wanglab/gogpt-training-data huggingface dataset:
Protein: Molybdopterin molybdenumtransferase 1 (MPT Mo-transferase 1) (EC 2.10.1.1) (P9WJQ7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
Interaction partners:
- Probable molybdenum cofactor guanylyltransferase
- Molybdopterin synthase catalytic subunit 1
- MobA-like NTP transferase domain-containing protein
- Molybdopterin molybdenumtransferase 2
- Probable molybdopterin biosynthesis Mog protein
- MobA-like NTP transferase domain-containing protein
- MoaB/Mog domain-containing protein
- Cyclic pyranopterin monophosphate synthase 2
- Cyclic pyranopterin monophosphate synthase 3
- Cyclic pyranopterin monophosphate synthase 1
Sequence:
MRSVEEQQARISAAAVAPRPIRVAIAEAQGLMCAEEVVTERPMPGFDQAAIDGYAVRSVDVAGVGDTGGVQVFADHGDLDGRDVLTLPVMGTIEAGARTLSRLQPRQAVRVQTGAPLPTLADAVLPLRWTDGGMSRVRVLRGAPSGAYVRRAGDDVQPGDVAVRAGTIIGAAQVGLLAAVGRERVLVHPRPRLSVMAVGGELVDISRTPGNGQVYDVNSYALAAAGRDACAEVNRVGIVSNDPTELGEIVEGQLNRAEVVVIAGGVGGAAAEAVRSVLSELGEMEVVRVAMHPGSVQGFGQLGRDGVPTFLLPANPVSALVVFEVMVRPLIRLSLGKRHPMRRIVSARTLSPITSVAGRKGYLRGQLMRDQDSGEYLVQALGGAPGASSHLLATLAEANCLVVVPTGAEQIRTGEIVDVAFLAQHG
Protein: Choline kinase (Phosphotransferase) (Q93MI3)
Organism: Streptococcus pneumoniae
Interaction partners:
Sequence:
MEKIIKEKISSLLSQEEEVLSVEQLGGMTNQNYLAKTTNKQYIVKFFGKGTEKLINRQDEKYNLELLKDLGLDVKNYLFDIEAGIKVNEYIESAITLDSTSIKTKFDKIAPILQTIHTSAKELRGEFAPFEEIKKYESLIEEQIPYANYESVRNAVFSLEKRLADLGVDRKSCHIDLVPENFIESPQGRLYLIDWEYSSMNDPMWDLAALFLESEFTSQEEETFLSHYESDQTPVSHEKIAIYKILQDTIWSLWTVYKEEQGEDFGDYGVNRYQRAVKGLASYGGSDEK
Protein: Indolepyruvate oxidoreductase subunit IorA (IOR) (EC 1.2.7.8) (Indolepyruvate ferredoxin oxidoreductase subunit alpha) (Q72AP1)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Indolepyruvate ferredoxin oxidoreductase, beta subunit, putative
- Nif-specific regulatory protein
- ACT domain protein
- Aldehyde:ferredoxin oxidoreductase, tungsten-containing
Sequence:
MSHPLLADTPGERHLLLGNEAIVRGALEAGINVVTCYPGTPSSEVPDTFRRIGGDGRYRLEYSVNEKVALEVGAGAALAGALTLVTMKHVGVNVAADPLLTMTYTGLPGGLVLLSADDPGCHSSQNEQDNRTYARFAGMPCFEPATAQEAKDMAREALLLSRETQQPVLLRTTTRVNHLRGGVTYGALPEPAAVVPFERNPRRFVPVPAVARARHFAQADVLGRVAELASASPWNTVHGEGRIGVIASGISRAYLADALHERGLEGRVKVLELGFTWPLPERLLVDFLSGCDKVLVLEELEPLLERDVRALVQRLGLGVDVTGKGGVLTVFGEYSTTIVGDALSAFLGETPAAPVQCSPDAASMELPMRPPNLCAGCSHRAVYYAVRKVFGDDAYYSSDIGCYTLGLLPPLSMADFLFCMGSSISSGSGFAAASGRPVVAYIGDSTFFHSGITGLANALFNKHDVLVVILDNGTTAMTGHQPNPGVDAAVLGDACLHLDIEAIVRGCGVEQVATVHPYNLKATMAALEDMKQRTGVRVIIAQEPCVLYARRTLKKAARQTAYVAEQGPEVEACLAELACPAFRRDGQDIAIDSEQCSGCMVCLQVSSKIKARKRSA
Protein: MFS domain-containing protein (G5ECR3)
Organism: Caenorhabditis elegans
Interaction partners:
- GRIP domain-containing protein
- Choline kinase B2
- Arf-GAP domain-containing protein
Sequence:
MTIERATRQNVRRGRPPGTRRAVVFDDTPQPSEWRNIWVAICGFYILFAETGVRQVMNGFVEPVIKTYNCTKDQADTAVLVVPMASSLILGPFCSIFYQRSGARISIIAGSFLTGGSFVVGPFCKNIYLLMLATFGMGIGCGLMRNSIISIQCEYFKKKRNTVMAAISIGPGLGIFILPRTLKFIMVKYNSWGPAWWFLSLFYIVSAIMGLFITKPPSEQTSTFSFGSAFKVCKKLEFDLHLIACFFASSVMFIYIANILILMESENIEDKEILYGYQGLTSIAGKFVLTFVMSLNKVHNGIIMILSYVIAQLSLSAAAFCYKFWQFRLQNAFAGIGIGLYQACLAPFLVALVGPSQLAYALGFTNLINGVSIISGVWISGFASKGTTGDHARSAFFVSIWLGLAAIVMSIATSSVLMAREKHKRKPSMKQMKHSSELNALTNITSVENS
Protein: Mitochondrial 2-methylisocitrate lyase (Methylisocitrate lyase) (EC 4.1.3.30) (Q9P6J1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA. Does not act on isocitrate (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Aconitate hydratase, mitochondrial
- Probable citrate synthase, mitochondrial
- Putative 2-hydroxyacid dehydrogenase UNK4.10
- D-amino-acid oxidase
- Peroxisomal ATPase pex6
- Malate dehydrogenase, mitochondrial
- Probable acetyl-coenzyme A synthetase
- Fructose-1,6-bisphosphatase
- Aconitase-ribosomal protein bL21m fusion protein
- Ureidoglycolate lyase
Sequence:
MTTDMDLEQLEYEKEVEEIEKWWATPKQSQIKRPYTASTVAVLSEVTKAYYPSSQQALKLYDLLREHRNKGTATLTYGVVDPVLASQASKAGLETIFVSGCLCGLSSVDEPGMDHADYPWDTVPKAVDRIFRSQNWHARRQKQFHLMKPAEERKQLPKYDYLLPIIADGDMGFGSVTSTMKMTKRFVESGVAMIHLDDLAIGLKRFTVGQGRTVVPTSEYLRRLTAVRLQFDIMKAETMLLCRCDTDHAEFITSVVDPRDHAYVLGATTKIESLIKALKDAESTGVSMKKARENWIERAKLMTFDEAVKSTATPKEYENYISAISKKPFHSISERQELAEKYLSNEVFFDWELPRSSDGQYFFKPTVQTVIERAIAAAPLGEMTWARMDYPKWQDIKAFHEGVRAVYPDRMFAFGFTGNYDFKAAGFSEEQLRNLTSDMAKLGVCWQVQPYFTCQVLNKASVDYSNIWKKDGIFGYVKTVQEPALKEDVDGFENEWCGTYFADKLLSAAGSSDKTIPY
Protein: AT-hook motif nuclear-localized protein 12 (Q8LPN5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8VYJ2}.
Interaction partners:
- Dof zinc finger protein DOF5.7
- WUSCHEL-related homeobox 13
Sequence:
MDGREAMAFPGSHSQYYLQRGAFTNLAPSQVASGLHAPPPHTGLRPMSNPNIHHPQANNPGPPFSDFGHTIHMGVVSSASDADVQPPPPPPPPEEPMVKRKRGRPRKYGEPMVSNKSRDSSPMSDPNEPKRARGRPPGTGRKQRLANLGEWMNTSAGLAFAPHVISIGAGEDIAAKVLSFSQQRPRALCIMSGTGTISSVTLCKPGSTDRHLTYEGPFEIISFGGSYLVNEEGGSRSRTGGLSVSLSRPDGSIIAGGVDMLIAANLVQVVACSFVYGARAKTHNNNNKTIRQEKEPNEEDNNSEMETTPGSAAEPAASAGQQTPQNFSSQGIRGWPGSGSGSGRSLDICRNPLTDFDLTRG
Protein: Molybdopterin synthase sulfur carrier subunit (Q7D640)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MIKVNVLYFGAVREACDETPREEVEVQNGTDVGNLVDQLQQKYPRLRDHCQRVQMAVNQFIAPLSTVLGDGDEVAFIPQVAGG
Protein: Protein BEX1 (Brain-expressed X-linked protein 1 homolog) (Reduced expression protein 3) (REX-3) (Q9R224)
Organism: Mus musculus (Mouse)
Function: Signaling adapter molecule involved in p75NTR/NGFR signaling. Plays a role in cell cycle progression and neuronal differentiation. Inhibits neuronal differentiation in response to nerve growth factor (NGF). May act as a link between the cell cycle and neurotrophic factor signaling, possibly by functioning as an upstream modulator of receptor signaling, coordinating biological responses to external signals with internal cellular states (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12911636}. Cytoplasm {ECO:0000269|PubMed:12911636}. Note=Shuttles between the cytoplasm and the nucleus. Predominantly nuclear. {ECO:0000269|PubMed:12911636}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 16
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Calmodulin-4
- Calmodulin 5
- Protein BEX3
- Olfactory marker protein
Sequence:
MESKDQGVKNLNMENDHQKKEEKEEKPQDTIRREPAVALTSEAGKNCAPRGGRRRFRVRQPIAHYRWDLMQRVGEPQGRMREENVQRFGGDVRQLMEKLRERQLSHSLRAVSTDPPHHDHHDEFCLMP
Protein: Inositol polyphosphate 5-phosphatase OCRL (EC 3.1.3.36) (EC 3.1.3.56) (Inositol polyphosphate 5-phosphatase OCRL-1) (OCRL-1) (Lowe oculocerebrorenal syndrome protein) (Phosphatidylinositol 3,4,5-triphosphate 5-phosphatase) (EC 3.1.3.86) (Q01968)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of the 5-position phosphate of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol-3,4,5-bisphosphate (PtdIns(3,4,5)P3), with the greatest catalytic activity towards PtdIns(4,5)P2. Able also to hydrolyze the 5-phosphate of inositol 1,4,5-trisphosphate and of inositol 1,3,4,5-tetrakisphosphate. Regulates traffic in the endosomal pathway by regulating the specific pool of phosphatidylinositol 4,5-bisphosphate that is associated with endosomes. Involved in primary cilia assembly. Acts as a regulator of phagocytosis, hydrolyzing PtdIns(4,5)P2 to promote phagosome closure, through attenuation of PI3K signaling.
Subcellular location: Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:D3ZGS3}. Early endosome membrane {ECO:0000269|PubMed:21971085, ECO:0000269|PubMed:25869668}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:25869668}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:22543976}. Cell projection, cilium {ECO:0000269|PubMed:22543976}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:D3ZGS3}. Endosome {ECO:0000269|PubMed:21971085, ECO:0000269|PubMed:25869668}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:D3ZGS3}. Lysosome {ECO:0000269|PubMed:9430698}. Note=Also found on macropinosomes (PubMed:25869668). Colocalized with APPL1 on phagosomes (PubMed:22072788). {ECO:0000269|PubMed:22072788, ECO:0000269|PubMed:25869668}.
Interaction partners:
- Ras-related protein Rab-8A
- Sesquipedalian-1
- Type II inositol 1,4,5-trisphosphate 5-phosphatase
- DCC-interacting protein 13-alpha
- Ras-related protein Rab-5A
- Ras-related protein Rab-6A
- Inositol polyphosphate-4-phosphatase type I A
- Clathrin heavy chain 1
- Ras-related protein Rab-35
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
Sequence:
MEPPLPVGAQPLATVEGMEMKGPLREPCALTLAQRNGQYELIIQLHEKEQHVQDIIPINSHFRCVQEAEETLLIDIASNSGCKIRVQGDWIRERRFEIPDEEHCLKFLSAVLAAQKAQSQLLVPEQKDSSSWYQKLDTKDKPSVFSGLLGFEDNFSSMNLDKKINSQNQPTGIHREPPPPPFSVNKMLPREKEASNKEQPKVTNTMRKLFVPNTQSGQREGLIKHILAKREKEYVNIQTFRFFVGTWNVNGQSPDSGLEPWLNCDPNPPDIYCIGFQELDLSTEAFFYFESVKEQEWSMAVERGLHSKAKYKKVQLVRLVGMMLLIFARKDQCRYIRDIATETVGTGIMGKMGNKGGVAVRFVFHNTTFCIVNSHLAAHVEDFERRNQDYKDICARMSFVVPNQTLPQLNIMKHEVVIWLGDLNYRLCMPDANEVKSLINKKDLQRLLKFDQLNIQRTQKKAFVDFNEGEIKFIPTYKYDSKTDRWDSSGKCRVPAWCDRILWRGTNVNQLNYRSHMELKTSDHKPVSALFHIGVKVVDERRYRKVFEDSVRIMDRMENDFLPSLELSRREFVFENVKFRQLQKEKFQISNNGQVPCHFSFIPKLNDSQYCKPWLRAEPFEGYLEPNETVDISLDVYVSKDSVTILNSGEDKIEDILVLHLDRGKDYFLTISGNYLPSCFGTSLEALCRMKRPIREVPVTKLIDLEEDSFLEKEKSLLQMVPLDEGASERPLQVPKEIWLLVDHLFKYACHQEDLFQTPGMQEELQQIIDCLDTSIPETIPGSNHSVAEALLIFLEALPEPVICYELYQRCLDSAYDPRICRQVISQLPRCHRNVFRYLMAFLRELLKFSEYNSVNANMIATLFTSLLLRPPPNLMARQTPSDRQRAIQFLLGFLLGSEED
Protein: Delta-type opioid receptor (D-OR-1) (DOR-1) (P41143)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22184124, ECO:0000269|PubMed:7808419, ECO:0000269|PubMed:8201839}; Multi-pass membrane protein {ECO:0000269|PubMed:22184124, ECO:0000269|PubMed:7808419, ECO:0000269|PubMed:8201839}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Proenkephalin-A
- Proenkephalin-B
- Mu-type opioid receptor
- Pro-opiomelanocortin
- Kininogen-1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Prepronociceptin
- G-protein coupled receptor-associated sorting protein 1
Sequence:
MEPAPSAGAELQPPLFANASDAYPSACPSAGANASGPPGARSASSLALAIAITALYSAVCAVGLLGNVLVMFGIVRYTKMKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTRPRDGAVVCMLQFPSPSWYWDTVTKICVFLFAFVVPILIITVCYGLMLLRLRSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDIDRRDPLVVAALHLCIALGYANSSLNPVLYAFLDENFKRCFRQLCRKPCGRPDPSSFSRAREATARERVTACTPSDGPGGGAAA
Protein: Protein E7 (P03129)
Organism: Human papillomavirus type 16
Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04004, ECO:0000269|PubMed:18996550, ECO:0000269|PubMed:3033296}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04004, ECO:0000269|PubMed:18996550}. Note=Predominantly found in the host nucleus. {ECO:0000255|HAMAP-Rule:MF_04004, ECO:0000269|PubMed:18996550}.
Interaction partners:
Sequence:
MHGDTPTLHEYMLDLQPETTDLYCYEQLNDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPICSQKP
Protein: Zinc transporter 63C, isoform F (M9PEG6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- RE15841p
- IP18018p
- Zinc/iron regulated transporter-related protein 42C.2
- Zinc transporter ZIP11
- FI18611p1
- Protein catecholamines up
- P-type Cu
- FI24038p1
- Metallothionein-2
- LD23375p
Sequence:
MAKYSGKKCRLLSMMWLTAFFFFVEIIVGYVTNSMALVADSFHMLGDIAALVISFLSVKMSPKKWSKNTFGWARAEVLGALVNAVFLVALCFSITIEACKRFIEEEPIHEPELLVIVGALGLLVNVIGLCLLYEHGGHHGHSHGGGLTRNHSRLTELANMDEGEDEQNDFAYEKQKEKAPVKKSSHGHSHDPGQMNMRGAFLHVLSDALGSIIVVISAVVVWKTEWKYRYYMDPALSIVLVVLILHSVWPLLRESALILLQTVPTHIQVDAIQKRLLEKVDGVLAVHEFHVWQLAGDRIIASAHIRCRNLSEYMKIAEKVKEFFHNEGIHSTTIQPEFSEIEGCNMSDGTSSINISGSDCCALDCPTTEEGCVKATCCQNNNKLNQLPSPTNSPYLCRQRNAARQAGDVEAGSLLEATSSGNQGATGGASTGAPVAAIGATSTPKSDLVXRQPHQAQQHVHFATTKTETATATTKAATTAAATSIRDIMYEPRANNLVVSSAQVDVNLGLTVTAQRRRELQLQAEQQYQEQVSPLSTRNGDEVAL
Protein: Solute carrier family 5 member 4 (Q3UNC8)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MASTLSPSITPQTEEPPVVPVRIQNATDISVIVIYFIVVLAVGLWSMVRSNRGTVGGFFLAGHDMAWWPMGASLFASNIGSNHFVGLAGTGAASGIAIAAVEWNALLMVLVLGWVFLPIYIKAGVLTMPEYLRKRFGGKRLQIYLSVLSLFIMVALQTSSIIFSGAIFIQLALGLNLYLAVFILLAITAFYTVAGGLASVIYTDSVQTFIMLLGSLILMGFAFAEVGGYESFTEKYMNAIPSVVEGDNLTISPKCYTPQPDSFHVFRDPVTGDIPWPGLIFGMTILAIWYWCADQVIVQRCLCGRNMSHVKAACILCGYLKLLPMFLMVMPGMISRILYTDKVACVVPSECEKQCGTAVGCTNYAYPTLVLELMPDGLRGLMLSVMLASLMSSLTSIFNSASTLFTIDLYTKIRKKASERELMIAGRIFGMVLIAVSILWVPLVQVSQNGQLFHYIGSVSSYLGPPLGAVFMLAIFFKRVNEQGAFWGLMVGLVVGLIRLIAEFVYGTGSCVAPSNCPKIICGVHYMYFAIILFFVSIIVILGVSFLTEPIPDVHLYRLCWSLWNNTEERIDLDAEELETQEEAGGALEEDSEQSRGCLKRACCLLCGLQNTGPKLTKEEEAALRQKFSDTSEKPLWRTVMNINAVLLLGVAVFVHAYFA
Protein: NSFL1 cofactor p47 (UBX domain-containing protein 2C) (p97 cofactor p47) (Q9UNZ2)
Organism: Homo sapiens (Human)
Function: Reduces the ATPase activity of VCP (By similarity). Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis (By similarity). May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro). Together with UBXN2B/p37, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase. Also, regulates spindle orientation during mitosis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O35987}. Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:O35987}. Chromosome {ECO:0000250|UniProtKB:O35987}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O35987}. Note=Predominantly nuclear in interphase cells. Bound to the axial elements of sex chromosomes in pachytene spermatocytes. A small proportion of the protein is cytoplasmic, associated with Golgi stacks. Localizes to centrosome during mitotic prophase and metaphase. {ECO:0000250|UniProtKB:O35987}.
Interaction partners:
- Deubiquitinating protein VCPIP1
- UBX domain-containing protein 6
- Transitional endoplasmic reticulum ATPase
- UBX domain-containing protein 2A
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Nuclear protein localization protein 4 homolog
- Tether containing UBX domain for GLUT4
- FAS-associated factor 1
- UBX domain-containing protein 7
- UBX domain-containing protein 10
Sequence:
MAAERQEALREFVAVTGAEEDRARFFLESAGWDLQIALASFYEDGGDEDIVTISQATPSSVSRGTAPSDNRVTSFRDLIHDQDEDEEEEEGQRFYAGGSERSGQQIVGPPRKKSPNELVDDLFKGAKEHGAVAVERVTKSPGETSKPRPFAGGGYRLGAAPEEESAYVAGEKRQHSSQDVHVVLKLWKSGFSLDNGELRSYQDPSNAQFLESIRRGEVPAELRRLAHGGQVNLDMEDHRDEDFVKPKGAFKAFTGEGQKLGSTAPQVLSTSSPAQQAENEAKASSSILIDESEPTTNIQIRLADGGRLVQKFNHSHRISDIRLFIVDARPAMAATSFILMTTFPNKELADESQTLKEANLLNAVIVQRLT
Protein: Intermediate neuroblasts defective protein (O96620)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MSRSFLMDSLLSDRPNLSQKKEKLGSPVGSPTAAAAVAAAAMLPSIPMLPYPASYVGSYLFSLGIQQQQQQQQQQQQQAAAAAAAAAAAAALQQHPHVSSSPGSLYHPYAQLFASKRKSSGFSNYEGCYPSPPLSANPNSQQLPPIHNLYGSPVVGGLPLPEPGSFCTSPSASSSASLDYTNNFDEPQGKRFKHESSCSPNSSPLKNHSSGGPVEITPLINDYADSSKRIRTAFTSTQLLELEREFSHNAYLSRLRRIEIANRLRLSEKQVKIWFQNRRVKQKKGGSESPTFNLSTNSNGSPQASPVSPQVKVHELKVEA
Protein: Short-chain dehydrogenase/reductase 3 (EC 1.1.1.300) (DD83.1) (Retinal short-chain dehydrogenase/reductase 1) (retSDR1) (Retinol dehydrogenase 17) (Short chain dehydrogenase/reductase family 16C member 1) (O75911)
Organism: Homo sapiens (Human)
Function: Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome P450 26A1
- Retinaldehyde dehydrogenase 3
- Retinal dehydrogenase 2
- Aldehyde dehydrogenase 1A1
- Dehydrogenase/reductase SDR family member 9
- Lecithin retinol acyltransferase
- Beta,beta-carotene 15,15'-dioxygenase
- All-trans-retinol 13,14-reductase
- Dehydrogenase/reductase SDR family member 4
- Cytochrome P450 27C1
Sequence:
MVWKRLGALVMFPLQMIYLVVKAAVGLVLPAKLRDLSRENVLITGGGRGIGRQLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQTAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHINTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVEAVQLNQALLLLPWTMHALVILKSILPQAALEEIHKFSGTYTCMNTFKGRT
Protein: Eyes absent homolog (EC 3.1.3.48) (A0A8I6AS60)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKDRKASQLAGVSLLAVKTEPLHSSETTTTTGDGALDTFTGSVITSSGYSPRSAHQYSPQLYPSKPYPHILSTPAAQTMSAYAGQTQYSGMQQPAVYTAYSQTGQPYSLPAYDLGVMLPAIKTESGLPQTQSPLQSGCLSYSPGFSTPQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFSGSQQDYPSYTAFGQNQYAQYYSASTYGAYMTSNNTADGTSSSTSTYQLQESLQGLTSQPGEFDTVQSPSTPIKDLDDRTCRSSGSKSRGRGRKNNPSPPPDSDLERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYSFATDGFHATASSANLCLPTGVRGGVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLTNALKSLSIISTRSNCVNVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVSRFGTNITYVVIGDGRDEEHAANQHNMPFWRISSHSDLLALHQALELEYL
Protein: Small ribosomal subunit protein eS27A (40S ribosomal protein S27-A) (RP61) (YS20) (P35997)
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:
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS26A
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein eS4A
- Small ribosomal subunit protein eS1A
- Small ribosomal subunit protein eS10A
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein uS11B
- Small ribosomal subunit protein eS7B
Sequence:
MVLVQDLLHPTAASEARKHKLKTLVQGPRSYFLDVKCPGCLNITTVFSHAQTAVTCESCSTILCTPTGGKAKLSEGTSFRRK
Protein: Alpha-crystallin A chain (Q8UUZ6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Alpha-crystallin B chain
- Beta-crystallin B2
- Beta A1-crystallin
- Beta-crystallin A2
- Crystallin, beta B1
- Beta-crystallin B3
- Beta-crystallin A4
- Novel protein similar to heat shock cognate 70-kd protein
- Crystallin, gamma S1
- Gap junction protein
Sequence:
MDIAIQHPWFRRTLGYPTRLFDQFFGEGLFDYDLFPFTTSTVSPYYRHSLFRNILDSSNSGVSEVRSDREKFTVYLDVKHFSPDELSVKVTDDYVEIQGKHGERQDDHGYISREFHRRYRLPSNVDQSAITCTLSADGLLTLCGPKTSGIDAGRGDRTIPVTREDKSNSGSSS
Protein: Probable eukaryotic initiation factor 4A (ATP-dependent RNA helicase eIF4A) (Q38BK1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Uncharacterized protein
- U6 snRNA-associated Sm-like protein LSm7p
- NOT1
- poly
- Uncharacterized protein
- PAB1-binding protein 1
- U6 snRNA-associated Sm-like protein LSm4
- Argonaute-like protein
- Endonuclease/exonuclease/phosphatase domain-containing protein
- Endonuclease/exonuclease/phosphatase, putative
Sequence:
MVTDDDWREGLKAPTKDVRKKTEDVESRRNVTFEEYGLRRELQMGIFEKGFERPSPVQEEAIPVALQGKDVLARAKNGTGKTASFVIPVLEKVDTQLPHIQALLMVPTRELALQTAQVTKELGKHITGLEVMVTTGGTTLRDDILRLQSVVHVLVATPGRAVDLASKGTAKLDHCRIIVLDEADKLLSQEFTSLMRDLYGFLPKGRQSLLFSATFPVTVKDFADKYLRNPYEINLMEELTLRGVTQYYAFVEERQKIHCLNTLFNRLQINQSIIFCNSVNRVELLAKKITQLGYSCYYIHARMQQQHRNRVFHDFREGHCRNLVCSDLITRGIDIQAVNVVINFDFPKYAETYLHRIGRSGRFGHLGLAINFVTYEDRHNVYRIEQELDTEIKPIPAEVDPELYTA
Protein: Serine incorporator 2 (Q4FZV1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-1-interacting protein
Sequence:
MGACLGACSLLSCASCLCGSAPCILCSCCPSTRNSTVSRLLFTGFLFLGVLVSIIMLSPGVESQLYKLPWVCEDRAQQPVVLQGPLDCGSLLGFRAVYRMCFATAAFFFLFMMLMICVRSSRDPRAAIQNGFWFFKFLILVGITVGAFYIPDGSFPKIWFYFGVVGSFLFILIQLILFIDFAHSWNQRWLCKAEECDSPVWYAGLFFFTFLFYLLSIAAVALMFVYYTESGACHEGKVFIGLNLTFCVCVSIIAVLPKVQSAQPNSGLLQASVVTLYTMFVTWSALSNVPDQKCNPHLPTKNGTGQVNLEDYSTVWWDAPSIVGLVIFILCTFFISLRSSDHRQVNSLMQTEECPAEMVQQQQVAVGDGRTYDNEQDGVTYSYSFFHFCLVLASLHVMMTLTNWYSPGETRKMISTWTSVWVKICASWAGLFLYLWTLVAPLLLPNRDFS