wanglab/gogpt-training-data huggingface dataset:
Protein: tRNA pseudouridine synthase (EC 5.4.99.12) (F4I2L0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSDNLKHPLDCTASEESLERLSKVARIEGFSDEESEEQQGLADLESMNPVNPRVQRYLVAIEYIGTRFSGSQQQAKDRTVVGVLQEAFHKFIGQPVKIFCSSRTDAGVHALSNVCHVDVERISKRKPGEVLPPHEPGVVQRAVNHFLQRKDGDVMVIDVRCVPSNYHARYKAQERTYFYRLLSGSDPLSILEKDRCWHVPEELNLRFMQEACRVLVGSHDFSSFRAAGCQAKSPMRSLDELNITEVPSTPYFPSITERTLSNLNNGDPLACSNQPKSETAGVTTNVGEVEGSTEGDSFGRRRRHRCYVVTARSRGFLYHQVRLIVGALKCVGTGELTVSDVERILEAKTVSAAKPMAPASGLYLARVRYEFP
Protein: Zinc finger CCCH domain-containing protein 13 (Q5T200)
Organism: Homo sapiens (Human)
Function: Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR (By similarity). Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation (By similarity). In the WMM complex, anchors component of the MACOM subcomplex in the nucleus (By similarity). Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B) (By similarity).
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:24100041}. Nucleus, nucleoplasm {ECO:0000269|PubMed:24100041}.
Interaction partners:
- RNA-binding protein 15
- E3 ubiquitin-protein ligase Hakai
- Pre-mRNA-splicing regulator WTAP
- Protein virilizer homolog
- N
- N
- Putative RNA-binding protein 15B
- RNA N
- DNA-directed RNA polymerase II subunit RPB1
- Mediator of RNA polymerase II transcription subunit 17
Sequence:
MSKIRRKVTVENTKTISDSTSRRPSVFERLGPSTGSTAETQCRNWLKTGNCLYGNTCRFVHGPSPRGKGYSSNYRRSPERPTGDLRERMKNKRQDVDTEPQKRNTEESSSPVRKESSRGRHREKEDIKITKERTPESEEENVEWETNRDDSDNGDINYDYVHELSLEMKRQKIQRELMKLEQENMEKREEIIIKKEVSPEVVRSKLSPSPSLRKSSKSPKRKSSPKSSSASKKDRKTSAVSSPLLDQQRNSKTNQSKKKGPRTPSPPPPIPEDIALGKKYKEKYKVKDRIEEKTRDGKDRGRDFERQREKRDKPRSTSPAGQHHSPISSRHHSSSSQSGSSIQRHSPSPRRKRTPSPSYQRTLTPPLRRSASPYPSHSLSSPQRKQSPPRHRSPMREKGRHDHERTSQSHDRRHERREDTRGKRDREKDSREEREYEQDQSSSRDHRDDREPRDGRDRRDARDTRDRRELRDSRDMRDSREMRDYSRDTKESRDPRDSRSTRDAHDYRDREGRDTHRKEDTYPEESRSYGRNHLREESSRTEIRNESRNESRSEIRNDRMGRSRGRVPELPEKGSRGSRGSQIDSHSSNSNYHDSWETRSSYPERDRYPERDNRDQARDSSFERRHGERDRRDNRERDQRPSSPIRHQGRNDELERDERREERRVDRVDDRRDERARERDRERERDRERERERERERDREREKERELERERAREREREREKERDRERDRDRDHDRERERERERDREKEREREREERERERERERERERERERERERARERDKERERQRDWEDKDKGRDDRREKREEIREDRNPRDGHDERKSKKRYRNEGSPSPRQSPKRRREHSPDSDAYNSGDDKNEKHRLLSQVVRPQESRSLSPSHLTEDRQGRWKEEDRKPERKESSRRYEEQELKEKVSSVDKQREQTEILESSRMRAQDIIGHHQSEDRETSDRAHDENKKKAKIQKKPIKKKKEDDVGIERGNIETTSEDGQVFSPKKGQKKKSIEKKRKKSKGDSDISDEEAAQQSKKKRGPRTPPITTKEELVEMCNGKNGILEDSQKKEDTAFSDWSDEDVPDRTEVTEAEHTATATTPGSTPSPLSSLLPPPPPVATATATTVPATLAATTAAAATSFSTSAITISTSATPTNTTNNTFANEDSHRKCHRTRVEKVETPHVTIEDAQHRKPMDQKRSSSLGSNRSNRSHTSGRLRSPSNDSAHRSGDDQSGRKRVLHSGSRDREKTKSLEITGERKSRIDQLKRGEPSRSTSSDRQDSRSHSSRRSSPESDRQVHSRSGSFDSRDRLQERDRYEHDRERERERRDTRQREWDRDADKDWPRNRDRDRLRERERERERDKRRDLDRERERLISDSVERDRDRDRDRTFESSQIESVKRCEAKLEGEHERDLESTSRDSLALDKERMDKDLGSVQGFEETNKSERTESLEGDDESKLDDAHSLGSGAGEGYEPISDDELDEILAGDAEKREDQQDEEKMPDPLDVIDVDWSGLMPKHPKEPREPGAALLKFTPGAVMLRVGISKKLAGSELFAKVKETCQRLLEKPKDADNLFEHELGALNMAALLRKEERASLLSNLGPCCKALCFRRDSAIRKQLVKNEKGTIKQAYTSAPMVDNELLRLSLRLFKRKTTCHAPGHEKTEDNKLSQSSIQQELCVS
Protein: RE61046p (Q8MT37)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MKMVGCHPNDKKVKYDGIKSKTSSVTILTSVLNDAISALKSAFYKNQAPISEQNRSQIVSRMSLLRTILLIIISIHFKLAHADQVVLLDTTREATLEWTRYPYGPQAQTPGWVEESFTDFVKGINWRSYVVCDVAYHNVNNWLWSPFIDRGSANRLYIEIQFTIRDCSLFPGNALSCKETFSLLFYEFDAATREPPPWQTDSYRLIARIAAGEGRFNQNSDVDINTEVKSIAVNKKGVYFAFRDQGACISVLAVKVYYITCPAVTENFAHFNETPTGREITIIEKQNGTCVDNAEPYETPTYLCKGDGKWTILTGGCRCKAGYEPNYTNKTCTECPLGTFKSPEVTKCTPCPPNSNASKTGSPFCKCASGFYRHPNDGRHMPCYSPPAAPTNLTLLFVDQTSAIISWSAPAKNESFSSETNSKIYHSDIVYKIKCNICSPNVVYNPSTDTFNETKITLTNLEPVTTYTVQIHAINSVSHINEFKRHSNESSLVAVSDIVFSNTSLLNIPLDLNEVKTGQAEIVFTTESVLLSTVFNLRILAITNKDADLEWDKPVQSDFPLEFYEVRWFPKVELDAINKSALNTKETKAHIVGLLENTEYGFQVRCKTNNGFGSYSNMIYAQTLQSVGSVYDDSVQIRFIAGAIVTGVLFLVIFIIATVYFMRSKHQDDLDKK
Protein: TP53BP2 protein (Q05BL1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNAPLAGTLVVSGPRSQDPSLKRNGVKVPGEYRRKENGVNSPRMDLTLAELQEMASRQQQQIEAQQQLLATKEQRLKFLKQQDQRQQQQVAEQEKLKRLKEIAENQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNNLFQQKQRELVLAVSKVEELTRQLEMLKNGRIDSHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVNELRDRLWKKKAALQQKENLPVSSDGNLPQQAASAPSRVAAVGPYIQSSTMPRMPSRPELLVKPALPDGSLVIQASEGPMKIQTLPNMRSGAASQTKGSKIHPVGPDWSPSNADLFPSQGSASVPQSTGNALDQVDDGEVPLREKEKKVRPFSMFDAVDQSNAPPSFGTLRKNQSSEDILRDAQVANKNVAKVPPPVPTKPKQINLPYFGQTNQPPSDIKPDGSSQQLSTVVPSMGTKPKPAGQQPRVLLSPSIPSVGQDQTLSPGSKQESPPAAAVRPFTPQPSKDTLLPPFRKPQTVAASSIYSMYTQQQAPGKNFQQAVQSALTKTHTRGPHFSSVYGKPVIAAAQNQQQHPENIYSNSQGKPGSPEPETEPVSSVQENHENERIPRPLSPTKLLPFLSNPYRNQSDADLEALRKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSYPSKSASVTASSESPVEIQNPYLHVEPEKEVVSLVPESLSPEDVGNASTENSDMPAPSPGLDYEPEGVPDNSPNLQNNPEEPNPEAPHVLDVYLEEYPPYPPPPYPSGEPEGPGEDSVSMRPPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYEPQNDDELPMKEGDCMTIIHREDEDEIEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA
Protein: Statherin (P02808)
Organism: Homo sapiens (Human)
Function: Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface.
Subcellular location: Secreted.
Interaction partners:
- Histatin-1
- Mucin-7
- Mucin-5B
- Histatin-3
- Cystatin-S
- C4b-binding protein alpha chain
- Proline-rich protein 4
- Submaxillary gland androgen-regulated protein 3B
Sequence:
MKFLVFAFILALMVSMIGADSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQQYTF
Protein: Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I] (P18648)
Organism: Sus scrofa (Pig)
Function: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.
Subcellular location: Secreted.
Interaction partners:
- P-type phospholipid transporter
- Apolipoprotein B
- Apolipoprotein A-II
- Apolipoprotein C-III
- Apolipoprotein E
- Scavenger receptor class B member 1
- Phosphatidylcholine-sterol acyltransferase.
- Apolipoprotein C-IV
- ATP binding cassette subfamily A member 7.
- Albumin
Sequence:
MKAVVLTLAVLFLTGSQARHFWQQDDPQSPWDRVKDFATVYVDAIKDSGRDYVAQFEASALGKHLNLKLLDNWDSLGSTFTKVREQLGPVTQEFWDNLEKETEALRQEMSKDLEEVKKKVQPYLDDFQNKWQEEMETYRQKMAPLGAEFREGARQKVQELQEKLSPLAEELRDRLRAHVEALRQHVAPYSDDLRQRMAARFEALKEGGGSLAEYQAKAQEQLKALGEKAKPALEDLRQGLLPVLENLKVSILAAIDEASKKLNAQ
Protein: F-box domain-containing protein (Q22513)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNDGFQLLRLPHLVMIKTLNFMPIEDLLQISDNPLLYNSIREHVNTEKFTVNFYTDQSQLKIKGFTWLFYKTKFWDESESIKTIGPVTEKAHVFKNTWWTHSKNHRDIVVQLVHFFQNFFMRAKLETILYIATEDRNEERISQMDLKFLKESQYIVRDDASQTIHEYLKMFSNNKQLVAMDGFSDRARIARTKITSKNFTSGKLPVNPNEWFEYDYFHERLFEIVLISRLIVDNQNIQTIISSFVDGETFERLRFLHCQNADNIDLRYALQGVAAIEWTENNVFMEKFKGIPAMTNYFIETGYIIWDSKGKVATVHVDPEKSTFTLIGWENIISPRLMTALSNLEFN
Protein: Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Cellular thyroid hormone-binding protein) (Endoplasmic reticulum resident protein 59) (ER protein 59) (ERp59) (Prolyl 4-hydroxylase subunit beta) (p55) (P09103)
Organism: Mus musculus (Mouse)
Function: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP (By similarity). Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07237}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P07237}. Melanosome {ECO:0000250|UniProtKB:P07237}. Cell membrane {ECO:0000269|PubMed:21670307}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces. Colocalizes with MTTP in the endoplasmic reticulum. {ECO:0000250|UniProtKB:P07237}.
Interaction partners:
- Prolyl 4-hydroxylase subunit alpha-2
- Prolyl 4-hydroxylase subunit alpha-1
- Endoplasmic reticulum chaperone BiP
- Endoplasmin
- Microsomal triglyceride transfer protein large subunit
- ERO1-like protein alpha
- ERO1-like protein beta
- Prolyl 4-hydroxylase subunit alpha-3
- Calreticulin
- Peptidyl-prolyl cis-trans isomerase B
Sequence:
MLSRALLCLALAWAARVGADALEEEDNVLVLKKSNFEEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAAKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLSDTAAAESLVDSSEVTVIGFFKDVESDSAKQFLLAAEAIDDIPFGITSNSGVFSKYQLDKDGVVLFKKFDEGRNNFEGEITKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSSFKRAAEGFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAEKITEFCHRFLEGKIKPHLMSQEVPEDWDKQPVKVLVGANFEEVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIIIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDEDLDLEEALEPDMEEDDDQKAVKDEL
Protein: HIG1 domain family member 1A, mitochondrial (Hypoxia-inducible gene 1 protein) (RCF1 homolog A) (RCF1a) (Q9Y241)
Organism: Homo sapiens (Human)
Function: Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May play a role in the assembly of respiratory supercomplexes.
Subcellular location: Mitochondrion membrane {ECO:0000255|PROSITE-ProRule:PRU00836, ECO:0000269|PubMed:22342701}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836, ECO:0000269|PubMed:22342701}. Mitochondrion inner membrane {ECO:0000305|PubMed:22342701}.
Interaction partners:
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit NDUFA4
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 2
Sequence:
MSTDTGVSLPSYEEDQGSKLIRKAKEAPFVPVGIAGFAAIVAYGLYKLKSRGNTKMSIHLIHMRVAAQGFVVGAMTVGMGYSMYREFWAKPKP
Protein: Major vault protein (MVP) (Q6P3L0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q14764}. Nucleus {ECO:0000250|UniProtKB:Q14764}.
Interaction partners:
- Telomerase-associated protein 1.
- Poly [ADP-ribose] polymerase.
Sequence:
MDADHLLGASIIRIPPHHYIHVLDQNTNIARVEIGPLTYIRQDNERVLFAPVRMMMVPPRHYCVVLNPAVRDDEGQVQFDGSGQVKLRHADLEIRLAQDPFPLYPGEEIQKDVTPLQIVYPDTALRLQALLDFEEEGGEKRVAGDEWLFEGPGTYIPRKEVTVLEVIKATVIRENQAIRLRARKEGLDRSGVQRVTGEEWQVSKVGAYLPGAHEEVVDIVSAFILTDKKALHVRAIRPFRDAGGRDRRTGEEWLVTVADREAHIPSVAEEVVGVVDVTTLNSRQYCVIMDPVGADGKPQLGQKRVVKGERSFFLMPGEHLENGIQDVYVLSEEEGLVLRAVEAFIDTQGDEAEEEERESRAKKRGVQRRPGDRWMLRGPIEYVPPATVEVLLTRTAIPLDENEGIYVRDIKTGKVRAVIGQTYMLTQDEELWEKELPANVESLLAQSRDPLADRSDRGRSFGQAERDKTRVVSYRIPHNATVQVYDYREKKARVMFGPEMVMLGPDEQFTVLSLSGDKPKRPNVIKTICLLLGPDFCTDIITIETADHARLQLQLSYNWHFDLKQPADAAQAAALFSVPDFVGDACKAIASRIRGAVASVQFDDFHKNSNRIICSAVFGFDEKLAVRSSLRFGQNGLVISSVDIQSVEPVDQRTRDALQKSVQLAIEITTNSQEAAARHEAERLEQEARGRLERQKITDQAEAEKARKELLELEAQSAAVESTGAAKAEAQSRAEAARIQGEAAVEEAKLKAEAQKIEADSELARLCKAREQELNYKKQIDHLEVEKQQKLADIESQRFKHLMDNLGTETLKEMARAGPELQVKLLQSLGLKSTLITDGSSPINLFTTANGLLGSLQGKDKDE
Protein: C-X-C motif chemokine 11 (Beta-R1) (H174) (Interferon gamma-inducible protein 9) (IP-9) (Interferon-inducible T-cell alpha chemoattractant) (I-TAC) (Small-inducible cytokine B11) (O14625)
Organism: Homo sapiens (Human)
Function: Chemotactic for interleukin-activated T-cells but not unstimulated T-cells, neutrophils or monocytes. Induces calcium release in activated T-cells. Binds to CXCR3. May play an important role in CNS diseases which involve T-cell recruitment. May play a role in skin immune responses.
Subcellular location: Secreted.
Interaction partners:
- Platelet basic protein
- C-C motif chemokine 20
- C-C motif chemokine 25
- C-C motif chemokine 13
- Stromal cell-derived factor 1
- C-C motif chemokine 21
- C-C motif chemokine 8
- C-C motif chemokine 5
- C-X-C motif chemokine 2
- C-X-C motif chemokine 9
Sequence:
MSVKGMAIALAVILCATVVQGFPMFKRGRCLCIGPGVKAVKVADIEKASIMYPSNNCDKIEVIITLKENKGQRCLNPKSKQARLIIKKVERKNF
Protein: Hepatocyte nuclear factor 1-beta-B (HNF-1-beta-B) (HNF-1B-B) (Hepatocyte nuclear factor 1-beta-like) (Hepatocyte nuclear factor 1-gamma) (HNF1g) (Q8UW00)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor that binds to the inverted palindrome 5'-GTTAATNATTAAC-3' (By similarity). Acts downstream of hnf1ba but is not required for induction of rhombomere r5/r6 gene expression in the hindbrain.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P35680, ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Iroquois homeobox 3b.
- Pterin-4-alpha-carbinolamine dehydratase
- POU domain, class 3, transcription factor 3-A
- Hepatocyte nuclear factor 1-beta-A
Sequence:
MFTDMVSKLTSLQQELLSALLDSGVTKDVLVQALEDLCPCPAEFGIKIEKPLSPSSANGGSDCGDSKPVFLTLTGAQGKGGKLSGDEGSEDGDDFDTPPILRELQSLNTEEAAEQRAEVDRMLSEDPWRVARTIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTAKRAALYTWYVQKQREIDRQFDRVQGSDPSDSASQDQVLFFFPEFNHGGHSSGAAGGSGAAVGDEGEPGSKRMRRNRFKWGPASQEILYQAYERQKNPSKEEREALVEECNRAECVQRGVSPSKAHGLGSNLVTEVRVYNWFANRRKEEAFRQKLAMDTYTPHMNPLLSHTASLSHHHSSESKLRYSQQAASEVTSSTTISHPSVLQQVSPGGLDHCHGLLSTDAKMISVSGGVLPPVSTLTNIHSLSQSSHHHHHHHHQQAQSLIMSLAAQSLTSPQSQSVPVINSVSGLTTLQPMQFPQSSSLTQLTTAHISQQPFAQSHMYSPKQEAGQFSHPSRYSTMDSSTITHLGSSKQCPLQAW
Protein: Repressor ROX1 (Heme-dependent repression factor) (Hypoxic function repressor) (P25042)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor that represses the expression of HEM13, COX5B, ANB1, CYC7 or AAC3 (hypoxic function). Binds to the DNA sequence 5'-RRRTAACAAGAG-3'.
Subcellular location: Nucleus.
Interaction partners:
- Protein disulfide-isomerase EUG1
- Transcriptional activator/repressor MOT3
- Cytochrome c isoform 2
- General transcriptional corepressor CYC8
- General transcriptional corepressor TUP1
- Oxygen-dependent coproporphyrinogen-III oxidase
- SUMO-conjugating enzyme UBC9
- AP-1-like transcription factor YAP6
- Eukaryotic translation initiation factor 5A-2
- Putative uncharacterized protein YJL064W
Sequence:
MNPKSSTPKIPRPKNAFILFRQHYHRILIDEWTAQGVEIPHNSNISKIIGTKWKGLQPEDKAHWENLAEKEKLEHERKYPEYKYKPVRKSKKKQLLLKEIEQQQQQQQKEQQQQKQSQPQLQQPFNNNIVLMKRAHSLSPSSSVSSSNSYQFQLNNDLKRLPIPSVNTSNYMVSRSLSGLPLTHDKTARDLPQLSSQLNSIPYYSAPHDPSTRHHYLNVAQAQPRANSTPQLPFISSIINNSSQTPVTTTTTSTTTATSSPGKFSSSPNSSVLENNRLNSINNSNQYLPPPLLPSLQDFQLDQYQQLKQMGPTYIVKPLSHTRNNLLSTTTPTHHHIPHIPNQNIPLHQIINSSNTEVTAKTSLVSPK
Protein: Immunoglobulin superfamily member 1 (IgSF1) (Immunoglobulin-like domain-containing protein 1) (Inhibin-binding protein) (InhBP) (Pituitary gland-specific factor 2) (p120) (Q8N6C5)
Organism: Homo sapiens (Human)
Function: Seems to be a coreceptor in inhibin signaling, but seems not to be a high-affinity inhibin receptor. Antagonizes activin A signaling in the presence or absence of inhibin B (By similarity). Necessary to mediate a specific antagonistic effect of inhibin B on activin-stimulated transcription.
Subcellular location: [Isoform 1]: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
Interaction partners:
- Inhibin beta A chain
Sequence:
MTLDRPGEGATMLKTFTVLLFCIRMSLGMTSIVMDPQPELWIESNYPQAPWENITLWCRSPSRISSKFLLLKDKTQMTWIRPSHKTFQVSFLIGALTESNAGLYRCCYWKETGWSKPSKVLELEAPGQLPKPIFWIQAETPALPGCNVNILCHGWLQDLVFMLFKEGYAEPVDYQVPTGTMAIFSIDNLTPEDEGVYICRTHIQMLPTLWSEPSNPLKLVVAGLYPKPTLTAHPGPIMAPGESLNLRCQGPIYGMTFALMRVEDLEKSFYHKKTIKNEANFFFQSLKIQDTGHYLCFYYDASYRGSLLSDVLKIWVTDTFPKTWLLARPSAVVQMGQNVSLRCRGPVDGVGLALYKKGEDKPLQFLDATSIDDNTSFFLNNVTYSDTGIYSCHYLLTWKTSIRMPSHNTVELMVVDKPPKPSLSAWPSTVFKLGKAITLQCRVSHPVLEFSLEWEERETFQKFSVNGDFIISNVDGKGTGTYSCSYRVETHPNIWSHRSEPLKLMGPAGYLTWNYVLNEAIRLSLIMQLVALLLVVLWIRWKCRRLRIREAWLLGTAQGVTMLFIVTALLCCGLCNGVLIEETEIVMPTPKPELWAETNFPLAPWKNLTLWCRSPSGSTKEFVLLKDGTGWIATRPASEQVRAAFPLGALTQSHTGSYHCHSWEEMAVSEPSEALELVGTDILPKPVISASPTIRGQELQLRCKGWLAGMGFALYKEGEQEPVQQLGAVGREAFFTIQRMEDKDEGNYSCRTHTEKRPFKWSEPSEPLELVIKEMYPKPFFKTWASPVVTPGARVTFNCSTPHQHMSFILYKDGSEIASSDRSWASPGASAAHFLIISVGIGDGGNYSCRYYDFSIWSEPSDPVELVVTEFYPKPTLLAQPGPVVFPGKSVILRCQGTFQGMRFALLQEGAHVPLQFRSVSGNSADFLLHTVGAEDSGNYSCIYYETTMSNRGSYLSMPLMIWVTDTFPKPWLFAEPSSVVPMGQNVTLWCRGPVHGVGYILHKEGEATSMQLWGSTSNDGAFPITNISGTSMGRYSCCYHPDWTSSIKIQPSNTLELLVTGLLPKPSLLAQPGPMVAPGENMTLQCQGELPDSTFVLLKEGAQEPLEQQRPSGYRADFWMPAVRGEDSGIYSCVYYLDSTPFAASNHSDSLEIWVTDKPPKPSLSAWPSTMFKLGKDITLQCRGPLPGVEFVLEHDGEEAPQQFSEDGDFVINNVEGKGIGNYSCSYRLQAYPDIWSEPSDPLELVGAAGPVAQECTVGNIVRSSLIVVVVVALGVVLAIEWKKWPRLRTRGSETDGRDQTIALEECNQEGEPGTPANSPSSTSQRISVELPVPI
Protein: Poly(A)-specific ribonuclease PNLDC1 (EC 3.1.13.4) (PARN-like domain-containing protein 1) (Poly(A)-specific ribonuclease domain-containing protein 1) (B2RXZ1)
Organism: Mus musculus (Mouse)
Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. May act as a regulator of multipotency in embryonic stem cells. Is a critical factor for proper spermatogenesis, involved in pre-piRNAs processing to generate mature piRNAs (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27515512}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8NA58}. Note=Localizes mainly in the endoplasmic reticulum. {ECO:0000269|PubMed:27515512}.
Interaction partners:
- Poly
- Poly
- Tudor and KH domain-containing protein
- Mitochondrial cardiolipin hydrolase
- Symplekin
- Small RNA 2'-O-methyltransferase
- Neuroguidin
Sequence:
MDVGADEFEQSLPLLQELVAGADFVGLDIEFTGLRSNLSRPQQISLFDLPSEWYLKTRQSVQQFTICQIGLSMFSSIEGESNKYVAHSCNFFLFPTTFGILDSEFSFQASSVQFLNQYGFDYNKFLKNGIPYMNEEQEKKIKHSILRGNWRVRSSLDKDQIKVVIDKVTQWLDLAEEGDQMTLPGIAGFQAFEVQLVLRQALPNIWTVLKEEWVIVKKVSQPQRWYLEHASCDQVSCWKEQILLSARGFSVFFQMLVKAQKPLVGHNMMMDLLHLHEKFFRPLPESYDQFKQNIHSLFPVLIDTKNVTKDIWKELRFPRVSNLLEVYEVLSSNLNPTKDSGPVIIHARQCKKYAETKCPHEAAYDAFLCGSVLLKVAHLLLQRVHGNGAVHEPAFPQYLDVLAPYVNQVNLIRAGVPKINFSGPDYPSIRPPVLILTVKRWPGVSEQQVYREFQNLCKFDVRRFTRSQFLLLTNKFKDARSVLKEYRNHPTLQVSLYRSWRHSPNITCLLQVCSIVTTWAMIAFLLGRPMP
Protein: Programmed cell death protein 5 (TF-1 cell apoptosis-related protein 19) (Protein TFAR19) (O14737)
Organism: Homo sapiens (Human)
Function: May function in the process of apoptosis.
Interaction partners:
- Small ribosomal subunit protein eS19
- Small nuclear ribonucleoprotein E
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein eS24
Sequence:
MADEELEALRRQRLAELQAKHGDPGDAAQQEAKHREAEMRNSILAQVLDQSARARLSNLALVKPEKTKAVENYLIQMARYGQLSEKVSEQGLIEILKKVSQQTEKTTTVKFNRRKVMDSDEDDDY
Protein: Transcriptional regulator PsrA (Q4KFB4)
Organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Interaction partners:
Sequence:
MAQSETVERILDAAEQLFAEKGFAETSLRLITSKAGVNLAAVNYHFGSKKALIQAVFSRFLGPFCISLDRELERRQSRPENKPSLEELLEILVEQALVVQPRSGNDLSIFMRLLGLAFSQSQGHLRRYLEDMYGKVFRRYMLLVNEAAPRIPPIELFWRVHFMLGAAAFSMSGIKALRAIAETDFGVNTSIEQVMRLMVPFLAAGMRAETGVTDEAMASAQLKPRSKSAPAAAKA
Protein: Mitotic spindle-associated protein SHE1 (Sensitive to high expression protein 1) (P38200)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May have a role related to the spindle integrity function of the DAM1 complex, which is essential for proper chromosome segregation. Causes growth arrest when highly overexpressed.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Bud neck.
Interaction partners:
- Uncharacterized protein YHR127W
- PH domain-containing protein YHR131C
- Golgi apparatus membrane protein TVP38
Sequence:
MNDKLQEEHNEKDTTSQINGFTPPHMSIDFHSNNNSNIIETIGVSKRLGNSVLSELDSRASSKFEFLKDQSEQQYNGDKNNEPKSGSYNINEFFQAKHDSQFGQMESLDTHYTLLHTPKRKSQHAIPQDRSDSMKRSRPSRSIPYTTPVVNDITRRIRRLKLRNSLVNGNDIVARARSMQANSNINSIKNTPLSKPKPFMHKPNFLMPTTNSLNKINSAHRNTSSSSTASSIPRSKVHRSISIRDLHAKTKPVERTPVAQGTNSQLKNSVSVFDRLYKQTTFSRSTSMNNLSSGTSAKSKEHTNVKTRLVKSKTSGSLSSNLKQSTATGTKSDRPIWR
Protein: Serine/threonine-protein kinase STK11 (EC 2.7.11.1) (Liver kinase B1 homolog) (LKB1) (Q0GGW5)
Organism: Gallus gallus (Chicken)
Function: Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, leading to promote their activity (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- STE20-related kinase adapter protein alpha
- Calcium binding protein 39
- Uncharacterized protein.
- 5'-AMP-activated protein kinase subunit beta-1
- Protein kinase AMP-activated non-catalytic subunit gamma 2
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase beta-2 non-catalytic subunit transcript variant 2
- STE20 related adaptor beta.
- Protein kinase domain-containing protein.
Sequence:
MDMQESQQLGMFGESELMSVGMDTFIHRIDSTEVIYQPRRKRAKLIGKYLMGDLLGEGSYGKVKEMLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRHKNVIQLVDVLYNEEKQKMYMVMEYCVCGMQEMLDSVPEKRFPVFQAHGYFCQLIDGLEYLHSQGIVHKDIKPGNLLLTTNGTLKISDLGVAEALHPFAEDDTCRTSQGSPAFQPPEIANGLDTFSGFKVDIWSAGVTLYNITTGLYPFEGDNIYKLFENIGKGDFTIPEDCGPPLSDLLRGMLEYDPAKRFSIQQIRQHNWFRKKHAQAETLVPIPPSPETKDKWRSMTAVPYLEDLHGYNEDEDDDLYDIEDDIIYTQDFTVPGQVPEEEAGQNGQSRGRGLPKAICMNGTEPGQLSTKSKAERRASASSNPSRKACSASSKIRKLSTCKQQ