wanglab/gogpt-training-data huggingface dataset:
Protein: Phosducin-like protein 3 (Viral IAP-associated factor 1 homolog) (Q6P268)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation. Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H2J4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}.
Interaction partners:
- Tcp1 protein.
- T-complex protein 1 subunit delta
- Chaperonin-containing TCP1, subunit 6A
- T-complex protein 1 subunit gamma.
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit theta
- Chaperonin-containing TCP1, subunit 2
- Chaperonin-containing TCP1, subunit 2
- Protein FAM161A
Sequence:
MQDPNADTEWNDILRKKGILPPKETPVEEEEDEQLHLQSQSVVKTYEDMTLEELEENEDEFSEEDEHAMEMYRLKRLAEWKANQMKNVFGELKEISGQDYVQEVNKAGEGIWVVLHLYKQGIPLCSLINQHLAQLARKFPQSKFLKSISSTCIPNYPDRNLPTLFVYRDGEMKAQFIGPLVFGGMNLTCDELEWRLSESGAVKTDLEENPRKQIQDQLMTSIRCSANTHRDGEEDSDED
Protein: Protein CFT1 (Cleavage factor two protein 1) (Q06632)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Involved in poly(A) site recognition. May be involved in coupling transcription termination and mRNA 3'-end formation.
Subcellular location: Nucleus {ECO:0000269|PubMed:12819204, ECO:0000269|PubMed:14562095}.
Interaction partners:
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Polyadenylation factor subunit 2
- Pre-tRNA-processing protein PTA1
- Protein MPE1
- Protein PTI1
- COMPASS component SWD2
- Poly
- Endoribonuclease YSH1
- Cleavage factor two protein 2
- mRNA 3'-end-processing protein RNA15
Sequence:
MNVYDDVLDATVVSHSLATHFTTSDYEELLVVRTNILSVYRPTRDGKLYLTDEFKFHGLITDIGLIPQKDSPLSCLLLCTGVAKISILKFNTLTNSIDTLSLHYYEGKFKGKSLVELAKISTLRMDPGSSCALLFNNDIIAFLPFHVNKNDDDEEEEDEDENIDDSELIHSMNQKSQGTNTFNKRKRTKLGDKFTAPSVVLVASELYEGAKNIIDIQFLKNFTKPTIALLYQPKLVWAGNTTISKLPTQYVILTLNIQPAESATKIESTTIAFVKELPWDLHTIVPVSNGAIIVGTNELAFLDNTGVLQSTVLLNSFADKELQKTKIINNSSLEIMFREKNTTSIWIPSSKSKNGGSNNDETLLLMDLKSNIYYIQMEAEGRLLIKFDIFKLPIVNDLLKENSNPKCITRLNATNSNKNMDLFIGFGSGNALVLRLNNLKSTIETREAHNPSSGTNSLMDINDDDDEEMDDLYADEAPENGLTTNDSKGTVETVQPFDIELLSSLRNVGPITSLTVGKVSSIDDVVKGLPNPNKNEYSLVATSGNGSGSHLTVIQTSVQPEIELALKFISITQIWNLKIKGRDRYLITTDSTKSRSDIYESDNNFKLHKGGRLRRDATTVYISMFGEEKRIIQVTTNHLYLYDTHFRRLTTIKFDYEVIHVSVMDPYILVTVSRGDIKIFELEEKNKRKLLKVDLPEILNEMVITSGLILKSNMCNEFLIGLSKSQEEQLLFTFVTADNQIIFFTKDHNDRIFQLNGVDQLNESLYISTYQLGDEIVPDPSIKQVMINKLGHDNKEEYLTILTFGGEIYQYRKLPQRRSRFYRNVTRNDLAITGAPDNAYAKGVSSIERIMHYFPDYNGYSVIFVTGSVPYILIKEDDSTPKIFKFGNIPLVSVTPWSERSVMCVDDIKNARVYTLTTDNMYYGNKLPLKQIKISNVLDDYKTLQKLVYHERAQLFLVSYCKRVPYEALGEDGEKVIGYDENVPHAEGFQSGILLINPKSWKVIDKIDFPKNSVVNEMRSSMIQINSKTKRKREYIIAGVANATTEDTPPTGAFHIYDVIEVVPEPGKPDTNYKLKEIFQEEVSGTVSTVCEVSGRFMISQSQKVLVRDIQEDNSVIPVAFLDIPVFVTDSKSFGNLLIIGDAMQGFQFIGFDAEPYRMISLGRSMSKFQTMSLEFLVNGGDMYFAATDADRNVHVLKYAPDEPNSLSGQRLVHCSSFTLHSTNSCMMLLPRNEEFGSPQVPSFQNVGGQVDGSVFKIVPLSEEKYRRLYVIQQQIIDRELQLGGLNPRMERLANDFYQMGHSMRPMLDFNVIRRFCGLAIDRRKSIAQKAGRHAHFEAWRDIINIEFSMRSLCQGK
Protein: Delta-1-pyrroline-5-carboxylate synthase [Includes: Glutamate 5-kinase (GK) (EC 2.7.2.11) (Gamma-glutamyl kinase); Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase)] (A0A8I6AAN3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLRHVQRSGLQPFSQRLLPWVQSIALPRSHRVQPSAIRHVRSWSNIPFITVPLSRAHGKPFAHRSELKHAKRIVVKLGSAVVTRGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQALHSGQNHLKEMAIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAEPNSDLQGVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQSVTFGTKSRVGLGGMEAKVKAALWALQGGTSVVIANGTHPKVSGHVITDIVEGKKVGTFFSEVKPAGPTVEQQGEMARSGGRMLATLEPEQRAEIINHLADLLTDQREEILLANKKDLEEAEGRLAGPLLKRLSLSTSKLNSLAIGLRQIAASSQESVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAMHSNRILHLLTQEALSIHGVKEAIQLVNTREEVEDLCRLDKIIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRLVRDSKCEYPAACNALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSEVKSLRTEYGDLEVCIEVVDSVQEAIDHIHKYGSSHTDVIVTENEKTAEFFLQHVDSACVFWNASTRFSDGYRFGLGISTSRIHARGPVGLEGLLTTKWLLRGQDHVVSDFSEHGRLKYLHENLPVPQRHFS
Protein: Cinnamoyl-CoA reductase 1 (Mt-CCR1) (EC 1.2.1.44) (Caffeoyl-CoA reductase) (EC 1.2.1.-) (Coumaroyl-CoA reductase) (Feruloyl-CoA reductase) (Sinapoyl-CoA reductase) (A0A072VDF2)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Involved in the latter stages of lignin biosynthesis. Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes. Mediates the conversion of feruloyl-CoA to coniferylaldehyde. Also active, with a lower efficiency, toward coumaroyl-CoA, caffeoyl CoA and sinapoyl-CoA. Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A0A059TC02}.
Interaction partners:
- Caffeoyl-CoA O-methyltransferase
- Caffeoyl-CoA-O-methyltransferase
- Trans-cinnamate 4-monooxygenase
- Caffeoyl-CoA 3-O-methyltransferase
- Caffeoyl-CoA 3-O-methyltransferase
- Caffeoyl-CoA 3-O-methyltransferase
- caffeoyl-CoA O-methyltransferase
- Caffeoyl-CoA 3-O-methyltransferase
- Trans-cinnamate 4-monooxygenase
- Caffeoyl-CoA 3-O-methyltransferase
Sequence:
MPAATAAAAAESSSVSGETICVTGAGGFIASWMVKLLLEKGYTVRGTLRNPDDPKNGHLKKLEGAKERLTLVKVDLLDLNSVKEAVNGCHGVFHTASPVTDNPEEMVEPAVNGAKNVIIAGAEAKVRRVVFTSSIGAVYMDPNRSVDVEVDESCWSDLEFCKKTKNWYCYGKAVAEAAAWDVAKEKGVDLVVVNPVLVLGPLLQPTINASTIHILKYLTGSAKTYANATQAYVHVRDVALAHILVYEKPSASGRYLCAETSLHRGELVEILAKYFPEYPIPTKCSDEKNPRVKPHIFSNKKLKDLGLEFTPVSECLYETVKSLQDQGHLSIPNKEDSLAVKS
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (Q8IS82)
Organism: Giardia intestinalis (Giardia lamblia)
Interaction partners:
Sequence:
MPLAVFNIKGTRFCVPDYYKVTKALGAGAYGVVAEAVDTRTNTTVAIKKISNLFVHLVDSKRTLREITILRMLDHENIVKLLDVLVPEDPSNFDDLYVVFDFMQTDMHKIISSKQDLSPDHMQYFVYQLLRGLKYLHSANCVHRDLKPSNLLLNSDCALEICDLGLARLVDDHAAKTKELKDAEKHDTQMTEYVATRWYRAPEIILGWPQYGKPVDIFSVGCIFAELIARKPLFPGRDYIHQLHLILEVLGTPEKELLDRIASDSAKSYVLALKPSAPQDLSQKFPMLDEAGIDLLTRMLTLDPLKRITVNECLSHPYFEGIHDESDEPVYTGQPLELFFEKYELTKPLLEMCFLNEARKFHPDELKDEVAKRAKALGIPESVWM
Protein: chitinase (EC 3.2.1.14) (Q8KKF5)
Organism: Serratia plymuthica
Interaction partners:
Sequence:
MRKFNKPLLALLIGSTLCSAAQAATPGKPTLAWGNTKFAIVEVGQAATAYNNLVKLKTAADVSVSWNLWNGDTGTTAKVLLNGKEVWSGASTGASGTANFKVNKGGRYQMQVALCNAEGCTASDATEIVVADTDGSHLAPLKEPLLEKNKPYKQDSGKVVGSYFVEWGVYNRNFTVDKIPAQNLTHLLYGFIPVCGGDGINDSLKEIEGSFQALQRSCQGREDFKVSIHDPFAALQKGQKGVTAWDDPYKGNFGQLMALKQARPDLKILPSIGGWTVSDPFFFMGDKEKRDRFVGSVKEFLQTWKFFGGADIDWEFPGGQGANPKLGSAQDGATYVQLMKDLRAMLDQLSAETGRKYELTSAISAGKDKIDKVDYNTAQNSMDHIFLMSYDFYGAFDLKNLGHQTPLKAPAWKPDTAYTTVNGVNALLAQGVKPGKIVVGAAKYGRGWTGVSGYQNNNPFTGTATGPVKGTWENGIVDYRQIANEFMSGEWQYNYDATAEAPYVFKPSTGDLITFDDPRSVQAKGKYVLDKQLGGLFSWEIDADNGDILNNMNTSLGNSAGVQ
Protein: Beta-adducin (Adducin-63) (Erythrocyte adducin subunit beta) (Q05764)
Organism: Rattus norvegicus (Rat)
Function: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to the erythrocyte membrane receptor SLC2A1/GLUT1 and may therefore provide a link between the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin. Calmodulin binds preferentially to the beta subunit (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Alpha-adducin
- Tropomodulin-1
- Dematin actin binding protein
- Tropomodulin-2
- Tropomodulin 4
- RCG25684, isoform CRA_a.
- Ankyrin 2
- Protein 4.1
- Ankyrin-3
- Band 3 anion transport protein
Sequence:
MSEDTVPEAASPPPSQGQHYFDRFSEDDPEYLRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPASSMNFSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLVGDMAYYDFNGEMEQEADRINLQKCLGPTCKILVLRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALSSAGGTENLILLEQEKHRPHEVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYTYRHPFVQEKTKHKSEVEIPATVTAFVFEEDGVPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRNMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLDMRNKIREQNRQDIKSAGPQSQLLASVIAEKSRSPSTESQLASKGDADTKDELEETVPNPFSQLTDQELEEYKKEVERKKLEQEQEGEKDAATEEPGSPVKSTPASPVQSPTRAGTKSPAVSPSKASEDAKKTEVSEANTEPEPEKPEGVVVNGKEEEPCVEEVLSKGPGQMTTNADTDGDSYKDKTESVTSGPLSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES
Protein: K Homology domain-containing protein (D4YW53)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLSTMVHHFDANDYVSADWKPEPTLTTTATTDPLVATSSSSTTSSESHVTTASTSAPQSPTLLAPPISLQDVMTHASTDLLTPNGSANGVSTSQQQQYSAEYLSQLLKDKKQLAAFPNVFHHLERLADEEINKVRVVLFQCEFSKESAPLPDAEGDSTVHTEKVFVPAKEHPDYNFVGRILGPRGMTAKQLEQETGCKIMVRGRGSMRDKKKEELNRGKPNWEHLSEELHVLIQCEDTENRAKVKLMRAVEEVRKLLVPAPEGEDDLKRKQLMELAIINGTYRSGTDQSALAAAQLAAVKHQQQPFAAALQAAALQRGVLPMMANGLSRSPTMAVCGAPIVMSPSGRASSAGATATSQAALIMQQQSQLHAANAGNAALQQQAALLQQQQAAEYQQLLLSQAGLYDFSAMQQQYAAVGQNAAVAAAQAQAQAQYGALAAAAAANSAGNQQYADYAGVDLTSQQSAHGAMLNNRRLLGASREHPYKQ
Protein: Origin recognition complex subunit 6 (O74796)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. ORC binds to multiple sites within the ars1 origin of DNA replication in an ATP-independent manner.
Subcellular location: Nucleus.
Interaction partners:
- Origin recognition complex subunit 1
- Origin recognition complex subunit 2
- Origin recognition complex subunit 4
- Origin recognition complex subunit 3
- Origin recognition complex subunit 5
- Cell division control protein 18
- DNA replication licensing factor mcm2
- Cell division cycle protein cdt1
- Histone acetyltransferase type B catalytic subunit
- Nucleolar complex-associated protein 3
Sequence:
MERQQIIESLRRIIPTESTEYNERLISLGESFLEWSKYKHNLKATEELCRPYMAAHLACELLSNDLNLEINLLATPIPKKKYYKLFTYFQEILSPLTKSLAAKDDLMETITYLCTKLGGSTAIPYVKQLVKAVVTNDMRIEHKRGIIIAAYLLVSAKAFGKDELHINHTERRKAQSVLQDTSSALQIQYWMHVLSESWQYKEIPLNGIEGYESQKQRIKPWSGIASMIQIDYEKRLQNYPIWKACIEERIQYYKSQLEKDGTAS
Protein: NPC intracellular cholesterol transporter 2 (Epididymal secretory protein E1) (mE1) (Niemann Pick type C2 protein homolog) (Q9Z0J0)
Organism: Mus musculus (Mouse)
Function: Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment. Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1. May bind and mobilize cholesterol that is associated with membranes. NPC2 binds cholesterol with a 1:1 stoichiometry. Can bind a variety of sterols, including lathosterol, desmosterol and the plant sterols stigmasterol and beta-sitosterol (By similarity). The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport.
Subcellular location: Secreted {ECO:0000269|PubMed:10863096, ECO:0000269|PubMed:12591949, ECO:0000269|PubMed:21315718}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P61916}. Lysosome {ECO:0000250|UniProtKB:P61916}. Note=Interaction with cell-surface M6PR mediates endocytosis and targeting to lysosomes. {ECO:0000305|PubMed:12591949}.
Interaction partners:
- NPC intracellular cholesterol transporter 1
- NPC1-like intracellular cholesterol transporter 1
- Sterol regulatory element-binding protein cleavage-activating protein
- StAR-related lipid transfer protein 3
- Apolipoprotein B-100
Sequence:
MRFLAATILLLALVAASQAEPLHFKDCGSKVGVIKEVNVSPCPTDPCQLHKGQSYSVNITFTSGTQSQNSTALVHGILEGIRVPFPIPEPDGCKSGINCPIQKDKVYSYLNKLPVKNEYPSIKLVVEWKLEDDKKNNLFCWEIPVQITS
Protein: Testin (A4D0U5)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDLENKVKKMGLGHEQGFGAPCLKCKEKCEGFELHFWRKICRNCKCGQEEHDVLLSNEEDRKVGKLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPREVKEMEQFVKKYKSEALGVGDVKLPCEMDAQGPKQMNIPGGDRSTPAAVGAMEDKSAEHKRTQYSCYCCKLSMKEGDPAIYAERAGYDKLWHPACFVCSTCHELLVDMIYFWKNEKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQNWHLKHFCCFDCDSILAGEIYVMVNDKPVCKPCYVKNHAVVCQGCHNAIDPEVQRVTYNNFSWHASTECFLCSCCSKCLIGQKFMPVEGMVFCSVECKKRMS
Protein: Patterned expression site protein 10 (P41991)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000269|PubMed:7607073}. Cytoplasm {ECO:0000269|PubMed:7607073}.
Interaction partners:
- MI domain-containing protein
- Myosin-2
- Uncharacterized protein F22B7.9
Sequence:
MNKNEYMMHLLARTIRTRNDDMITPLITQLADMQVSMDILEKHNFPALVAEYAPFNKAAQSLSHSVLVWKNDELAQEKSYMLKEFVRICKDQHQPEEFLLRLTCSLINLNDFELTRSCFDIIVSFGLTLNAYDEFGIFRKAMEYQGQMEEADKIISDVDAMLLRNEFLEEDEAEEQADNEMDAFEEEGVEEVDQEVVDFNDNESVISETESGVFTDEELDMEDHAEVMRRHAQDQALVSEICMVFLAGCIKSGRSDVISAAIQFTGAFFYPLALLRKYDIQYLIYCYGSHNEDAELLMNHIKHLQAIEIAGERQEFFKMFMETTFRNAETVTDSVMAQMKGFLEDGDDFMISCTLHVFLKMPITLSQFKNSHVEACLENLESGLAAQLGFMLKMKIQLLEQIDYEIW
Protein: Inner membrane mitoribosome receptor MBA1, mitochondrial (Multi-copy bypass of AFG3 protein) (P38300)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial inner membrane-associated mitoribosome receptor that spatially aligns the mitoribosome exit tunnel with the membrane insertion machinery and allows cotranslational protein membrane insertion.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11381092, ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:25609543, ECO:0000269|PubMed:8690083}; Peripheral membrane protein {ECO:0000269|PubMed:11381092, ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:25609543, ECO:0000269|PubMed:8690083}; Matrix side {ECO:0000269|PubMed:11381092, ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:25609543, ECO:0000269|PubMed:8690083}. Note=Localizes near the mitoribosome exit tunnel. {ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:20404317}.
Interaction partners:
- Mitochondrial inner membrane protein OXA1
- Large ribosomal subunit protein uL29m
- Mitochondrial inner membrane m-AAA protease component YTA10
- Mitochondrial inner membrane m-AAA protease component YTA12
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein mL41
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein uL4m
Sequence:
MSVLRSTCLFFPPRSLLISFNKRRLFSTSRLILNKESETTKKKDKSKQQDFNPRHLGVAAEIFIPSAYKNLPNVFAHPLIVANALIRRLYTFGLNSVQVALFRFQSGIKPSFLLWKNKAIETYINVNTSFAHKNLSDIKGLVSLWVQEALEARSRQLPGNATLDWQLIKFNAVPKLVSVQPIMIPGMPLEHLQLVYKFDTKQRLIKVNQQTKKTETLDRDVVDYIAFLCDATTNDMILMGSLFESKPNDKLPKSYEDDAKVAIHRMKVNGDIYRLPPS
Protein: LEM domain-containing protein 2 (hLEM2) (Q8NC56)
Organism: Homo sapiens (Human)
Function: Nuclear lamina-associated inner nuclear membrane protein that is involved in nuclear structure organization, maintenance of nuclear envelope (NE) integrity and NE reformation after mitosis. Plays a role as transmembrane adapter for the endosomal sorting complexes required for transport (ESCRT), and is thereby involved in ESCRT-mediated NE reformation. Promotes ESCRT-mediated NE closure by recruiting CHMP7 and downstream ESCRT-III proteins IST1/CHMP8 and CHMP2A to the reforming NE during anaphase. During nuclear reassembly, condenses into a liquid-like coating around microtubule spindles and coassembles with CHMP7 to form a macromolecular O-ring seal at the confluence between membranes, chromatin, and the spindle to facilitate early nuclear sealing. Plays a role in the organization of heterochromatin associated with the NE and in the maintenance of NE organization under mechanical stress (By similarity). Required for embryonic development and involved in regulation of several signaling pathways such as MAPK and AKT (By similarity). Required for myoblast differentiation involving regulation of ERK signaling (By similarity). Essential for cardiac homeostasis and proper heart function (By similarity).
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:17097643, ECO:0000269|PubMed:28242692, ECO:0000269|PubMed:30905398, ECO:0000269|PubMed:32494070}; Multi-pass membrane protein {ECO:0000269|PubMed:16339967}. Nucleus envelope {ECO:0000269|PubMed:28242692}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:32494070}. Note=Lamina-associated protein residing in the inner nuclear membrane (INM) of the nuclear envelope (NE) (PubMed:16339967). The localization to the INM is dependent on LMNA (PubMed:16339967). Evenly distributed around the NE during interphase (PubMed:16339967). During metaphase, found in a reticular network (PubMed:28242692). Recruited to the reforming NE on chromatin disks in early anaphase (PubMed:28242692). In late anaphase, concentrates at the NE core proximal to spindle microtubules, and then broadening to a distributed nuclear rim pattern (PubMed:28242692, PubMed:32494070). {ECO:0000269|PubMed:16339967, ECO:0000269|PubMed:28242692, ECO:0000269|PubMed:32494070}.
Interaction partners:
- Charged multivesicular body protein 7
- IST1 homolog
- Barrier-to-autointegration factor
- Emerin
- Barrier-to-autointegration factor-like protein
- Ankyrin repeat and LEM domain-containing protein 2
- Prelamin-A/C
- Fizzy-related protein homolog
- Lamin-B1
Sequence:
MAGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGEARLRDEERLREEARPRGEERLREEARLREDAPLRARPAAASPRAEPWLSQPASGSAYATPGAYGDIRPSAASWVGSRGLAYPARPAQLRRRASVRGSSEEDEDARTPDRATQGPGLAARRWWAASPAPARLPSSLLGPDPRPGLRATRAGPAGAARARPEVGRRLERWLSRLLLWASLGLLLVFLGILWVKMGKPSAPQEAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPENLKSKCIPVMEAQEYIANVTSSSSAKFEAALTWILSSNKDVGIWLKGEDQSELVTTVDKVVCLESAHPRMGVGCRLSRALLTAVTNVLIFFWCLAFLWGLLILLKYRWRKLEEEEQAMYEMVKKIIDVVQDHYVDWEQDMERYPYVGILHVRDSLIPPQSRRRMKRVWDRAVEFLASNESRIQTESHRVAGEDMLVWRWTKPSSFSDSER
Protein: Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2'] (P59594)
Organism: Severe acute respiratory syndrome coronavirus (SARS-CoV)
Function: May down-regulate host tetherin (BST2) by lysosomal degradation, thereby counteracting its antiviral activity.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:20861307}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Colocalizes with S in the host endoplasmic reticulum-Golgi intermediate compartment (PubMed:20861307). Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:20861307}.
Interaction partners:
Sequence:
MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT
Protein: Odorant receptor 94a (Q9VCS9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 74a
- Odorant receptor 30a
- Odorant receptor 45b
- Odorant receptor 22c
Sequence:
MDKHKDRIESMRLILQVMQLFGLWPWSLKSEEEWTFTGFVKRNYRFLLHLPITFTFIGLMWLEAFISSNLEQAGQVLYMSITEMALVVKILSIWHYRTEAWRLMYELQHAPDYQLHNQEEVDFWRREQRFFKWFFYIYILISLGVVYSGCTGVLFLEGYELPFAYYVPFEWQNERRYWFAYGYDMAGMTLTCISNITLDTLGCYFLFHISLLYRLLGLRLRETKNMKNDTIFGQQLRAIFIMHQRIRSLTLTCQRIVSPYILSQIILSALIICFSGYRLQHVGIRDNPGQFISMLQFVSVMILQIYLPCYYGNEITVYANQLTNEVYHTNWLECRPPIRKLLNAYMEHLKKPVTIRAGNFFAVGLPIFVKTINNAYSFLALLLNVSN
Protein: Probable boron transporter 2 (Q9M1P7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable boron transporter. Boron is essential for maintaining the integrity of plants cell walls (By similarity).
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Probable aquaporin NIP5-1
- peptidylprolyl isomerase
- Receptor-like cytosolic serine/threonine-protein kinase RBK2
- MD-2-related lipid-recognition protein 3
- Probable disease resistance protein At1g61310
- Probable disease resistance protein At1g61300
- Putative disease resistance protein At5g05400
- Putative disease resistance protein At4g10780
- Probable disease resistance protein At5g47250
- AT3g50910/F18B3_190
Sequence:
MEETFVPFEGIKNDLKGRLMCYKQDWTGGIKAGFRILAPTTYIFFASAIPVISFGEQLERSTDGVLTAVQTLASTAICGIIHSIIGGQPLLILGVAEPTVIMYTFMFNFAKGRPELGRNLFLAWSGWVCVWTSLILFVLAICGACSFINRFTRVAGELFGLLIAMLFMQQAIKGLVDEFRAPAREDLKLVEFLPSWRFANGMFALVLSFGLLITALRSRKARSWRYGTGWLRSLVADYGVPLMVLVWTGVSYIPTGDVPKGIPRRLFSPNPWSPGAYENWTVVKEMLQVPIVYIIGAFIPATMIAVLYYFDHSVASQLAQQKEFNLRKPSSYHYDLLLLGFLTLMCGLLGIPPSNGVIPQSPMHTKSLATLKYQLLRNRLVATARKSIKQNASLGQLYGNMQDVYNQMQTPLVYQQPQGLKELRESTIQATTFTGNLDAPVDETLFDIEKEIDDLLPIEVKEQRVSNLLQAVMVGGCVAAMPLLKMIPTSVLWGYFAFMAIESLPGNQFWERILLLFTAPSRRFKVLEDNHATFVETVPFKTIAMFTIFQTTYLLTCFGLTWIPIAGVMFPLLIMFLIPVRQYILPRFFKSAHLQDLDAAEYEEAPALPFHLAVPEAEMGSTASYPCDSEILDEFITRSRGEFRHTCSPKVTSSTSTPVYNRNLSQVFSPRVIDLRGEMSPRLSGKGQNSPKPSPLNPSSSSK