wanglab/gogpt-training-data huggingface dataset:
Protein: Sideroflexin fsf1 (Fungal sideroflexin-1) (O13793)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial amino-acid transporter that mediates transport of serine into mitochondria.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8CFD0, ECO:0000255, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein mS43
Sequence:
MSSNKLPTSKYDLSTYWGRVRHAMDITDPRTLLSTSQDLNSAVKTLEDYGAGKIAQLDETVWHAKKIVDSTLHPDTKEPVFLPFRMSCFVLTNLVVTAGMLQPNLGTAGTVFWQWMNQSVNVAFNSANANKSTQLTLPQMTKSYIYAVSASCGVAIGLNKIVPRMNFLSSSSKAVLGRLTPFAAVASAGVLNVFLMRGEELRQGIDVFDKEGESLGKSKKAAFYAVGETALSRVINASPIMVIPPLVLMRLQKQNWLRTRPKLTIPVNLGLITLTSLIALPLAIGVFPAREKISPFKLEPQFHHLKDKSDQPIVEVEFNRGL
Protein: Core-2/I-branching beta-1,6-N-acetylglucosaminyltransferase family protein (Glycosyltransferase) (Q9LIQ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Probable xyloglucan galactosyltransferase GT14
- C-terminal binding protein AN
- Arabinogalactan O-methyltransferase 2
Sequence:
MQHTPEQPRVTLYIILTTAFLSLCFLLSLSSSSQYSSSSYTGRPDDLRPDPRLFPSSSKIAADTAPPSIAYLISGSSGDTRRILRLLYATYHPRNRYLLHLDSLATQSERDRLAVDVQDVPIFRAARNVDVIGKPDFAYQRGSSPMASTLHGASILLRLSGTWDWFVSISVDDYPLVTQDELLHIMSHLPKDLNFVNHTSYIGWKESRKLKPVIVDPGLYLVEKTDMFFASQKRELPKAFKLFSGPSFSILSRNFMEHCVLGTDNFPRTLLMYLSNTPDSLSNYFPTILCNTDTFKKTIMNNNLLYLASNDTSKERYHQLDHKEFTEMVDSGAAFARGFRYDDTVLDRIDHELLGRKPGEVVPGGWCLGDSSKNRSSCSVWGDSGILRPGSGSDRLERRIVELLSNDWFRLHQCVPE
Protein: Kunitz/Bovine pancreatic trypsin inhibitor domain protein (Q18761)
Organism: Caenorhabditis elegans
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- MEC-5
- Degenerin mec-10
- Degenerin mec-4
- Mechanosensory protein 2
- Mechanosensory abnormality protein 6
- Tubulin alpha-3 chain
- Tubulin beta-1 chain
- AMP-binding domain-containing protein
- Band 7 domain-containing protein
- Band 7 domain-containing protein
Sequence:
MFLPPPHKLFPFFLVFLNLVDTKDEPVFVKNNEDICLEDVDPGPCQYYQVQWFWDKQVEECKEFHYGGCMGTKNRFSSKQQCVKQCKYKMFNPVAVPDLCLLDADQGHCGDERNGHWWYFFNQESGECEKFFYYGCGGNDNKFYSLHMCRKVCGERLSPQIACDHCDLRTSFCKSNSKFNYTCECRSGYEKNQYGECIDIDECRGYKAVCDRNAWCVNEIGSYKCECMASYRGDGKHCTYVGLGRSSIDCKDCSMHATCMNGVCQCKEGYEGDGFNCTDVNECLRRPEMCNKNAECINREGSFICTCLEGYAGNGYNCTVSKNSCLDKFDHDYKDTCGNENWRPHFFFNHQTRMCEQFWYDGCRGRSRNIFSEYDTCTTMCEETNVLTRAEVCWDKFDMNYRNQCMNGQWQQRYYFDHASLTCRQFWFDGCRSDSRNIFDDELTCQWLCESQPMYKSRSCLEDFDEGLKKECNGGRWRHQWYFDKGSKKCFSFWYDGCKGANENIFQDELSCLHTCENPAKKDPKKPWHNNDKFKMKEIIGDIYKPNLTDTCLAKNPCKNNGTCIFVWKKDTHYCKCQPGFHGNNCDKVVDYDPCAEKPCLNGATCQIKYNDDDVDEKPTFECFCAAGFGGPKCDQRPCESNPCLNNGTCRTTKGYSTYFCECANGFGGKNCDVSIGNTPPEEKFGKNVEQISSGKEEWIAQMRQRLKETGGGIGGASGSGLKSENGTMGGSSGEKSGEKKSGKNKKSKATQVADEPYKDPATRKREREEREKKEAEIQAAEEEEKQRKEYEEDAQRKKAEEMELEAKKALEAANFGLKTDFSMSLLTILMAFVLREF
Protein: Taste receptor type 2 member 42 (T2R42) (Taste receptor type 2 member 55) (T2R55) (Q7RTR8)
Organism: Homo sapiens (Human)
Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity).
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Taste receptor type 1 member 2
- Taste receptor type 1 member 1
- Taste receptor type 1 member 3
- Extracellular calcium-sensing receptor
Sequence:
MATELDKIFLILAIAEFIISMLGNVFIGLVNCSEGIKNQKVFSADFILTCLAISTIGQLLVILFDSFLVGLASHLYTTYRLGKTVIMLWHMTNHLTTWLATCLSIFYFFKIAHFPHSLFLWLRWRMNGMIVMLLILSLFLLIFDSLVLEIFIDISLNIIDKSNLTLYLDESKTLYDKLSILKTLLSLTSFIPFSLFLTSLLFLFLSLVRHTRNLKLSSLGSRDSSTEAHRRAMKMVMSFLFLFIVHFFSLQVANWIFFMLWNNKCIKFVMLALNAFPSCHSFILILGNSKLQQTAVRLLWHLRNYTKTPNPLPL
Protein: Large ribosomal subunit protein uL15m (39S ribosomal protein L15, mitochondrial) (L15mt) (MRP-L15) (Q9P015)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL2m
- Small ribosomal subunit protein uS5m
Sequence:
MAGPLQGGGARALDLLRGLPRVSLANLKPNPGSKKPERRPRGRRRGRKCGRGHKGERQRGTRPRLGFEGGQTPFYIRIPKYGFNEGHSFRRQYKPLSLNRLQYLIDLGRVDPSQPIDLTQLVNGRGVTIQPLKRDYGVQLVEEGADTFTAKVNIEVQLASELAIAAIEKNGGVVTTAFYDPRSLDIVCKPVPFFLRGQPIPKRMLPPEELVPYYTDAKNRGYLADPAKFPEARLELARKYGYILPDITKDELFKMLCTRKDPRQIFFGLAPGWVVNMADKKILKPTDENLLKYYTS
Protein: Mitochondrial division protein 1 (Mitochondria fission 2 protein) (P47025)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:11038180, ECO:0000269|PubMed:11038182, ECO:0000269|PubMed:11038183, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:16823961}; Peripheral membrane protein {ECO:0000269|PubMed:11038180, ECO:0000269|PubMed:11038182, ECO:0000269|PubMed:11038183, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:16823961}; Cytoplasmic side {ECO:0000269|PubMed:11038180, ECO:0000269|PubMed:11038182, ECO:0000269|PubMed:11038183, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:16823961}. Note=Uniformly distributed on the cytoplasmic face of the mitochondrial outer membrane. This localization is dependent on FIS1. Reorganizes to punctate structures on mitochondria, corresponding to mitochondrial constriction sites, at a late step in mitochondrial division. This relocalization is dependent on DNM1.
Interaction partners:
- Mitochondrial fission 1 protein
- CCR4-associated factor 4
- Dynamin-related protein DNM1
- Mitofusin FZO1
- Dynamin-like GTPase MGM1, mitochondrial
- Cytosolic iron-sulfur protein assembly protein 1
- Mitochondrial fusion and transport protein UGO1
Sequence:
MSVNDQITHIGKTLSTTASAFLNYQKSNSNTQDVLTNNGPYKNLLSNTVNNASSTSYFYKRTEHGRFVKNASNTFEDIYSKTRRGDVFRNKFTDNKTCFRMLTYISDDLLNEIPTKEGLKSDADGKLLTEGGENENLRKNASKKETSLFQGFKSYLPIAELAIENTERLNYDTNGTSGTVGAKDVMSKTNERDEIHTELPNFQDSFLIPPGVETKKISSSYSPSALKSFSQTLVNSLEFLNIQKNSTLSEIRDIEVEVENLRQKKEKLLGKIANIEQNQLLLEDNLKQIDDRLDFLEEYGLEVIEANSDENAEDDGMSERKALKNDAIRNEGVTTESISSEASNLPPRRRQQLRDDNSLNRLGAFYSKSKKRHRKSFPTFQQLYEPGTKIGSIMSTHDDFLTCLDFDAPFGTLCTAGYLDHTVKIWDLSKQNKIGELAGHLATINCMQINRDYGTLVTGGRDAALKLWNLNLAQQLYQETQNLTSPTNHIDSPCVHTFEAHTDEVTALSLDPSFLVSGSQDRTIRQWDLRSGKCLQTIDLSFANVLTTSTNVDLSKSTLLTQRNERPSIGALQSFDAALATGTKDGVVRLWDLRSGKVIRTLKGHTDAITSLKFDSACLVTGSYDRTVRIWDLRTGLLNKFHAYSAPVLSLDLFQENAAVVVADEPSVQIYDSEKDESWSCVEQGNETSVSTVKYKENYMVEGRENGDVNIWAV
Protein: ELAV-like protein (A0A2R8QTX4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Pabpn1 protein
- Aly/REF export factor.
- Heterogeneous nuclear ribonucleoprotein C
Sequence:
MAVRRGHIRYLKVCEVQNQGNDRDSHKGASSIKQEVYDMPNGYEDPMGDEPSDAKTNLIINYLPQNMSQEELRSLFSSIGEVESAKLIRDKMAGHSLGYGFVNYVNPSDAERAINTLNGLRLQSKTIKVSYARPSSDGIKDANLYISGLPKTMTQKNVEDMFTQYGRIINSRILVDQASGLSRGVAFIRFDKRSEAEEAIKDLNGSKPSGASEPITVKFAANPNQSKNSQLLSQLYHTQSRRFGGPVHHQPQRFRFSPMSVDHSVSSMNVASSSSSGWCIFVYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTSKCKGFGFVTMTNYEEAAMAISSLNGYRLGDKVLQVSFKSSKSHK
Protein: Retinol dehydrogenase (EC 1.1.1.300) (D3Z6W3)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|PIRNR:PIRNR000095}.
Interaction partners:
- Lecithin retinol acyltransferase
- Cytochrome P450 26A1
- Beta,beta-carotene 15,15'-dioxygenase
- All-trans-retinol 13,14-reductase
- Aldehyde dehydrogenase, cytosolic 1
- Retinal-specific phospholipid-transporting ATPase ABCA4
- Retinal dehydrogenase 2
- Retinaldehyde dehydrogenase 3
- Aldehyde dehydrogenase 1A1
- Retinol dehydrogenase 12
Sequence:
MASQQRTVLISGCSSGIGLELALQLAHDPRQRYQVVATMRDLGKKEPLEAAAGEALGKTLSVVQLDVCNDESVTDCLSHIEGGQVDVLVNNAGVGLVGPLEGLSLATMQSVFNTNFFGAVRLVKAVLPGMKRRRQGHIVVVSSVMGLQGVMFNDVYAASKFALEGFFESLAIQLRQFNIFISMVEPGPVTTDFEGKLLAQVSKAEFPDTDPDTLGYFRDLYLPASRELFRSVGQSPRDVAQVIAKVIGTTRPPLRRQTNTRYLPLTALKAMDPSGSLYVKTAHRLLFRWPHLLNLGLRCLACGCLPTRVWPRQTEQN
Protein: Uncharacterized protein (Q38B49)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRSFVVAPVVATACSLSTPIRTIIACKGIVENRITKHYSNRTVEEAKAAREAQIAKAKHPNPRNRKEELSHLTHHCSYEYVPEFQRWANDMLAVYSDPHGYGHDMAYHYHRIWKAKSPTRRGIEDGSGAFDVCKIHPK
Protein: Glucose-6-phosphate 1-epimerase (EC 5.1.3.15) (Q5A1Q0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- phosphoglucomutase
- Glucose-6-phosphate isomerase
- Phosphoribomutase
- Phosphotransferase
- Hexokinase-2
- N-acetylglucosamine kinase 1
- Phosphotransferase
- Transketolase
- Transaldolase
- Glucose-6-phosphate 1-dehydrogenase
Sequence:
MPVEELEDRVIITDPNDSTNRATILKFGATVVSWKNNNQEKLWLSEGAHLDGSKAVRGGIPLVFPVFGKQKDSNHPTFKLPQHGFARNSTWEFLGQTQESPITVQFGLGPENVDPETLKLWNYDFTLILTVSLTKDKLVTSIDVENTGKEAFEFNWLFHTYYRIHDITDTLVTNLIDQQCYDQLIGESYIEKAPVISFHEEFDRIYSKVSLEKSIQVVDKGQVLFNLHRKNLPDSVVWNPWTKKAEGMADFQPKSGFHQMVCVEPGHVNSMVSLPAGGKWSGGQEITIGGEIKVQANIY
Protein: Large ribosomal subunit protein eL42B (60S ribosomal protein L42-B) (L41) (Maintenance of killer protein 18) (YL27) (YP44) (P0CX28)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
Sequence:
MVNVPKTRKTYCKGKTCRKHTQHKVTQYKAGKASLFAQGKRRYDRKQSGFGGQTKPVFHKKAKTTKKVVLRLECVKCKTRAQLTLKRCKHFELGGEKKQKGQALQF
Protein: tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD) (tRNA threonylcarbamoyladenosine biosynthesis protein TsaD) (O05518)
Organism: Bacillus subtilis (strain 168)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB; this reaction does not require ATP in vitro. TsaD likely plays a direct catalytic role in this reaction.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445}.
Interaction partners:
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaE
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaB
- Putative [ribosomal protein bS18]-alanine N-acetyltransferase
- Threonylcarbamoyl-AMP synthase
- Thiamine-monophosphate kinase
- Phenylalanine--tRNA ligase alpha subunit
- Uncharacterized protein YycS
- Uncharacterized protein YwcI
- Ribosomal RNA large subunit methyltransferase H-methyltransferase)
- tRNA-specific 2-thiouridylase MnmA
Sequence:
MSEQKDMYVLGIETSCDETAAAIVKNGKEIISNVVASQIESHKRFGGVVPEIASRHHVEQITLVIEEAFRKAGMTYSDIDAIAVTEGPGLVGALLIGVNAAKALSFAYNIPLVGVHHIAGHIYANRLVEDIVFPALALVVSGGHTELVYMKEHGSFEVIGETLDDAAGEAYDKVARTMGLPYPGGPQIDKLAEKGNDNIPLPRAWLEEGSYNFSFSGLKSAVINTLHNASQKGQEIAPEDLSASFQNSVIDVLVTKTARAAKEYDVKQVLLAGGVAANRGLRAALEKEFAQHEGITLVIPPLALCTDNAAMIAAAGTIAFEKGIRGAYDMNGQPGLELTSYQSLTR
Protein: Cyclo(L-leucyl-L-leucyl) synthase (EC 2.3.2.22) (Cyclodileucine synthase) (Cyclodipeptide synthase) (CDPS) (O34351)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the biosynthesis of pulcherrimin, a red extracellular pigment. It uses activated amino acids in the form of aminoacyl-tRNAs (aa-tRNAs) as substrates to catalyze the ATP-independent formation of cyclodipeptides which are intermediates in diketopiperazine (DKP) biosynthetic pathways. Catalyzes the formation of cyclo(L-Leu-L-Leu) (cLL) from L-leucyl-tRNA(Leu). Can also incorporate various nonpolar residues, such as L-phenylalanine, L-leucine and methionine, into cyclodipeptides.
Interaction partners:
- Pulcherriminic acid synthase
- Uncharacterized MFS-type transporter YvmA
- HTH-type transcriptional regulator PchR
- Uncharacterized HTH-type transcriptional regulator YvnA
- Uncharacterized protein YvnB
Sequence:
MTGMVTERRSVHFIAEALTENCREIFERRRHVLVGISPFNSRFSEDYIYRLIGWAKAQFKSVSVLLAGHEAANLLEALGTPRGKAERKVRKEVSRNRRFAERALVAHGGDPKAIHTFSDFIDNKAYQLLRQEVEHAFFEQPHFRHACLDMSREAIIGRARGVSLMMEEVSEDMLNLAVEYVIAELPFFIGAPDILEVEETLLAYHRPWKLGEKISNHEFSICMRPNQGYLIVQEMAQMLSEKRITSEG
Protein: Uncharacterized protein C343.20 (Q9C111)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Glucan 1,3-beta-glucosidase 1
Sequence:
MKVTMLPLQLNDEINSASFGPASSSTSHSSTIFCVHHRVRYIYVPRHCLLRSLTYATTNFTKFSKFVYYLAITLHTSLLTKLIYCHADLYALQSIKYKRLRINNGMLDSPKRE
Protein: Rho GTPase activating protein at 16F, isoform E (X2JCF3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI17823p1
- Rho GTPase activating protein at 15B, isoform C
- Rho GTPase-activating protein 92B
- Rho GTPase-activating protein 39
- Rho GTPase-activating protein 190
- Rho GTPase activating protein at 71E, isoform D
Sequence:
MQTTTSQRPVTPGTPDSAHIVIGAAGFVAHERRQPGKTLMNCFRDRSTTSSSSSQAQHAYVRGHSVTSSTLFRLEGSGGSNCTLDKAGKQDTGRPEAVVLLRELKTRPNKLALLKSSSSKDLTRLFLDDSTNTAVLVSNTSIDVCSSNSSSGGSPAVGRSKSGRDRRNGLECCSSCSKRWHDLKQRMHTLEQDLLVQTTYSQELEQKVGEMSRQLTELLQERDRERDKDKARFAAAGGVAAPGKRTAHGSPNVRPSRLVAWMNLSNWFKSRPSVETLREQRIFFDEPCFDTELEMVLKHDQHRTVPRIVVDCCDLIEQKYRRSTQPIEGIYRQCGDYNKIQTLRFSIDANDYDSLRQPDVDIHTLTGVLKLFLREIKSPLVRVNEAKTFIGQPNQWLLTDLSAKLDSLKRLIRSLPESNRDTMDYIFGHFNRITKVPLQQISAETLSISVTPSIFHTVPQGVHMQDIQQLLREGETLADCVKLMIEYQGRIFDRLRLIQTAHLLCRCVERFANHSKSEILNPKPNTPLYLPHLYTHSRFAPESVSNPDHIVYRCTADRRRLSMRNLKKTLSQPDLLFHNLF
Protein: Sepiapterin reductase (SPR) (EC 1.1.1.153) (Q64105)
Organism: Mus musculus (Mouse)
Function: Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.
Subcellular location: Cytoplasm.
Interaction partners:
- 6-pyruvoyl tetrahydrobiopterin synthase
- Dihydropteridine reductase
- Phenylalanine-4-hydroxylase
- Dihydrofolate reductase
- Tyrosine 3-monooxygenase
- Aldo-keto reductase family 1 member B1
- Tryptophan 5-hydroxylase 2
- Tryptophan 5-hydroxylase 1
- Carbonyl reductase 1])
- GTP cyclohydrolase 1
Sequence:
MEADGLGCAVCVLTGASRGFGRALAPQLARLLSPGSVMLVSARSESMLRQLKEELGAQQPDLKVVLAAADLGTEAGVQRLLSAVRELPRPEGLQRLLLINNAATLGDVSKGFLNVNDLAEVNNYWALNLTSMLCLTSGTLNAFQDSPGLSKTVVNISSLCALQPYKGWGLYCAGKAARDMLYQVLAAEEPSVRVLSYAPGPLDNDMQQLARETSKDPELRSKLQKLKSDGALVDCGTSAQKLLGLLQKDTFQSGAHVDFYD
Protein: High mobility group 20B (C9JQA7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSHGPKQPGAAAAPAGGKAPGQHGGFVVTVKQERGEGPRAGEKGSHEEEPVKKRGWPKGKKRKKILPNGPKAPVTGYVRFLNERREQIRTRHPDLPFPEITKMLGAEWSKLQPTEKQRYLDEAEREKQQYMKELRAYQQSEA
Protein: Neurensin-2 (Q5HZK2)
Organism: Mus musculus (Mouse)
Function: May play a role in maintenance and/or transport of vesicles.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSCSRPCVCSHGTSVEESTWYGFDFYPNLFYNDWLGTTTLPYNPERIPIRYINRPWPSLCWKVTVAVASLFLLLGVAALTTGYAVPPKLELVNESKFSSMEDPVADYNQALMTCRVVGATLCGVAGIMLAVCLFLIASGWMFQDIKAEPLVTETDSPVEVFRDEPEKLSPAFHETSSQSPFLTPPSPFGQQSVQTSQPQRDL
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (F1P3H0)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Bone morphogenetic protein 4
- Bone morphogenetic protein 7.
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein 2
- Bone morphogenetic protein 6.
- Mothers against decapentaplegic homolog 5
- BMP5
- Growth/differentiation factor 5
- Mothers against decapentaplegic homolog.
- Mothers against decapentaplegic homolog
Sequence:
MTRLRVCERLLGAYLLIILHVQGQNLDSMLHGTGMKTNPDQKKQGNGVTLAPEDTLPFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDEHGEPTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTDFCNQDLQPTLPPLDSTDGLFDGSIRWMAVLISMAVCIIVMIILFSCFCYKHYCKSMAKRHCYNRDLEQDEAFIPAGESLKDLIDQSQSSGSGSGLPLLVQRTIAKQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFLKCTTLDNRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCVTGGIVEEYQLPYYDMVPNDPSYEDMREVVCVKRLRPVVSNRWNSDECLRAILKLMSECWAHNPASRLTALRIKKTLAKMVESQDVKI
Protein: Essential MCU regulator, mitochondrial (Single-pass membrane protein with aspartate-rich tail 1, mitochondrial) (Q9H4I9)
Organism: Homo sapiens (Human)
Function: Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria. Required to bridge the calcium-sensing proteins MICU1 and MICU2 with the calcium-conducting subunit MCU. Plays a central role in regulating the uniplex complex response to intracellular calcium signaling. Acts by mediating activation of MCU and retention of MICU1 to the MCU pore, in order to ensure tight regulation of the uniplex complex and appropriate responses to intracellular calcium signaling.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:24231807, ECO:0000269|PubMed:26774479, ECO:0000269|PubMed:27099988, ECO:0000269|PubMed:27642048, ECO:0000269|PubMed:31080062}; Single-pass membrane protein {ECO:0000269|PubMed:24231807, ECO:0000269|PubMed:27099988, ECO:0000269|PubMed:31080062}. Note=MAIP1 is required to assist sorting of EMRE/SMDT1 into mitochondrion by protecting EMRE/SMDT1 against protein degradation by YME1L1, thereby ensuring SMDT1/EMRE maturation by the mitochondrial processing peptidase (PMPCA and PMPCB) (PubMed:27642048). {ECO:0000269|PubMed:27642048}.
Interaction partners:
- Calcium uptake protein 2, mitochondrial
- Calcium uniporter protein, mitochondrial
- Calcium uniporter regulatory subunit MCUb, mitochondrial
- Calcium uptake protein 1, mitochondrial
- Calcium uptake protein 3, mitochondrial
- Mitochondrial calcium uniporter regulator 1
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- m-AAA protease-interacting protein 1, mitochondrial
- Mitochondrial inner membrane m-AAA protease component paraplegin
Sequence:
MASGAARWLVLAPVRSGALRSGPSLRKDGDVSAAWSGSGRSLVPSRSVIVTRSGAILPKPVKMSFGLLRVFSIVIPFLYVGTLISKNFAALLEEHDIFVPEDDDDDD
Protein: Leptin (Obesity factor) (G8BLB4)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR001837}.
Interaction partners:
Sequence:
MRCGPLYRFLWLWPYLSYVEAVPICKVQDDTKTLIKTIVTRINDISHTQSVSSKQRVTGLDFIPGLHPLLSLSKMDQTLAIYQQILTSLPSRNVVQISNDLENLRDLLHLLAASKSCPLPQVRALESLESLGVVLEASLYSTEVVALSRLQGSLQDMLRQLDLSPGC
Protein: Peptidyl-prolyl cis-trans isomerase B (PPIase B) (EC 5.2.1.8) (CYP-S1) (Cyclophilin B) (Rotamase B) (S-cyclophilin) (SCYLP) (P23284)
Organism: Homo sapiens (Human)
Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding.
Subcellular location: Virion {ECO:0000269|PubMed:20147391}. Note=(Microbial infection).; SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:1530944}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). {ECO:0000269|PubMed:17081065}.
Interaction partners:
- Prolyl 3-hydroxylase 1
- Cartilage-associated protein
- Basigin
- Protein disulfide-isomerase A4
- Endoplasmin
- Calreticulin
- Guided entry of tail-anchored proteins factor CAMLG
- Protein disulfide-isomerase
- DnaJ homolog subfamily B member 11
- Endoplasmic reticulum chaperone BiP
Sequence:
MLRLSERNMKVLLAAALIAGSVFFLLLPGPSAADEKKKGPKVTVKVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVIIADCGKIEVEKPFAIAKE
Protein: Cytochrome b (Complex III subunit 3) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Ubiquinol-cytochrome-c reductase complex cytochrome b subunit) (P0C523)
Organism: Oryza sativa subsp. indica (Rice)
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00163}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00163}.
Interaction partners:
Sequence:
MTIRNQRFSLLKQPIYSTLNQHLIDYPLPSILSYWWGFGSLAGICLVIQIVTGVFLAMNYTPHVDLAFNSVEHIMRDVEGGWLLRYMHANGASMFFIVVYLHIFRGLYYASYSSPREFVWCLGVVIFLLMIVTAFIGYVLPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNATLNRFFSLHYLLPFILVGASLLHLAALHQYGSNNPLGVHSEMDKIAFYPYFYVKDLVGWVAFAIFFSIWIFFAPNVLGHPDNYIPANPMSTPPHIVPEWYFLPIYAILRSIPDKAGGVAAIALVFISLLALPFFKEMYVRSSSFRPIYQGIFWLLLADCLLLGWIGCQPVEAPFVTIGQISSFFFFLFFAITPILGRVGRGIPKYYTDETHRTGSFS
Protein: Zinc finger and BTB domain containing 1 (G3V447)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAKPSHSSYVLQQLNNQREWGFLCDCCIAIDDIYFQAHKAVLAACSSYFRMFFMNHQHSTAQLNLSNMKISAECFDLILQFMYLGKIMTAPSSFEQFKVAMNYLQLYNVPDCLEDIQDADCSSSKCSSSASSKQNSKMIFGVRMYEDTVARNGNE
Protein: Corazonin receptor, isoform B (M9PF00)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Pro-corazonin
- Adipokinetic hormone
Sequence:
MEDEWGSFDRLPSVPSASMDLETENEVVSNWSTLANFTRLVAGAAPEIVNYTLNMIDVGVGMATDISNLSVSTTPLPAYAISNSSSLAHTNSRHEAPPMAEQVPEHVMDHAPQLSRSGLLKVYVLAVMALFSLLGNLLTIWNIYKTRISRRNSRHTWSAIYSLMFHLSIADVLVTWFCIIGEAAWCYTVQWLANELTCKLVKLFQMFSLYLSTYVLVLIGVDRWIAVKYPMKSLNMAKRCHRLLGGTYILSLVLSLPQFFIFHVARGPFVEEFYQCVTHGFYTADWQEQMYATFTLVFTFLLPLCILFGTYMSTFRTISSSEKMFQGSKLANYSTAKLPTQTNRQRLIHKAKMKSLRISVVIIIAFLICWTPYYVMMIMFMFLNPDKRLGDDLQDAIFFFGMSNSLVNPLIYGAFHLCPGKGGKSSGGGGNNNAYSLNRGDSQRTPSMLTAVTQVDGTGGSSRQMRAFRQQSYYRSSSNGTAGPGAAPFKEQVGLLHVGPGNGTPGGSVSSGATPQLIRKGSALLARQPSCLREQEHQQRLLLHEKPSTLVLSYDSQRGGVGVGVASGLLDNNERVSSVXEQLAMAVAAAAVAVDAPDTVEAAAATASADADANVAMEDACSCCHCLSRELVRRQLELQVLPVQ
Protein: Peroxiredoxin (EC 1.11.1.15) (Q8IJD0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- indole-3-glycerol-phosphate synthase
Sequence:
MAQLAENTVLDESIQKVEVLNHNGETTSFYNEVEKHKENNEGIVVFTYPKANTPGCTKQAELFKEKHEEFVNNKYVVYGLSADTAEDQLKWKEKLELPYELLCDVDKNLLKLLGLTNEEDKTIRSHLVLKNDFTVSYVKKSVSPGKSATQVLNFLVNGDDGGDGNEEEENEENNNNEDKDNNENDEEGDVQGEGEGEGEGDEEKTADTDKEKPKKSSTSTQKKKGSVSSTISKKSVKKSNKVVKKNVKVKKEIKKKTNKKADNKKGKNVNNKLMKSNAKGANKKGGKKNSVVKKEDNKKKGKNNKKKNKNQNLKDLKKKNVKSGKGSVSSSNKKLPKGLKNAAKKAGKKIDKKKEQANKKNNNNKNKNKNKNLSKGNNMKHNKKPAKKVVKKK