wanglab/gogpt-training-data huggingface dataset:
Protein: Cellular tumor antigen p53 (Tumor suppressor p53) (P13481)
Organism: Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Function: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04637}. Note=Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates to mitochondria in response to mitomycin C treatment (By similarity). Competitive inhibition of TP53 interaction with HSPA9/MOT-2 by UBXN2A results in increased protein abundance and subsequent translocation of TP53 to the nucleus (By similarity). {ECO:0000250|UniProtKB:P04637}.
Interaction partners:
Sequence:
MEEPQSDPSIEPPLSQETFSDLWKLLPENNVLSPLPSQAVDDLMLSPDDLAQWLTEDPGPDEAPRMSEAAPHMAPTPAAPTPAAPAPAPSWPLSSSVPSQKTYHGSYGFRLGFLHSGTAKSVTCTYSPDLNKMFCQLAKTCPVQLWVDSTPPPGSRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYSDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENFRKKGEPCHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPAGSRAHSSHLKSKKGQSTSRHKKFMFKTEGPDSD
Protein: Disease resistance protein LAZ5 (EC 3.2.2.6) (Protein LAZARUS 5) (Protein TOLERANCE TO TOBACCO RINGSPOT VIRUS 1) (O48573)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: TIR-NB-LRR receptor-like protein that may play a role in plant innate immunity. May trigger hypersensitive programmed cell death in response to pathogen attack. Involved in tolerance to tobacco ringspot virus (TRSV).
Interaction partners:
- Accelerated cell death 11
- Histone-lysine N-methyltransferase ASHH2
- Transcription elongation factor
- Dormancy-associated protein homolog 3
- Disease resistance protein ADR1
- LRR protein
- Phosphatidylinositol:ceramide inositolphosphotransferase 2
Sequence:
MAASSEILPESWQVFINFRGADLRNGFISHLAGALTSAGITYYIDTEEVPSEDLTVLFKRIEESEIALSIFSSNYAESKWCLDELVKIMEQVKKGKLRIMPVFFNVKPEEVREQNGEFGLKLYGEGKSKRPNIPNWENALRSVPSKIGLNLANFRNEKELLDKIIDSIKKVLARITRASRVAESLNGISKDSEAKNVDTFSPNSSDFPSTSIDDDLSINSPQYQATIPPASREGERLNTISTVSSTGSIEHPPPNYGIEPRLKEMEEKLDFDSLETKTVGIVGMPGIGKTTLAETLYRKWEHKFERSMFFPDASKMANEHGMCWLQKRLLEELLKDTNLNIGYTTNEHEFCKDVLLLKKVFLVIDNVSSEEQIETLFGKWNWIKNGSKIVITSSDESMLKGFVKDTYVVPSLNSRDSLLWFTNHAFGLDDAQGNLVKLSKHFLNYAKGNPLALGAFGVELCGKDKADWEKRIKTLTLISNKMIQDVLRRRYDELTERQKDIFLDVACFFKSENESYVRHVVNSCDSESTKSWDEITDLKGKFLVNISGGRVEMHDILCTFAKELASQALTEDTRVHLRLWNYQDIMWFLNNELEMENVRGIFLDMSKVPEEMTFDGNIFSNMCNLRYLKIYSSVCHKEGEGIFKFDTVREIQLPLDKVRYLHWMKYPWEKLPSDFNPENLVDLELPYSSIKKVWEGVKDTPILKWANLSYSSKLTNLLGLSNAKNLERLNLEGCTSLLKLPQEMENMKSLVFLNMRRCTSLTCLQSIKVSSLKILILSDCSKLEEFEVISENLEELYLDGTAIKGLPPAAGDLTRLVVLNMEGCTELESLPKRLGKQKALQELVLSGCSKLESVPTDVKDMKHLRLLLLDGTRIRKIPKIKSLKCLCLSRNIAMVNLQDNLKDFSNLKCLVMKNCENLRYLPSLPKCLEYLNVYGCERLESVENPLVADRLTLFLDRSEELRSTFLFTNCHNLFQDAKDSISTYAKWKCHRLAVECYEQDIVSGAFFNTCYPGYIVPSWFDHQAVGSVLEPRLEPHWYNTMLSGIALCAVVSFHENQDPIIGSFSVKCTLQFENEDGSLRFDCDIGCLNEPGMIEADHVFIGYVTCSRLKDHHSIPIHHPTTVKMQFHLTDACKSKVVDCGFRLMYTQSRGCLLEEEVNANFTKLYLGLL
Protein: Putative holocytochrome-c synthase (EC 4.4.1.17) (Cytochrome c heme lyase) (CCHL) (O74794)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P06182}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P06182}.
Interaction partners:
- Protoheme IX farnesyltransferase, mitochondrial
- Putative holocytochrome-c1 synthase
- Ferrochelatase, mitochondrial
- Cytochrome c
- Uncharacterized FAD-binding protein C17H9.12c
- Uroporphyrinogen decarboxylase
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MTSSETTTDHPRTGKCPIDHSKFARSNEANPDAYINGIKKDQQSSSWWNSLWSRNTDVASEPDVAMLHKKPSTVDTHDHPLANPPPGCPMHKASNENSTGFFSNLFGREKQNSEATPAVQPPATCPMSNSNQKPAGVSEVLTGVDSKQQSYVPEGCPVATPKRGWFNWFGNNDDQKQEAYEVDKSNMMYKNIPQTAVDDQVVGLETTRTTSSIPKVDGKNWEYPSPQQMYNAMWRKGYRDSGENVPIMVQVHNFLNEGAWSEIKAWEREAGENTEPKLLRFEGNANKRTPRALWYMMLGRINPNRWGSGEGPFDRHDWYVQRKDNSIVRYVIDYYEAPDSADGKPVFSLDVRPAVDSFESVALRWKHWRAMRQMQQQ
Protein: Galactose-binding lectin (MCL) (A0A0P0E482)
Organism: Mytilus californianus (California mussel)
Function: D-galactose-binding lectin. Binds also N-acetyl-D-galactosamine. Has hemagglutination activity towards all types of human erythrocytes (O, A and B) and rabbit erythrocytes. Agglutinates Gram-negative and Gram-positive bacteria including E.coli DH5-alpha and L.plantarum ATCC8014, respectively, and has bacteriostatic activity against them. Agglutinates also M.lysodeikticus. May be involved in innate immunity by recognizing and eliminating pathogens.
Interaction partners:
Sequence:
MTTFLIKHKASGKFLHPKGGSSNPANDTNLVLHSDIHERMYFQFDVVDERWGYIKHAASGKIVHPLGGKADPPNETKLVLHQDRHDRALFAMDFFNDNIIHKAGKYVHPKGGSTNPPNETLTVMHGDKHGAMEFIFVSPKNKDKRVLVYV
Protein: Acetoin utilization protein AcuA (EC 2.3.1.-) (Acetoin dehydrogenase) (Protein acetyltransferase AcuA) (Q65G33)
Organism: Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46)
Function: Part of the acuABC operon, which is possibly involved in the breakdown of acetoin and butanediol. Acts as an acetyltransferase inactivating acetyl-CoA synthetase AcsA via acetylation at a Lys residue.
Interaction partners:
- Acetoin utilization protein AcuC
- Acetoin dehydrogenase
- acetate--CoA ligase
- Glutamate synthase
- Lipoprotein
- Conserved membrane protein YuiB
- Conserved protein YqgY
- KinB-signaling pathway activation protein
- Conserved protein YqzF
- YugN-like family protein
Sequence:
MEHHKTYHAKELQTEKGSVLIEGPISPEKLAEYEFHDELTAFRPSQKQHEALIEIAGLPEGRIIIARFRQTIVGYVTYVYPDPLERWSEGNMENLIELGAIEVIPAFRGHSVGKTLLAVSMMDPQMEKYIIITTEYYWHWDLKGTNKDVWEYRKMMEKMMNAGGLVWFATDDPEISSHPANCLMARIGKEVSQESIERFDRLRFHNRFMY
Protein: Guanine nucleotide-exchange factor SEC12 (Mammalian guanine nucleotide exchange factor Sec12) (mSec12) (Prolactin regulatory element-binding protein) (Q9WUQ2)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide exchange factor that specifically activates the small GTPase SAR1B. Mediates the recruitment of SAR1B and other COPII coat components to endoplasmic reticulum membranes and is therefore required for the formation of COPII transport vesicles from the ER.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9WTV0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9WTV0}. Nucleus {ECO:0000250|UniProtKB:Q9WTV0}. Note=Concentrates at endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). {ECO:0000250|UniProtKB:Q9HCU5}.
Interaction partners:
- Melanoma inhibitory activity protein 2
- Small COPII coat GTPase SAR1B
- Small COPII coat GTPase SAR1A
- Protein transport protein Sec23A
- Protein transport protein Sec16A
- Protein SEC13 homolog
- SEC24 homolog B, COPII coat complex component)
- Transport and Golgi organization protein 1 homolog
- SEC24 homolog C, COPII coat complex component
- Protein transport protein Sec24A
Sequence:
MGRRRGVELYRAPFPLYALRIDPKTGLLIAAGGGGAAKTGIKNGVHFLQLELINGCLSASLLHSHDTETRATMNLALAGDILAAGQDAQCQLLRFQVHQQKGSKAEKSGSKEQGPRQRKGAPPAEKKSGAQVHPEGVELKVKNLEAVQTDFSNEPLQKVVCFNHDNTLLATGGTDGHVRVWKVPSLEKVLEFKAHEGEIGDLTLGPDGKLVTVGWDFKASVWQKDQLVTQLQWQENGPASSNTPYRYQACRFGQVPDQLGGLRLFTVQIPHKRLRQPPPCYLTAWDSSTFLPLRTRSCGHEVISCLSVSDSGTFLGLGTVTGSVAIYIAFSLQRLYYVKEAHGIVVTDVTFLPEKGCGPKLLGPHETALFSVAVDSRCQLHLLPSRRSVPVWLLLLLCVGLIIVTILLLQTAFPGFL
Protein: B-box domain protein 31 (AtBBX31) (Microprotein 1B) (Q9LRM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Developmental regulator acting by forming heterodimeric complexes, that sequester CO and CO-like (COL) proteins into non-functional complexes. Involved in the CO-mediated long-day flowering-promotion pathway. Engages CO and the transcriptional repressor TPL in a tripartite complex (By similarity). Involved in the CO-mediated long-day flowering-promotion pathway.
Interaction partners:
- Protein TOPLESS
- B-box zinc finger protein 19
- B-box zinc finger protein 25
- B-box zinc finger protein 23
- Zinc finger protein CONSTANS-LIKE 12
- B-box zinc finger protein 24
- B-box zinc finger protein 21
- Transcription factor HY5
- DNA-binding enhancer protein-like protein
- B-box zinc finger protein 20
Sequence:
MCRGLNNEESRRSDGGGCRSLCTRPSVPVRCELCDGDASVFCEADSAFLCRKCDRWVHGANFLAWRHVRRVLCTSCQKLTRRCLVGDHDFHVVLPSVTTVGETTVENRSEQDNHEVPFVFL
Protein: Uncharacterized protein At2g01755 (Q570J5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLITPANLSGGIAGLFVFGQKDQMTKIPSLTNSYNYRKKLFTVPPVAERRRALKMFWCGARRRVRDEGGGEDEDEMYGYNEEMAMLEIYSQSCREEALIVTAIVDDEEVEVVIFKGVSSCLSGETAVDPARSVLPERAVITKIDRVRGPFDPSQIHYIQRDISFQAFKETRLN
Protein: Silicatein alpha (Q2MEV3)
Organism: Suberites domuncula (Sponge)
Interaction partners:
Sequence:
MLVTVVVLGLLGFASAAQPKFEFVEEWQLWKSTHSKMYESQLMELERHLTWLSNKKYIEQHNVNSHIFGFTLAMNQFGDLSELEYADYLGQYRIEDKKSGNYSKTFQRDPLQDYPEAVDWRTKGAVTAVKDQGDCGASYAFSAMGALEGANALAKGNAVSLSEQNIIDCSIPYGNHGCHGGNMYDAFLYVIANEGVDQDSAYPFVGKQSSCNYNSKYKGTSMSGMVSIKSGSESDLQAAVSNVGPVSVAIDGANSAFRFYYSGVYDSSRCSSSSLNHAMVVTGYGSYNGKKYWLAKNSWGTNWGNSGYVMMARNKYNQCGIATDASYPTL
Protein: Small ribosomal subunit protein uS11 (40S ribosomal protein S14) (P62263)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.
Interaction partners:
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein eL15
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL18
Sequence:
MAPRKGKEKKEEQVISLGPQVAEGENVFGVCHIFASFNDTFVHVTDLSGKETICRVTGGMKVKADRDESSPYAAMLAAQDVAQRCKELGITALHIKLRATGGNRTKTPGPGAQSALRALARSGMKIGRIEDVTPIPSDSTRRKGGRRGRRL
Protein: DNA-directed RNA polymerases II, IV and V subunit 10 (DNA-directed RNA Polymerase II subunit L) (Q8LFJ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase II subunit 4
- DNA-directed RNA polymerases II and IV subunit 5A
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerases II, IV and V subunit 9B
- DNA-directed RNA polymerases IV and V subunit 2
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerases II and V subunit 6B
- DNA-directed RNA polymerase I subunit 2
- DNA-directed RNA polymerases IV and V subunit 4
- DNA-directed RNA polymerases II, IV and V subunit 12
Sequence:
MIIPVRCFTCGKVIGNKWDQYLDLLQLDYTEGDALDALQLVRYCCRRMLMTHVDLIEKLLNYNTLEKSDNS
Protein: Protein bicaudal D homolog 2 (Bic-D 2) (Q8TD16)
Organism: Homo sapiens (Human)
Function: Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates and stabilizes the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Facilitates the binding of RAB6A to the Golgi by stabilizing its GTP-bound form. Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport via its interaction with RAB6A and recruitment of the dynein-dynactin motor complex. Contributes to nuclear and centrosomal positioning prior to mitotic entry through regulation of both dynein and kinesin-1. During G2 phase of the cell cycle, associates with RANBP2 at the nuclear pores and recruits dynein and dynactin to the nuclear envelope to ensure proper positioning of the nucleus relative to centrosomes prior to the onset of mitosis (By similarity).
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664119}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11864968}. Cytoplasm {ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664120}. Nucleus envelope {ECO:0000269|PubMed:20386726}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:20386726}. Note=In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends (By similarity). Localizes to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae in a RANBP2-dependent manner during G2 phase of the cell cycle (PubMed:20386726). {ECO:0000250|UniProtKB:Q921C5, ECO:0000269|PubMed:11864968, ECO:0000269|PubMed:20386726}.
Interaction partners:
- Cytoplasmic dynein 1 heavy chain 1
- Dynactin subunit 2
- Cytoplasmic dynein 1 light intermediate chain 1
- Dynactin subunit 1
- Cytoplasmic dynein 1 intermediate chain 1
- E3 SUMO-protein ligase RanBP2
- Ras-related protein Rab-6A
- Serine/threonine-protein kinase Nek9
- RANBP2-like and GRIP domain-containing protein 2
- Protein Hook homolog 3
Sequence:
MSAPSEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDNKTSTPKKEGLAPPSPSLVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYREGQGGAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRADGGTGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQTRRGRAKAAPKTKPATPSL
Protein: Large ribosomal subunit protein eL37y (60S ribosomal protein L37-2) (Q43292)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to the 23S rRNA.
Interaction partners:
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein eL34z
- Large ribosomal subunit protein uL1z
- Large ribosomal subunit protein eL34y
- Small ribosomal subunit protein eS28z/eS28y
- Large ribosomal subunit protein eL43y
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL18y
Sequence:
MTKGTGSFGKRRNKSHTLCVRCGRRSFHIQKSRCSACAYPAARKRTYNWSVKAIRRKTTGTGRMRYLRNVPRRFKTGFREGTEAKPRNKGVASSA
Protein: Syntaxin binding protein 2 (M0R1A1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPSGLKAVVGEKILSGVIRSVKKDGEWKVLIMDHPSMRILSSCCKMSDILAEGITIVEDINKRREPIPSLEAIYLLSPTEKSVQALIKDFQGTPTFTYKAAHIFFTDTCPEPLFSELGRSRLAKVVKTLKEIHLAFLPYEAQVFSLDAPHSTYNLYCPFRAEERTRQLEVLAQQIATLCATLQEYPAIRYRKGPEDTAQLAHAVLAKLNAFKADTPSLGEGPEKTRSQLLIMDRAADPVSPLLHELTFQAMAYDLLDIEQDTYRYETTGLSEAREKAVLLDEDDDLWVELRHMHIADVSKKVTELLRTFCESKRLTTDKANIKDLSQILKKMPQYQKELNKYSTHLHLADDCMKHFKGSVEKLCSVEQDLAMGSDAEGEKIKDSMKLIVPVLLDAAVPAYDKIRVLLLYILLRNGVSEENLAKLIQHANVQAHSSLIRNLEQLGGTVTNPGGSGTSSRLEPRERMEPTYQLSRWTPVIKDVMEDAVEDRLDRNLWPFVSDPAPTASSQAAVRLLTHPHPDPLPG
Protein: Hemoglobin subunit zeta (HBAZ) (Hemoglobin zeta chain) (Zeta-globin) (P02008)
Organism: Homo sapiens (Human)
Function: The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin.
Interaction partners:
- Hemoglobin subunit beta
- Hemoglobin subunit epsilon
- Hemoglobin subunit gamma 1
- Hemoglobin subunit delta
- Transcription factor JunD
- Mothers against decapentaplegic homolog 2
- Hemoglobin subunit gamma-2
- Transcription factor Jun
- Histone acetyltransferase p300
- Hemoglobin subunit theta-1
Sequence:
MSLTKTERTIIVSMWAKISTQADTIGTETLERLFLSHPQTKTYFPHFDLHPGSAQLRAHGSKVVAAVGDAVKSIDDIGGALSKLSELHAYILRVDPVNFKLLSHCLLVTLAARFPADFTAEAHAAWDKFLSVVSSVLTEKYR
Protein: LTO1 family protein C191.08 (Q9Y7Q1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The complex LTO1:YAE1 may function as a target specific adapter that probably recruits apo-RPLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative tRNA 2'-phosphotransferase
- Translation initiation factor rli1
- Cytosolic Fe-S cluster assembly factor nbp35
- MIP18 family protein C144.16
- NADPH-dependent diflavin oxidoreductase 1
- Fe-S cluster assembly protein dre2
- DNA repair/transcription protein mms19
Sequence:
MDWEEVTKLEENEYKRGYDEGILKGIEQGYEEAFLFGLEHAYNKYLLAGEIYGRVCFWLKEENSQHPKIKKAHRHLEQLKSLLESLPTNNELEETDAGFDSYWNKITAKAKVVSSLLGTKILPAEKIDANDGFE
Protein: Nonribosomal peptide synthetase ivoA (NRPS ivoA) (EC 5.1.-.-) (Ivory mutation-related protein A) (C8V7P4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Nonribosomal peptide synthetase; part of the pathway that mediates the biosynthesis of the gray-brown conidiophore pigment. The first step of the pathway is performed by the nonribosomal peptide synthetase ivoA that catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion. While the stereoinversion is catalyzed by the epimerization (E) domain of ivoA, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a non-canonical C domain function. D-tryptophan is acetylated, probably by an endogenous acetyltransferase (Probable). N-acetyltryptophan is further 6-hydroxylated into N-acetyl-6-hydroxytryptophan (AHT) by the cytochrome P450 monooxygenase ivoC. N-acetyl-6-hydroxytryptophan is substrate of the N-acetyl-6-hydroxytryptophan oxidase ivoB to produce the gray-brown conidiophore pigment.
Interaction partners:
- N-acetyltryptophan 6-hydroxylase ivoC
- N-acetyl-6-hydroxytryptophan oxidase ivoB
Sequence:
MASPIIQPAGAGIHDIFTQLELWESIDKGLSMITILRDNDVLWKPFLQLTLFNQLNIVRKAWSATIQKASESDKVPTLKDVYTSESSFIAQALLDTKNLQITPPATPRTALSGALLAKTIVIFHHSERAQEELGTELPEEVRSLVNQNAICLKVLYNANQWHIDLHYKRDSLSSAQAGEVAEIFEQYLEEALEAVASAIPPSPPVEDDNAGHGGLCKERTDCPKVNRCIHDLIEEQAIARPDQEGICAYDGSLSYAGLSKLSSVLAEQLKTFGARPEQRVAILMNKSFWYPVVVLAVLKSGAAFVPLDPSHPKNRLKQLISEIEPCALITTSVLSELADDLGCPSLAIDSDLTRSKEGSTTALLPNTSASPNNAAYIIFTSGSTGKPKGVVVEHSALSTSAITRGVVLGLGPDSRVLQYAPHTFDVSVDEILTTLIHGGCVCVPSEDDRFSIAHFMESARVTVALLTPTSARTLHPDEVPSLRILQTGGEVLTEDVNDKWSNRVTLFNVYGPTEASVACVISNRTGLKGAGHVLGQAVGGKLWIVDPDDIERHLPDNEVGELVISGAILARGYFRDPSRTESSFVRMRNGERVYRTGDLASMDSAGTIIYHGRKDLEVKIRGQRINIAEIEIAILQCDLVHSVVVEYPRSGLFEKKLVAVLRFEDSSSDAEDGLFGGAKGLTEDIYCLLLSHVSSVLTPAMIPSKWLSLPCVPQMPSGKADRKQVRGWLEDMDKRTYTRIFHPNGTDNLISDPSDSMVAIWLKVLKLEPQSLRLDQSFIRNGGDSIMAMEARHQAHEAGINIDVRELLGSRALQEIGEMATKTSAVEEVSKIEDDRDEPFPLSPVQQMYFDKVSDPSLGLQQRVCVEIMTKIQPDMLREALNHVIQKHRMLAARFTKHMGQWMQQVPFGKNLKHLSRCHIYSQAVGSLGDFCSEPMALEDGTLLHAHLQSSGERQTLVLCVHHLVVDFVSWRVILQDLHDALAAAQNGLPSGISRSTLTFQQWCREQTKYASTLIPEAVLPFAPGPVNLRFWQPSNVQAVSNTYSEIVQHDFRLSSTQTTQMLEKFTTATVHPTDLMLATFALAFKRIFTERDTPTIFIEGHGREPWHASLDVSQTVGWFTAAFPIHLPKDTLLNTTTAILGASERRRSVLANGHPYWACRYLSPNGQKVFGDDPRHQEMEFVFNYAGSIVQRAPGQTLFAENVRIAEIGHPNCERFSLFDIGAAIEMPSSELVVSFTFPKGIAHRERVAELVKTYQELLETAVERDLDLSAKLSSPLVCPADVVRSLEVNGVCIERDVEIVYTPSSIQQHMLWRQSQEPWFYRVQGDWTIEKTTTQSEPVDIDRLSHAWNQVVHRHTTLRTVFRYSSEEERFVAIVLHEVKPAISIIRKGIQTSGSLCRDDDLSPPHRMVLREKDNGSVVCELEFSHTIIDAASRSIVVQDLLDAYDGKLAHRPLDFPPFWEYIRLAQSSTPSARKEELHRAGRVVTLPFQPTHVLSKVPEACKKNEITISSFFMTAWSIVLAKHFVAHNQRVDSTSSQAVAFDYVLSDRSANIPGIESAVGPYIRLPTLETHVKEGVSLKNIARGLHAQCTFQSLSQSTQDGSSLELPSKATALQKYSTLVNIRNSGSDSLDLVSDSGEWKWILQGFSDPWDYDLVFAVNVHAGKVTGWTVEYADGVVEHSAADEIAKDLNDVVERMVCEII
Protein: Ankyrin repeat domain-containing protein 49 (Q9V3Y0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:32750048}. Cell membrane {ECO:0000269|PubMed:32750048}; Peripheral membrane protein {ECO:0000269|PubMed:32750048}; Cytoplasmic side {ECO:0000269|PubMed:32750048}.
Interaction partners:
- Protein Bride of doubletime
Sequence:
MGDYDSDDEKSQVEKLRHAKVPRGMFVSGWDDDADELIEEDKNPQSSIERMILWAVNENRISEVREILKLDADTVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFGADVNAESDGKQTPLHITATVSNCRNTATVLLLDRYIQPRKENNSEELASVIARRTGMSFPIFESGEEAYDCETGLID
Protein: Protein kinase, putative (EC 2.7.11.1) (Q38DC7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mo25-like protein
- EF-hand domain-containing protein
Sequence:
MDDGTGHLLRPHSIIGMGAYGTVFKAFRLAKERAGDEEAWEREGKPVAVKQTIFSEVTEDITVVLKEVSYLSNLQHPNIVTYYTAFTGQGKLESISQAKRTSAELGAPTKEPGSKRNAEGKVPKSSLSFSTEPSLCIVEELVEGASVAKVIKMAAEQSVKQMTEAEIAAVVYDVLQALLYIHEECQLVHRDIKPLNMLLDRNASSVKLCDFGTCADLSQQDGRFTVIGTIGWIAPEVLDSGMMDHRSGHITSHSFPSDVWSLGVSALEMTQVGMTRSALSEYIKDLSVMPCSVQETVTGSRKSFLQEKLPTGHLRDFIACCLRRDPQIRPKVRQLLEHKLIVTSGVANAKERSAKIAGIIAAVTIAGKKKIGNNEKMNDEAIVLPQFADSTLTKNRCMEAVAALKREFFAAQAPLLETSRYSWCTPSHISRMTTSDDFRNLPKPPKLLDPEMSTNAKVSLPSRSSEAAKSLFDAVVVPATVESQRTVLNIVGQYRKLGGVHTSDGWADIDNRAAACYTFEELACKNIKHETFVQLHDDLIRCFKACCMSIPDFEATFLPAFLQALTSPGDLYDVRRFIAYVHQLQRDDLRHTYHGRLDAGDSKRDAARKASCSQQQPPLPNLTAADWMRFPRMPQSMGCIGTSGNIGGDKSDTSTDGLRHQAPLVSPPAYLYNKWLKEKQARAMGPI