wanglab/gogpt-training-data huggingface dataset:
Protein: At1g70770 (F15H11.2 protein) (Q9S791)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transmembrane protein
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- ACT domain-containing protein ACR12
- Type II inositol polyphosphate 5-phosphatase 15
- At5g16260 family protein)
- Eukaryotic translation initiation factor isoform 4G-2
- Peroxidase 66
- Protein indeterminate-domain 5, chloroplastic
- Defensin-like protein 4
Sequence:
MDPIESVEYNGFETSNGNVDHGWKKVVYPKRHRKQKQADQATANGGKTVASNGTVANGGDNVFRSLEEQAEDRRRRILAAKMTAIDSDDDGVVRSKHRSNGYGDDGYDFDGSDDEIATLKVEEVKKPKPKKEKKPKVSLPEAASKIDPLNLEAFLVEASESYASQPEIQLMRFADYFGRALSGVSSVQFPWVKMFKESPLSKLIEVPLAHIPEPVYKTSVDWINHRPIEALGAFVLWAFDCILTDLAAQQGGAKGGKKGGQQTTSKSQVAIFVALAMVLRRKPDALTNVLPTLRENPKYQGQDKLPVTVWMMAQASQGDIAVGLYSWAHNLLPVVGNKNCNPQSRDLILQLVEKILTNPKARTILVNGAVRKGERLIPPPSFEILLRLTFPASSARVKATERFEAIYPLLKEVALAGAPGSKAMKQVTQQIFTFALKLAGEGNPVLAKEATAIAIWSVTQNFDCCKHWDNLYKENLEASVAVLKKLVEEWKEHSVKLSSSPNDALTLNRTMKSFRLKNEEVITEGGANASLYKEADKSCKTISGRLSRGSGCLKGTAITLVFLAAAGAAAAAVLSSNPEVTNELKNLVDSLELHEYINKYTEVISTALKK
Protein: Calretinin (CR) (29 kDa calbindin) (P22676)
Organism: Homo sapiens (Human)
Function: Calretinin is a calcium-binding protein which is abundant in auditory neurons.
Subcellular location: Synapse {ECO:0000250|UniProtKB:Q08331}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q08331}. Note=Located in dendrioles, small dendrites that makes up a brush structure found as the terminal specialization of a dendrite of a unipolar brush cell. {ECO:0000250|UniProtKB:Q08331}.
Interaction partners:
- Parvalbumin alpha
- Somatostatin
- Pro-neuropeptide Y
- Transcription factor Sp8
- Glutamate decarboxylase 1
- Wilms tumor protein
- 45 kDa calcium-binding protein
- Homeobox protein DLX-1
- Keratin, type II cytoskeletal 5
- Keratin, type II cytoskeletal 7
Sequence:
MAGPQQQPPYLHLAELTASQFLEIWKHFDADGNGYIEGKELENFFQELEKARKGSGMMSKSDNFGEKMKEFMQKYDKNSDGKIEMAELAQILPTEENFLLCFRQHVGSSAEFMEAWRKYDTDRSGYIEANELKGFLSDLLKKANRPYDEPKLQEYTQTILRMFDLNGDGKLGLSEMSRLLPVQENFLLKFQGMKLTSEEFNAIFTFYDKDRSGYIDEHELDALLKDLYEKNKKEMNIQQLTNYRKSVMSLAEAGKLYRKDLEIVLCSEPPM
Protein: Kinesin light chain (KLC) (P46822)
Organism: Caenorhabditis elegans
Function: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport (Probable). The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (Probable). Recruits unc-83 (within the unc-83-unc-84 LINC complex) to the nuclear envelope during nuclear migration to mediate the link between the nuclear envelope and the microtubule cytoskeleton in hypodermal precursor cells.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:19605495}. Nucleus envelope {ECO:0000269|PubMed:19605495}. Note=Recruited to the nuclear envelope by unc-83 during nuclear migrations. {ECO:0000269|PubMed:19605495}.
Interaction partners:
- Kinesin heavy chain
- JNK-interacting protein
- PID domain-containing protein
- Nuclear migration protein unc-83
- Calsyntenin-1
- Kinesin-like protein unc-104
- Kinesin 1 cargo adaptor alternative variant a
- Kinesin like protein
- Actin
- Kinesin light chain
Sequence:
MSNMSQDDVTTGLRTVQQGLEALREEHSTISNTLETSVKGVKEDEAPLPKQKLSQINDNLDKLVCGVDETSLMLMVFQLTQGMDAQHQKYQAQRRRLCQENAWLRDELSSTQIKLQQSEQMVAQLEEENKHLKYMASIKQFDDGTQSDTKTSVDVGPQPVTNETLQELGFGPEDEEDMNASQFNQPTPANQMAASANVGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAANLLNEALSIREKCLGESHPAVAATLNNLAVLFGKRGKFKDAEPLCKRALEIREKVLGDDHPDVAKQLNNLALLCQNQGKYEEVEKYYKRALEIYESKLGPDDPNVAKTKNNLSSAYLKQGKYKEAEELYKQILTRAHEREFGQISGENKPIWQIAEEREENKHKGEGATANEQAGWAKAAKVDSPTVTTTLKNLGALYRRQGKYEAAETLEDVALRAKKQHEPLRSGAMGGIDEMSQSMMASTIGGSRNSMTTSTSQTGLKNKLMNALGFNS
Protein: Sugar transporter SWEET1 (Protein saliva) (Q7JVE7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MSAVAYDSLLSTTAVISTVFQFLSGAMICRKYIQKKSTGDSSGVPFICGFLSCSFWLRYGVLTNEQSIVLVNIIGSTLFLVYTLIYYVFTVNKRACVKQFGFVLTVLVVVIVYTNRLEDQRDRMIHVTGIVCCIVTVCFFAAPLASLLHVIRAKNSESLPLPLIATSFVVSLQWLIYGILISDSFIQIPNFLGCILSLLQLGLFVLYPPRSYSGHGYKLVEQAVPF
Protein: Cytochrome c oxidase subunit 7A1, mitochondrial (Cytochrome c oxidase subunit VIIa-heart) (Cytochrome c oxidase subunit VIIa-H) (Cytochrome c oxidase subunit VIIa-muscle) (Cytochrome c oxidase subunit VIIa-M) (P24310)
Organism: Homo sapiens (Human)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07470}; Single-pass membrane protein {ECO:0000250|UniProtKB:P07470}.
Interaction partners:
- Cytochrome b-c1 complex subunit 10
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6A2, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome b-c1 complex subunit 8
Sequence:
MQALRVSQALIRSFSSTARNRFQNRVREKQKLFQEDNDIPLYLKGGIVDNILYRVTMTLCLGGTVYSLYSLGWASFPRN
Protein: SIN3 transcription regulator family member A (H3BQ88)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKRRLDDQESPVYAAQQRRIPGSTEAFPHQHRVLAPAPPVYEAVSETMQSATGIQYSVTPSYQVSAMPQSSGSHGPAIAAVHSSHHHPTAVQPHGGQVVQSHAHPAPPVAPVQGQQQFQRLKV
Protein: Transposon Ty1-DR6 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (P0C2I3)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNYLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIEKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: NAC (No Apical Meristem) domain transcriptional regulator superfamily protein (No apical meristem family protein) (Q9LXY8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- NAC domain containing protein 97
- Putative NAC domain-containing protein 61
- AT3g04420/T27C4_6
- NAC domain-containing protein 68
Sequence:
MEPTHRALPVGFRFRSTNCEISNYFLKKKALGQPMKARTIPEECHDIFSRHPHDLPGYPSEEHWYYFCRKRDNQVTSNSHNLWTPIGEETNVLDPKNNDALVGIKRRFTLIAQEEEESDNICLSDDEEALKYNWFMDEISLPQTVANTDWVLCHIFGKKTKPETTDLSTIDSESE
Protein: Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 3 (AthCYSTM3) (A0A178WF56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates negatively salt stress responses and Na(+) homeostasis. Prevents Na(+) efflux, disturbs reactive oxygen species (ROS) homeostasis, and represses the expression of nuclear salt stress-responsive genes. Involved in resistance to abiotic stress.
Subcellular location: Cell membrane {ECO:0000269|PubMed:29272523}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29272523}. Mitochondrion {ECO:0000269|PubMed:30701352}.
Interaction partners:
Sequence:
MAQYHQQHEMKQTMAETQYVTAPPPMGYPVMMKDSPQTVQPPHEGQSKGSGGFLRGCLAAMCCCCVLDCVF
Protein: GEO10744p1 (IP06470p) (IP06570p) (Insulin-like peptide 8) (Q4V5V6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI21465p1
- Insulin-like peptide 7
- Insulin-like receptor
- Insulin-like peptide 1
- Insulin-like peptide 3
- Insulin-like peptide 6
- Insulin-like peptide 5
- Prothoracicotropic hormone, isoform F
- Insulin-like peptide 4
- U2 snRNP-associated SURP motif-containing protein
Sequence:
MSSKLHMCRWMLLVIGVCCLMGSSSGSFCSLERMKKFAMEACEHLFQADEGARRDRRSIEFAHHHLNRLGSGKTHNKHHYISRSSYPMGGYLKVTREHFNRLSELDIFPRYKPIKPHHEKKHRFKRDHSSRSYNNIPYCCLNQCEEEFFC
Protein: Tubulin glycylase 3A (EC 6.3.2.-) (Q23TC2)
Organism: Tetrahymena thermophila (strain SB210)
Function: Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:19531357}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:19531357}. Note=Mainly present in locomotory and oral cilia.
Interaction partners:
Sequence:
MFQQNQQSQNQQAQNLMHIQLNGNTQLGLGALQTINVKPIKLQSRAQSLNPNLRISERNKQTTQTSSNRQNISNKSPNNLQTSKSGGLQTQNANQKLSSSSAPKKISGNFSSRVIYRAKTKNEDEIIKKQSSQTSISTNGQEKKGEIIRFATESQINNENSTPNSKIQLPPIQEKNSYKFYINSQSSNNQVSQDQSPPLQGLQAFNINKNKENQFTKKRHFDFLERTKVKNQSEETDLLKMHRYFRCKVSNLITGSGKKQYYLQYLKDMKDLMTKVKQYERVAKQNLFINDVMNKLKKIVATRAKYKYKEKIDFTRSIIMRTLGYESRQIIQQLKENMALEEQEYEDLEDDADREYEELKKKQEQQALDKNQKKELISSEIIANWKKMRGYQPNQKVFICIGQYTDLKNYLKEQGWIENPNPESLVFDLKWVTKKKDVDKDLLLDQQITNHFQKNHNLTSKNGIALNLRNLIWYDSVDIDTFYPRCFDLSDVQEFEDFIEEFKFTQAESILKQYVENKLVIDQKAKQYEKYLRLKILLACVALKRRTFSIEKKISLISVNTLPIISPEEWSVLNRQDNNYLFLEQNPDVYHRLSQIITREMDSEESNAVDLSKLAQKYLEASKEYDPQYDLNEKNLWIVKPAGLSRGRGIRAFDQLEPLLNYIMGKDVMWVAQKYMENPLTIHKKKFDIRQWVLVTEWNPLTIYFYDTCYIRICFDEYDPSDLQNKFAHLANNCISKHADNFEEKVNDTMMYLEDFVEYIKKIEGKDMFYSKIQKEMMNIAINSIKSCKDSIEPRRNSLELYGYDFMVDQNYNTWLLEINSSPSMEYSTPVTTKLVKMGLEDTAKVIHHHFVEGEKRFNKNIEYGLWKNIYREQK
Protein: Probable endonuclease C19F8.04c (EC 3.1.-.-) (O60168)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Meiotic expression up-regulated protein 26
- Actin-related protein 2/3 complex subunit 2
- Uncharacterized protein C23H3.15c
Sequence:
MQESQYKEKAIIGTGLITTSIGGFFFLRRFRRISNASTIPKNYLNNSTVENRKYKTMFGYVTRVGDGDNFRFYHTPGGRLLGWHWLRKVPCSRSDLSNETISVRLAGIDAPESAHFGKQEQPYALEAKEFLHNKLYHKSVRIIPLKIDRYARLVAGVQYYPIPHFFWKKDIGPQMIRKGLAVVYEGSDGVFCPTKKECLLALEIVAKKKKLSLWSQGKKLILPSVYKRGV
Protein: RNA helicase (A7MNC7)
Organism: Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii)
Interaction partners:
Sequence:
MNSIFYSVITLLLLLSGVLFFMKENGANKPDNASGADPIPPRNKEEGEDHFSALLNAITPLWYWRVNHEYIDFTNATIKKMTFEELNATPGLFEAQRRCSNLNSAVYKYYDNLKKRCLNGELVTFSDIEVLNLRHCFHEFSQEAYPQLVAIVWPEFQRPQVDITQV
Protein: Growth/differentiation factor 10 (GDF-10) (Bone morphogenetic protein 3B) (BMP-3B) (xBMP-3B) (Q7T2X6)
Organism: Xenopus laevis (African clawed frog)
Function: Dorsalizing factor. Antagonizes mesoderm formation by nodal-like proteins and ventralizing BMPs. Cooperates with cer1 to promote embryonic head formation.
Subcellular location: Secreted {ECO:0000269|PubMed:12885561}.
Interaction partners:
Sequence:
MQFSLVMSYYCLACFLVMFALGRAIKAHTSKLPPEGVGTIRLQSDPLSLHMAKLYEKYSREGSRLQDGNTVRSFRAQPDSQFGSPLYRFNLSSLQQTEEVLAATLHFAPVKGSRSSRDSYCKRSKKSSCRLLLPTQHQKISLVFKSVIQNKTLGSEKWNTTNIFHKRAAWHVKDITNIIKDAQHERDLFISMEISFGEKFATVFENNPSELPYILVFADDRAISDPNSIALTLQRYDPFQPNGGNSKQAPNTFPESRVKRDTSDLASSHDNELPDIKYMRYSKEDLWESTYKSLKHKSPRKEKKKKGQENEETLPKSPVLHFDERTMKKARRRQWDEPRVCSRRYLKVDFADIGWSEWIISPKSFDAYYCSGACEFPMAKVVRPSNHATIQSIVKAVGIIPGVPEPCCTPDMMNSLSVLFLDEGRNMVLKVYPNMSVESCSCR
Protein: DNA (cytosine-5)-methyltransferase 1B (OsMET1b) (EC 2.1.1.37) (DNA methyltransferase 1-2) (OsMET1-2) (B1Q3J6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Major CG methylase that methylates chromatin CpG residues and maintains DNA methylation. Plays a major role in genomic imprinting, regulation of embryogenesis and seed viability. Maintains DNA methylation at the FIE1 gene locus in the embryo.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Adenosylhomocysteinase
- S-adenosylmethionine decarboxylase proenzyme
- DNA
- DNA
- DNA
- Os05g0149200 protein
- 1-aminocyclopropane-1-carboxylate synthase 1
- 1-aminocyclopropane-1-carboxylate synthase 2
- S-adenosylmethionine decarboxylase proenzyme
- Os05g0221800 protein
Sequence:
MVKSPCSPVTTGKKRCRAKPQKKDEDTTDKGKLDEGPLDATKEMNGVGKGDSRAACKRPRRAAACSDFKEKSVRLSDKSSVVATNGNKMEEEEMDAVKLTKLGPEVQRPCRKLIDFILHDADGKLQPFEMSEIDDFFITALIMPMDDDLEKDRQKGVRCEGFGRIEDWAISGYDEGTAVVWVSTEVADYECVKPAGNYKSYYDHFYEKAQVCVEVYRKLARSVGGNPNLGLEELLASVVRSINAIKGYSGTLSKDFVISNGEFVYNQLIGLDETANTDDEKFATLPVLLALRDGCKSRVEVSKLQPNISNGSLKINDAECKEVSEDDDEKLARLLQQEEEWKMMKQRGKRGTTSQKNVYIKISEAEIANDYPLPAYYKPSSQEMDEYIFDSEDSFYSDVPVRILNNWALYNADSRLIPLELIPMKAGAENDIVVFGSGFMREDDGSCCSTAESAKLSSSSSSNHQDAGVSIYLSPIKEWVIEFGGSMICITIRTDVAWYKLRQPTKQYAPWCEPVLKTARLSVSIITLLKEQSRASKLSFADVIKKVAEFDKGSPAFVSSNVALVERYIVVHGQIILQQFSDFPDETIRRSAFATGLLMKMEQRRHTKLVMKKKVQVMRGENLNPSATMGPASRRKVMRATTTRLINRIWSDYYTHHFPEDSKDADVNEAKEIDDELEENEDEDAEEEAQIEEENVSKTPPSTRSRKLVSQTCKEIRWEGEAIGKTPSGEALYKCAYVRELRINLGRTVALEDDSGELVMCFVEYMFQKLNGAKMVHGRLLQKGSETVLGNAANERDLFLTNECLEFELEDIKELMSVNLQSLPWGHKYRKENAEADRIERAKAEDRKKKGLPMEYLCKSLYWPEKGAFFSLPHDKLGLGNGFCSSCQQKEPDCDELQILSKNSFIYRNITYNVNDYLYIRPDFFSQEEDRATFKGGRNVGLKPYVVCHLLDVHEPAGSRKIHPASTKISVRRFYRPDDISSAKAYVSDIREVYYSENIVKVPVDMIEGKCEVKKKIDISNSDVPVMVEHEFFCEHFYDPATGALKQLPPNVKLMSVQQKATGALKKNKGKQICESDQVDSDKCTKVSKENRLATLDIFAGCGGLSEGLQQAGVSFTKWAIEYEEPAGEAFTKNHPEAAVFVDNCNVILKAIMDKCGDADDCISTSEAAEQAAKFSQDNIMNLPVPGEVEFINGGPPCQGFSGMNRFNQSPWSKVQCEMILAFLSFAEYFRPRFFLLENVRNFVSFNKGQTFRLTVASLLEMGYQVRFGILEAGTFGVAQSRKRAFIWAAAPGETLPDWPEPMHVFASPELKINLPDGKYYAAAKSTAGGAPFRAITVRDTIGDLPKVENGASKLLLEYGGEPISWFQKKIRGNTIALNDHISKEMNELNLIRCQRIPKRPGCDWHDLPDEKVKLSSGQLVDLIPWCLPNTAKRHNQWKGLYGRLDWEGNFPTSVTDPQPMGKVGMCFHPDQDRIITVRECARSQGFPDNYQFAGNIQSKHRQIGNAVPPPLAFALGRKLKEAVDAKRQ
Protein: Eukaryotic translation elongation factor 1 delta (E9PQR8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSGKASCTLETVWEDKHKYEEAERRFYEHEATQAAASAQQLPAEGPAMNGPGQDDPEDADEAEAPDGGSRRDPRKSQDSRKPLQKKRKRSPKSGLGPADLALLGLSAERVWLDKSLFDQAESSYRQKLADVAAQAAWPPALAPWGLCTHGNQVACHHVTWGIWVNKSSFDQAERAFVEWSQALLLAPDGSRRQGTPNTGQQVAVPDLAHQPSPPVNGQPPLGSLQALVREVWLEKPRYDAAERGFYEALFDGHPPGKVRLQERAGLAEGARRGRRDRRGRNILGNKRAGLRRADGEAPS
Protein: Sarcoplasmic calcium-binding protein, isoform C (M9PHB8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAFSIVSRGILRTSREILERNMAATVGVLQQNASPPPNTPISHSDCHRLASGGIICGHGAHSLLWHQMPTAVVQAVRQYSKKAGAAKLRREVESDSDSDSDDEFERRRQKMDSKRSERGDSAFWRRKMRTLHRILDVNHDGVVSFDDFSLLAKRFSDLGHLTPEVAAEFNDVIKHTWEEQFGEITPYNLVTAEQFLTDLHHRLNDKKMAKRIGRFLPYLFKAVDFDHTGHLDLEQYKLFFRCLGLTEDDAAVSFAVIDKNGDGQLSLKEFVHLGRQFFLTEDDSKISKMFWGPLVADHXRVAVTAVDYNTTKSTITQQKNPYYNQDYQNHQHNNVRCHNIGNNNTNEPMLHYTLNTTTMLANNNYNKIVATSLPTRVQAAGGSWLNLQHVAPHKSGPLINISNTTTIVIRNMSIYDYFRQHLSSSKRQRSTFEPHPSPTTYPASKLRKHNFSNYQKEREREREDRQKDNNNNNHRTKGKPSLDDYDIRFFVYLNSLIIFTMSCSRQSAAEGDDLKHFICDRIRKFDRLRRKARKRRKRRPKKLVEDQMHHL
Protein: Poly(A) RNA polymerase GLD2 (hGLD-2) (EC 2.7.7.19) (PAP-associated domain-containing protein 4) (Terminal nucleotidyltransferase 2) (Terminal uridylyltransferase 2) (TUTase 2) (Q6PIY7)
Organism: Homo sapiens (Human)
Function: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Does not play a role in replication-dependent histone mRNA degradation. Adds a single nucleotide to the 3' end of specific miRNAs, monoadenylation stabilizes and prolongs the activity of some but not all miRNAs.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q91YI6}. Nucleus {ECO:0000250|UniProtKB:Q91YI6}.
Interaction partners:
- Cytoplasmic polyadenylation element-binding protein 1
- Symplekin
- Poly
- Poly
- Poly
- Poly
- Poly
- Neuroguidin
- Polyadenylate-binding protein 1-like
- Telomerase reverse transcriptase
Sequence:
MFPNSILGRPPFTPNHQQHNNFFTLSPTVYSHQQLIDAQFNFQNADLSRAVSLQQLTYGNVSPIQTSASPLFRGRKRLSDEKNLPLDGKRQRFHSPHQEPTVVNQIVPLSGERRYSMPPLFHTHYVPDIVRCVPPFREIAFLEPREITLPEAKDKLSQQILELFETCQQQISDLKKKELCRTQLQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKEEPCFFQVNQKTEARHILTLVHKHFCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHQINDASRGTLSSYSLVLMVLHYLQTLPEPILPSLQKIYPESFSPAIQLHLVHQAPCNVPPYLSKNESNLGDLLLGFLKYYATEFDWNSQMISVREAKAIPRPDGIEWRNKYICVEEPFDGTNTARAVHEKQKFDMIKDQFLKSWHRLKNKRDLNSILPVRAAVLKR
Protein: Pantothenate kinase (A0A1D8PQ17)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Pantoate--beta-alanine ligase
- Phosphopantothenate--cysteine ligase
- Pantetheine-phosphate adenylyltransferase
- Phosphopantothenoylcysteine decarboxylase complex subunit
Sequence:
MPVFEKKDTVHTNVPSPRPSTNSHTSSTYIPRYRLSITTNEDINLQSIDPGTVKIDCSGAFIANDDLLRDTAPDITDEINNSSSSTSGTPPSSNTSSDLEDDTEESEFDTEENGGGLSDSSSTTVEDDENQLQQLQQQPLYGGVITKNNITLPQHNDEIIHISVDIGGTLTKLVYFTKSSSNRKNSSRKTTGGGGGGKLHFQDFQTENFKNEAMKFMIKLIQKSINKSNINPPITYIMATGGGAHKFYNLMKKTFKKHKLPMKIIAKDEMECLIKGLDWLITKIPQEIFTYDLTELTTKFEPIQSKKEIYPYLLVNIGSGVSMVKVTKPGPEGFERIGGSSLGGGTLWGLLSLLTDAKDYNEMLEMAQNGDNENIDLLVGDIYGTNYNKIGLKANHIASSFAKVFKKLRKFNSSTNSNNNNNSDNDSDGKFKKLTAAEKLAQFKQEDIARSLLFSISNNIGQIAYLHALRFNLKRIYFGGSYISGHMQTIHTLSYAVNFWSKGEMQSYFLRHEGYLGSVGAFMMGPAPILEENGNSSNENNHTNNVKIANGVQH
Protein: Endophilin B, isoform C (A8DYJ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNINLPNFNVKNLVKEAGSTISRVVQLTEEKLGTTERTEYDLHFQNLAERADVTKTWTEKIVRDTESVLIPNPQNRVEDFIFEKIEKSKPKRLSNLEHLALDMIEAGGDFGQDLPYGQALIKVGQAEQKLGQCEHDFIATSGICFTQPLRKFLDGEMKTIGKERGILETKRLDLDACKNRVKKARSMLGQQSKDGISPEAVLEQAERDLRVAQAEFDRQAEITKLLLDGISTSQASHLRHLHAFIQTQVRYYKQCGDVMEQLQRELAKMQHPKPRLRINSEDVDCGPPSSVSMHSCDSDSLGGIALDSDPDPDLDKSLTNLLEDFHIEFDTTAVSTVIFVTECSPVNEDYMYGKQGLLKGLVPRAFVEMLDEEHDVTL
Protein: C-C chemokine receptor type 4 (C-C CKR-4) (CC-CKR-4) (CCR-4) (CCR4) (CD antigen CD194) (P51680)
Organism: Mus musculus (Mouse)
Function: High affinity receptor for the C-C type chemokines CCL17/TARC and CCL22/MDC. The activity of this receptor is mediated by G(i) proteins which activate a phosphatidylinositol-calcium second messenger system. Could play a role in lipopolysaccharide (LPS)-induced endotoxic shock. In the CNS, could mediate hippocampal-neuron survival.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- C-C motif chemokine 22
- C-C motif chemokine
- C-C motif chemokine 5
- Guanine nucleotide-binding protein G
- Stromal cell-derived factor 1
- C-C motif chemokine 2
- C-C motif chemokine 6
- C-C motif chemokine 9
- C-C motif chemokine 3
- C-C motif chemokine 4
Sequence:
MNATEVTDTTQDETVYNSYYFYESMPKPCTKEGIKAFGEVFLPPLYSLVFLLGLFGNSVVVLVLFKYKRLKSMTDVYLLNLAISDLLFVLSLPFWGYYAADQWVFGLGLCKIVSWMYLVGFYSGIFFIMLMSIDRYLAIVHAVFSLKARTLTYGVITSLITWSVAVFASLPGLLFSTCYTEHNHTYCKTQYSVNSTTWKVLSSLEINVLGLLIPLGIMLFCYSMIIRTLQHCKNEKKNRAVRMIFAVVVLFLGFWTPYNVVLFLETLVELEVLQDCTLERYLDYAIQATETLAFIHCCLNPVIYFFLGEKFRKYITQLFRTCRGPLVLCKHCDFLQVYSADMSSSSYTQSTVDHDFRDAL
Protein: LIM/homeobox protein Lhx1 (LIM homeobox protein 1) (Homeobox protein Lim-1) (Rlim) (P63007)
Organism: Rattus norvegicus (Rat)
Function: Potential transcription factor. May play a role in early mesoderm formation and later in lateral mesoderm differentiation and neurogenesis (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:7914684, ECO:0000269|PubMed:8793615}.
Interaction partners:
- Paired box 2
- LIM domain binding 1
- Cyclin-K
- Paired box protein Pax-8
- Cyclin T1
Sequence:
MVHCAGCKRPILDRFLLNVLDRAWHVKCVQCCECKCNLTEKCFSREGKLYCKNDFFRCFGTKCAGCAQGISPSDLVRRARSKVFHLNCFTCMMCNKQLSTGEELYIIDENKFVCKEDYLSNSSVAKENSLHSATTGSDPSLSPDSQDPSQDDAKDSESANVSDKEGGSNENDDQNLGAKRRGPRTTIKAKQLETLKAAFAATPKPTRHIREQLAQETGLNMRVIQVWFQNRRSKERRMKQLSALGARRHAFFRSPRRMRPLVDRLEPGELIPNGPFSFYGDYQSEYYGPGGNYDFFPQGPPSSQAQTPVDLPFVPSSGPSGTPLGGLDHPLPGHHPSSEAQRFTDILAHPPGDSPSPEPSLPGPLHSMSAEVFGPSPPFSSLSVNGGASYGNHLSHPPEMNEAAVW
Protein: Zinc finger CCHC domain-containing protein 9 (Q8N567)
Organism: Homo sapiens (Human)
Function: May down-regulate transcription mediated by NF-kappa-B and the serum response element.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:18721783}. Nucleus {ECO:0000269|PubMed:18721783}. Note=Expressed throughout the nucleus and concentrated mainly in the nucleolus. {ECO:0000269|PubMed:18721783}.
Interaction partners:
- RNA exonuclease 4
Sequence:
MTRWARVSTTYNKRPLPATSWEDMKKGSFEGTSQNLPKRKQLEANRLSLKNDAPQAKHKKNKKKKEYLNEDVNGFMEYLRQNSQMVHNGQIIATDSEEVREEIAVALKKDSRREGRRLKRQAAKKNAMVCFHCRKPGHGIADCPAALENQDMGTGICYRCGSTEHEITKCKAKVDPALGEFPFAKCFVCGEMGHLSRSCPDNPKGLYADGGGCKLCGSVEHLKKDCPESQNSERMVTVGRWAKGMSADYEEILDVPKPQKPKTKIPKVVNF