSGLNGNSSNQNHSEYSDAVRQRGPGGSGGRLDYRESHVPTSSQENLNHGRMYGYGAPPPSREANNVPMPRVKGALDCSLLPAIEHLSRTRHATAALDQLRHVFRDVEDSCPGICNELIEELMQRIAVPQVSQSDLDAAIRRLTTPPS
Protein: Zinc finger CCCH domain-containing protein 3 (dZC3H3) (Q9VSK8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the export of polyadenylated mRNAs from the nucleu; binds to polyadenylated mRNA, and is involved in the regulation of mRNA polyadenylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:19364924}.
Interaction partners:
- Polyadenylate-binding protein 2
- Zinc finger protein swm
Sequence:
MLPHISADEAQPSMSRKVYINPNFQLQGQTAHQLPFQVPFQAFQAPLQPQPAIHINPHFLNRQRAMYDQYQREQQEQLMMQQVSASHYRLDPTIHLLATPPPPPAKIISKVSTCLVRKPSVVASGPAVKLAASVPVPTVSSLVQPPLVSISKRKIVRQGALKAAPAVAALHPPPPAKRTRYKLVRSISLTCTPLVKKRRPLREFVGQYALRRTNEAQPNRKLSSKPQALKLGVNKSLSMVSIHGVMYKKISKNKITKLDASSSARVAKSESPRTLQRTLSGRTLFVSGNKFILDPSGCRLTRVSTSSTGATQSSVNRSILRRIDIGGLTYVASPKALNVFVRTSNHVSRAHLITAKQRSLTLLNKSLVKTNVPCAIFQKLGKCVAHSRGKCRKLHDKRQVAICVSFLRGECTKPKCLLSHNVTLEKMPVCRYYLRGVCVREDCPYLHKKLSSKTEICIDFVRGYCPLAAECNKRHEFSCPELERKGKCELPRCVFCKKSPSKRLAKVKSRPKLGSKPVAFTDTAKESSTADELPTSSRYFGSHKEPAEAILTRDDVEQKKPEAEDEDQKEAGAPCPRRRPQLGTLPSFIPLGGEEKL
Protein: Protein C10 (F5GXW5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MASASTQPAALSAEQAKVVLAEVIQAFSAPENAVRMDEARDNACNDMGVLKFARLVKSYEAQDPEIASLSGKLKALFLPPMTLPPHGPAAGGSVAAS
Protein: Small ribosomal subunit protein eS27 (40S ribosomal protein S27) (Metallopan-stimulin 1) (MPS-1) (P42677)
Organism: Homo sapiens (Human)
Function: Component of the small ribosomal subunit. Required for proper rRNA processing and maturation of 18S rRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.
Interaction partners:
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein eL37
- Large ribosomal subunit protein eL33
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
Sequence:
MPLAKDLLHPSPEEEKRKHKKKRLVQSPNSYFMDVKCPGCYKITTVFSHAQTVVLCVGCSTVLCQPTGGKARLTEGCSFRRKQH
Protein: Prophage lipoprotein Bor homolog (Lipoprotein Bor homolog from lambdoid prophage DLP12) (P77330)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Protease 7
- ATP synthase gamma chain
- Uncharacterized fimbrial-like protein SfmH
- Type 1 fimbrin D-mannose specific adhesin
- PTS system maltose-specific EIICB component
- Probable autotransporter YfaL
- Uncharacterized fimbrial-like protein YfcV
- Probable fimbrial chaperone SfmC
- ATP synthase epsilon chain
- Chaperone protein FimC
Sequence:
MKKMLLATALALLITGCAQQTFTVQNKQTAVAPKETITHHFFVSGIGQKKTVDAAKICGGAENVVKTETQQTFVNGLLGFITLGIYTPLEARVYCSK
Protein: Murinoglobulin-1 (Alpha-1 inhibitor 3 variant I) (Alpha-X protein) (Q03626)
Organism: Rattus norvegicus (Rat)
Function: A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective.
Subcellular location: Secreted {ECO:0000269|PubMed:2511184}.
Interaction partners:
- UDP-glucuronosyltransferase 2B1
- Murinoglobulin-2.
- Serine protease inhibitor A3K
- Inter-alpha-trypsin inhibitor heavy chain 4
- Alpha-1-antiproteinase
- Alpha-2-HS-glycoprotein
- Beta-2-glycoprotein 1
- Histidine-rich glycoprotein
- Protein AMBP
- Apolipoprotein A-V
Sequence:
MKKNREAQLCLFSALLAFLPFASLLNGNSKYMVLVPSQLYTETPEKICLHLYHLNETVTVTASLISQRGTRKLFDELVVDKDLFHCLSFTIPRLPSSEEEESLDINIEGAKHKFSERRVVLVKNKESVVFVQTDKPVYKPGQSVKFRVVSMDKNLHPLNELFPLAYIEDPKMNRIMQWQDIKTENGLKQLSFSLSAEPIQGPYKIVILKQSGVKEEHSFTVMEFVLPRFGVDVKVPNAISVYDEIINVTACAIYTYGKPVPGHVKISLCHGNPSFSSETKSACKEEDSELDNNGCSTQEVNITEFQLKENYLKMHQAFHVNATVTEEGTGSEFSGSGRIEVERTRNKFLFLKADSHFRHGIPFFVKIRLVDIKGDPIPNEQVFIKAQEAGYTNATTTDQHGLAKFSIDTSSISGYSLNIKVYHKEESSCIHSSCTAERHAEEHHTAYAVYSLSKSYIYLDTEAGVLPCNQIHTVQAHFILKGQVLGVLPQIVFHYLVMAQGSILQTGNHTHQVEPGVSQVQGNFALEIPVEFSMVPVAKMLIYTILPDGEVIADSVTFQVEKCLRNKVHLSFSPSQSLPASQTHMRVTASPQSLCGLRAVDQSVLLLKPEAELSPSLIYDLPGMQDSNFIPSSYHPFEDEYDCLMYQPRDTEELTYSVPYGREKDVYRYVRDMGLTAFTNLKIKHPTYCYEMNMVVLSAPAVESELSPRGGEFEMMPLGVNKSPLPKEPPRKDPPPKDPVIETIRNYFPETWIWDLVTVNSSGVTEVEMTVPDTITEWKAGALCLSNDTGLGLSSVATLQAFQPFFVELTMPYSVIRGEAFMLKATVMNYLPTSLPMAVQLEASPDFTAVPVGNDQDSYCLGANGRHTSSWLVTPKSLGNVNFSVSVEAQQSPELCGSQVATVPETGRKDTVVKVLIVEPEGIKKEHTFSSLLCASDAELSETLSLLLPPTVVKDSARAHFSVMGDILSSAIKNTQNLIQMPYGCGEQNMVLFAPNIYVLKYLNETQQLTEKIKSKALGYLRAGYQRELNYKHKDGSYSAFGDHNGQGQGNTWLTAFVLKSFAQARAFIFIDESHITDAFTWLSKQQKDSGCFRSSGSLFNNAMKGGVDDEITLSAYITMALLESSLPDTDPVVSKALGCLEASWETIEQGRNGSFVYTKTLMAYAFALAGNQEKRNEILKSLDKEAIREDNSIHWERPQKPTKSEGYLYTPQASSAEVEMSAYVVLARLTAQPAPSPEDLALSMGTIKWLTKQQNSHGGFSSTQDTVVALDALSKYGAATFSKSQKTPLVTIQSSGSFSQKFQVDNSNRLLLQQVSLPDIPGNYTVSVSGEGCVYAQTTLRYNMPLEKQQPAFALKVQTVPLTCNNPKGQNSFQISLEISYTGSRPASNMVIADVKMLSGFIPLKPTVKKLERLEHVSRTEVTTNNVLLYLDQVTNQTLSFSFIIQQDIPVKNLQPAIVKVYDYYETDEVAFAEYSSPCSSDKQNV
Protein: Cancer/testis antigen family 45 member A10 (Cancer/testis antigen 45A10) (P0DMU9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:31429579}.
Interaction partners:
- Cancer/testis antigen family 45 member A1
- Cancer/testis antigen family 45 member A5
Sequence:
MTDKTEKVAVDPETVFKRPRECDSPSYQKRQRMALLARKQGAGDSLIAGSAMSKEKKLMTGHAIPPSQLDSQIDDFTGFSKDGMMQKPGSNAPVGGNVTSNFSGDDLECRGIASSPKSQQEINADIKCQVVKEIRCLGRKYEKIFEMLEGVQGPTAVRKRFFESIIKEAARCMRRDFVKHLKKKLKRMI
Protein: Ankyrin 2 (A0A5F9ZI81)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MMNEDAAQKSDSGEKFNGSSQRRKRPKKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGRASPCLERDNSSFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKELTEELGELEASSDEEAMVTTRVVRRRVIIQGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE
Protein: Exocyst complex component SEC15B (AtSec15b) (F4JHH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:24307681}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:20870962}. Secreted, cell wall {ECO:0000269|PubMed:20870962}. Secreted, extracellular exosome {ECO:0000269|PubMed:24307681}. Note=Localized to globular structures in the perinuclear region. During cytokinesis, localizes to the nascent cell plate and later to the cell plate insertion site and along the post-cytokinetic wall. Shuttles from the cytoplasm to the exocyst-positive organelle (EXPO) in the presence of EXO70E2 (PubMed:24307681). {ECO:0000269|PubMed:20870962, ECO:0000269|PubMed:24307681}.
Interaction partners:
- Exocyst complex component SEC8
- Exocyst complex component SEC6
- Exocyst complex component SEC3A
- Exocyst complex component SEC5A
- Exocyst complex component SEC5B
- Exocyst complex component EXO84B
- Exocyst complex component SEC10a
- Exocyst complex component SEC10b
- Exocyst complex component EXO84C
- Exocyst complex component EXO84A
Sequence:
MQSSKGRRKVGSTTAGAGIDSAEKLDELLISSAICNGEDLGPFVRKTFGTGKPETLLHHLKFFARSKESEIEEVCKAHYQDFIHAVDDLKSLLSDVESLKSALSDSNSKLQSVAAPLLSSLDSLVEAQTVSKNVDLAIGAVTHCVRVMELVSRANQHLQSGNFYMALKCVDSIESDFMEKTPSSTLKRMLENRIPAIRSYVERKVNKEFGDWLVEIRVVSRNLGQLAIGEASAARQREEELRIKQRQAEEQSRLSLRDCVYALNEEEDDEFGSGHEGSDGGSSGGGLLGFDLTPLYRAYHIHQTLSLGDTFKQYYYNNRDLQLTSDFQIAGFFIVEDRVLRTGGGLISKLEVETLWDTAVTKMCAVLEDQFSRMQTANHLLLIKDYVSLLGVSLRRYGYAVDSLLEVLSKHRDKYHELLLSDCRKQITEALSADKFEQMLMKKEYEYSMNVLSFQLQTSEIVPAFPFIAPFSTTVPDCCRIVRSFIEDSVSFMSHGGQLDFYDVVKKYLDRLLGEVLDEALLKLISTSVHGVSQAMQVAANMAVFERACDFFFRHAAHLSGVPLRMAERGRRHFPLTKSQNTAEDTLSGMLKKKIDGFMTLLENVNWTSDDIPQGGNEYMNEVLIYLETLVSTAQQILPAKVLKRVLRDVLAHISEKIVGTLCGDLVKRLSMAAIKGLDVDIQLLDSFTENLTPLLTDKEAREMKKAFVEIRQMINLLLSSHPENFVNPVIRERSYNALDYRKVATVSEKFRDPSDSIFGTFGTRGSRQNPKNKSLDALIKRLKDVS
Protein: Mismatch repair protein MSH3, putative (Q38F29)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA mismatch repair protein, putative
- Mismatch repair protein MSH8, putative
- Mismatch repair protein MLH1
- Mismatch repair protein PMS1, putative
- Proliferating cell nuclear antigen
- MutL C-terminal dimerisation domain-containing protein
- Exonuclease, putative
- Flap endonuclease 1
- Protein artemis
Sequence:
MSKRRRGDDESDIFRKAIELLCHRRATTEELSVATKLTPLERQVVCLKESLPPDVILMVACGYRVKFYGRDSRVVSRRFGIMCIQATPFEYSSVPYTGVNIYVRRLVAMGYRVAFADQESASIRSTSGNSKGLFSREIGRVYSRGTMLPDEVVVTAGTPQEGSATGQGDEGAPEGGDPVGVEELLPLKEGSSELFICFLWPSTGSAGVSLVEVTLLSFVTYSLSRHHLSSGGELLDILNRYNIVEVVLFYDEDGARELDRHQNAAATDGTLPPFRLCGLPEAFYTPLNTILSLHHGPTVNGEEDNNSVTVCTSPFIGSIDDSIAEYLKPSRFDTTFRKMCSKSPPLLARSTAGGVAELVMEMPGTTMSALDIFHSSIGLKGSLLALLDHSLTVPGLRRLRSWLAAPLCDLRAINSRREAVAFLLRGEGGDSVVGLLREFAKFGDLEATLGKLRAQRCTVTDYLRLLRAVKVTHKLALDILSLCGEGMCDQIRDALVAVTSENVELFLQSCKCELNLDADSPQEYYAALGSPLPDLLQTHAKERDEVLRALDVELECIRKTLKLPALEYRTIAGTTFIVDVPNVRANDAPKEWIVLTRTKTHVRFHTPRIVNLTVELCSAKERLAIAANEAWLAKQAELEGSVDTMEIFKSVINSVAVLDALHCLAVASSAPGYTAPSISDDEQSIVIRDGRHPMLESLMRGGYVGCDVSLVKHGAWILTGPNMGGKSALMRMVGTFVVLAQLGCYVPAKSAQLPLFGAVYCRMGSSDSLLEGSSTFLKEMEETSRILRSEIVSSSLVLLDELGRGTSSYDGIAIAAATLEYLLRKGATTFFVTHYSQLCEPYVNSSNNGLVSCYYMGFHEEKIVSREGEGEVKIVFTYKPTLGVTPSSFGARVARMAGLPSAVVTEAQLISEEAERTHDWCLSLLELRRFVKNNS
Protein: Short transient receptor potential channel 2 (TrpC2) (Transient receptor protein 2) (TRP-2) (mTrp2) (Q9R244)
Organism: Mus musculus (Mouse)
Function: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. May also be activated by intracellular calcium store depletion. Plays a role in mediating responsivity to pheromones that elicit aggressive and mating behaviors. Required for response to the Esp1 pheromone which enhances female sexual receptive behavior and to the Esp22 pheromone which inhibits adult male mating behavior.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Vomeronasal type-1 receptor 51
Sequence:
MLMSRTDSKSGKNRSGVRMFKDGDFLTPASGESWDRLRLTCSQPFTRHQSFGLAFLRVRSSLGSLADPVVDPSAPGSSGLNQNSTDVLESDPRPWLTNPSIRRTFFPDPQTSTKEISELKGMLKQLQPGPLGRAARMVLSAARKAPPASVVSPNNSHGEPGPSRAESAEPRAEEPNRKTAVGRRKRRKVQEPRRSLSNSSSQPNRRTGRTRQRQHRPQTKSDDGGVQAAGQCPICAGFFSIETLPQHAATCGESPPPQPASPASLSSSESVLRRHHVALTPVPLVPKPQPNWTEIVNKKLKFPPTLLRAIQEGQLGLVQQLLESSSDASGAGPGGPLRNVEESEDRSWREALNLAIRLGHEVITDVLLANVKFDFRQIHEALLVAVDTNQPAVVRRLLARLEREKGRKVDTKSFSLAFFDSSIDGSRFAPGVTPLTLACQKDLYEIAQLLMDQGHTIARPHPVSCACLECSNARRYDLLKFSLSRINTYRGIASRAHLSLASEDAMLAAFQLSRELRRLARKEPEFKPQYIALESLCQDYGFELLGMCRNQSEVTAVLNDLGEDSETEPEAEGLGQAFEEGIPNLARLRLAVNYNQKQFVAHPICQQVLSSIWCGNLAGWRGSTTIWKLFVAFLIFLTMPFLCIGYWLAPKSQLGRLLKIPVLKFLLHSASYLWFLIFLLGESLVMETQLSTFKGRSQSVWETSLHMIWVTGFLWFECKEVWIEGLRSYLLDWWNFLDVVILSLYLASFALRLLLAGLAYMHCRDASDSTTCRYFTTAERSEWRTEDPQFLAEVLFAVTSMLSFTRLAYILPAHESLGTLQISIGKMIDDMIRFMFILMIILTAFLCGLNNIYVPYQESEKLGNFNETFQFLFWTMFGMEEHTVVDMPQFLVPEFVGRAMYGIFTIVMVIVLLNMLIAMITNSFQKIEDDADVEWKFARSKLYLSYFREGLTLPVPFNILPSPKAAFYLVRRIFRFLCCGSSCCKAKKSDYPPIGTFTNPGARAGSAGEGERVSYRLRVIKALVQRYIETARREFEETRRKDLGNRLTELTKTVSRLQSEVASVQKNLAAGGAPRPPDGASILSRYITRVRNSFQNLGPPTSDTPAELTMPGIVETEVSLGDGLDGTGEAGAPAPGEPGSSSSAHVLVHREQEAEGSGDLLLEGDLETKGES
Protein: Alpha-1,3-mannosyltransferase MNN1 (EC 2.4.1.-) (P39106)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for addition of the terminal mannose residues to the outer chain of core N-linked polysaccharides and to O-linked mannotriose. Implicated in late Golgi modifications.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Mannosyltransferase KTR6
- Initiation-specific alpha-1,6-mannosyltransferase
- Alpha-1,2-mannosyltransferase MNN2
- Probable alpha-1,3-mannosyltransferase MNT4
- Mannosyltransferase regulator 4
- Mannan polymerase complexes subunit MNN9
- Alpha-1,2-mannosyltransferase MNN5
- Glycolipid 2-alpha-mannosyltransferase
- Mannan polymerase I complex VAN1 subunit
- Probable alpha-1,6-mannosyltransferase MNN10
Sequence:
MLALRRFILNQRSLRSCTIPILVGALIIILVLFQLVTHRNDALIRSSNVNSTNKKTLKDADPKVLIEAFGSPEVDPVDTIPVSPLELVPFYDQSIDTKRSSSWLINKKGYYKHFNELSLTDRCKFYFRTLYTLDDEWTNSVKKLEYSINDNEGVDEGKDANGNPMDEKSERLYRRKYDMFQAFERIRAYDRCFMQANPVNIQEIFPKSDKMSKERVQSKLIKTLNATFPNYDPDNFKKYDQFEFEHKMFPFINNFTTETFHEMVPKITSPFGKVLEQGFLPKFDHKTGKVQEYFKYEYDPSKTFWANWRDMSAKVAGRGIVLSLGSNQFPLAVKFIASLRFEGNTLPIQVVYRGDELSQELVDKLIYAARSPDFKPVENNYDNSTNVPQEIWFLDVSNTIHPKWRGDFGSYKSKWLVVLLNLLQEFVFLDIDAISYEKIDNYFKTTEYQKTGTVFYRERALRENVNERCIARYETLLPRNLESKNFQNSLLIDPDHALNECDNTLTTEEYIFKAFFHHRRQHQLEAGLFAVDKSKHTIPLVLAAMIHLAKNTAHCTHGDKENFWLGFLAAGHTYALQGVYSGAIGDYVKKTDLNGKRQEAAVEICSGQIAHMSTDKKTLLWVNGGGTFCKHDNAAKDDWKKDGDFKKFKDQFKTFEEMEKYYYITPISSKYVILPDPKSDDWHRASAGACGGYIWCATHKTLLKPYSYNHRTTHGELITLDEEQRLHIDAVNTVWSHANKDNTRSFTEEEIKELENSRHEQS
Protein: Small ribosomal subunit protein eS7 (40S ribosomal protein S7) (Q9VA91)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein eS19A
- IP17351p
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL30
Sequence:
MAIGSKIIKPGGSDPDDFEKSIAQALVELEANSDLKPYLRDLHITRAREIEFGSKKAVIIYVPIPQQKVFQKIQIILVRELEKKFSGKHVVVIAERKILPKPTRKARNPLKQKRPRSRTLTAVYDAILEDLVFPAEIVGKRIRVKLDGSQLVKVHLDKNQQTTIEHKVDTFTSVYKKLTGRDVTFEFPDNYLNV
Protein: RNA-binding (RRM/RBD/RNP motifs) family protein (Q9LZD9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEESAIKRLKSLELNDSDKQSTSTAICVEGYDTSLKEYPLRLALTKHFASCGEITQIYVPRDFKKKILKSVSFMWIKGEGAEDKALQLSGTDVGGWTVIVKPKPKHEPPSPITTISVEGYDTSLQKYLLELILEKHFDSCGEIRHVYVPTDYERGVLKSVAFLRIEGEGAEDKALQLSGTDVVGWTVIVKPSEIFYDNSSRAPATTPEASKIHRFRVTGYDASLPEIDIQMALCKHFSSCGEIWQVTVLSSTAFVSLRGERCVDKALELSGCNMGERTLVVNEPVVPQPELLKRKRVRHCTTTGYMPPGTWDKADADVYDE
Protein: Spermine oxidase (EC 1.5.3.16) (Polyamine oxidase 1) (PAO-1) (PAOh1) (Q9NWM0)
Organism: Homo sapiens (Human)
Function: Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. May contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-amino-propanal.
Subcellular location: [Isoform 1]: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm. Nucleus.
Interaction partners:
- Diamine acetyltransferase 1
- Spermine synthase
- Ornithine decarboxylase
- Spermidine synthase
Sequence:
MQSCESSGDSADDPLSRGLRRRGQPRVVVIGAGLAGLAAAKALLEQGFTDVTVLEASSHIGGRVQSVKLGHATFELGATWIHGSHGNPIYHLAEANGLLEETTDGERSVGRISLYSKNGVACYLTNHGRRIPKDVVEEFSDLYNEVYNLTQEFFRHDKPVNAESQNSVGVFTREEVRNRIRNDPDDPEATKRLKLAMIQQYLKVESCESSSHSMDEVSLSAFGEWTEIPGAHHIIPSGFMRVVELLAEGIPAHVIQLGKPVRCIHWDQASARPRGPEIEPRGEGDHNHDTGEGGQGGEEPRGGRWDEDEQWSVVVECEDCELIPADHVIVTVSLGVLKRQYTSFFRPGLPTEKVAAIHRLGIGTTDKIFLEFEEPFWGPECNSLQFVWEDEAESHTLTYPPELWYRKICGFDVLYPPERYGHVLSGWICGEEALVMEKCDDEAVAEICTEMLRQFTGNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGADVEKLAKPLPYTESSKTAPMQVLFSGEATHRKYYSTTHGALLSGQREAARLIEMYRDLFQQGT
Protein: Ethylene-responsive transcription factor SHINE 2 (Q9LFN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes cuticle formation by inducing the expression of enzymes involved in wax biosynthesis. Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- At5g15190
- Exosome complex component RRP45B
- Homeobox-leucine zipper protein HDG1
- GDSL esterase/lipase At1g58430
- Mitochondrial substrate carrier family protein
- Putative receptor-like protein kinase At3g47110
- Cytochrome P450 86A4
- Transcription factor MYB94
- Protein ECERIFERUM 2
Sequence:
MVHSRKFRGVRQRQWGSWVSEIRHPLLKRRVWLGTFETAEAAARAYDQAALLMNGQNAKTNFPVVKSEEGSDHVKDVNSPLMSPKSLSELLNAKLRKSCKDLTPSLTCLRLDTDSSHIGVWQKRAGSKTSPTWVMRLELGNVVNESAVDLGLTTMNKQNVEKEEEEEEAIISDEDQLAMEMIEELLNWS
Protein: Protein LYRIC (3D3/LYRIC) (Lysine-rich CEACAM1 co-isolated protein) (Metadherin) (Metastasis adhesion protein) (Q80WJ7)
Organism: Mus musculus (Mouse)
Function: Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=In epithelial cells, recruited to tight junctions (TJ) during the maturation of the TJ complexes. A nucleolar staining may be due to nuclear targeting of an isoform lacking the transmembrane domain. TNF-alpha causes translocation from the cytoplasm to the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Staphylococcal nuclease domain-containing protein 1
Sequence:
MAARSWQDELAQQAEEGSARLRELLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEAAPPTPAPDDLAQLKNLRSEEQKKKNRKKLPEKPKPNGRTVEVPEDEVVRNPRSITAKQAPETDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENIITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSRLNENLTVNGGGWSEKSVKLSSQLSEEKWNSVPPASAGKRKTEPSAWTQDTGDTNANGKDWGRNWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPSSDWNAPAEEWGNWVDEDRASLLKSQEPISNDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSHTQDTEDLEKDTREELPVNTSKARPKQEKACSLKTMSTSDPAEVLIKNSQPVKTLPPAISAEPSITLSKGDSDNSSSQVPPMLQDTDKPKSNAKQNSVPPSQTKSETNWESPKQIKKKKKARRET
Protein: Polyadenylate-binding protein 5 (PABP-5) (Poly(A)-binding protein 5) (Q96DU9)
Organism: Homo sapiens (Human)
Function: Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion matrix {ECO:0000269|PubMed:23275553}. Note=Co-fractionates with mtDNA and co-immunoprecipitates with the mitochondrial poly(A) polymerase.
Interaction partners:
- Polyadenylate-binding protein-interacting protein 1
- Homeobox protein TGIF2LX
- Homeobox protein TGIF2LY
- Polyadenylate-binding protein 2
- Eukaryotic translation initiation factor 4 gamma 1
- Homeobox protein TGIF2
- Protocadherin-11 X-linked
- Eukaryotic translation initiation factor 4E
- Polyadenylate-binding protein-interacting protein 2
- Eukaryotic initiation factor 4A-I
Sequence:
MGSGEPNPAGKKKKYLKAALYVGDLDPDVTEDMLYKKFRPAGPLRFTRICRDPVTRSPLGYGYVNFRFPADAEWALNTMNFDLINGKPFRLMWSQPDDRLRKSGVGNIFIKNLDKSIDNRALFYLFSAFGNILSCKVVCDDNGSKGYAYVHFDSLAAANRAIWHMNGVRLNNRQVYVGRFKFPEERAAEVRTRDRATFTNVFVKNIGDDIDDEKLKELFCEYGPTESVKVIRDASGKSKGFGFVRYETHEAAQKAVLDLHGKSIDGKVLYVGRAQKKIERLAELRRRFERLRLKEKSRPPGVPIYIKNLDETINDEKLKEEFSSFGSISRAKVMMEVGQGKGFGVVCFSSFEEATKAVDEMNGRIVGSKPLHVTLGQARRRC