wanglab/gogpt-training-data huggingface dataset:
Protein: Isoflavonoid malonyl transferase 1 (B4Y0U0)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Interaction partners:
Sequence:
MASNNNSNIKVHDHFKVVPPSSTKTTSIPLTFFDIFWLRFHPVERVFFYTLPNSQSHPSFFFQTIVPNLKSSLSLTLQHFLPLAGNIVWPSDSSKPIIQFDPNDDGVSLIIAESDSDFNHVVENSPHEASLSRSFIPHLESSDSFASIMSLQITLFPNSGFSIGISTHHAVLDGKSSTMFVKAWAYLCKKAIERDESPTLLSEFEPSFNREVIKDPNGNNVMDLVSTLFPSEKGNDRSLKIFPFEPQLEDSVRATFKLKHEDLDKIKQRVLSTWEIFDTKESKPQTLSSFVITCAYSLVCVAKAIHGAHNDKEKFSFVFSVDCRARLEPTIPNNYLGNCVWAYFIDTQPLDFIKEDGVFLVAKSIYEKIKMINEKGFLEGEINDMFNKIISLSSEGFEFMGVAGSHRFGVYEIDFGWGRPEKVEIVSIDRGVTIGLAESKDSKGGIEVGLALNKPVMDIFSTLFLEGLSYNE
Protein: Telomere length regulation protein TEL2 homolog (Q9DC40)
Organism: Mus musculus (Mouse)
Function: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. May be involved in telomere length regulation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000305}.
Interaction partners:
- TELO2-interacting protein 1 homolog
- Serine/threonine-protein kinase mTOR
- TELO2-interacting protein 2
- Target of rapamycin complex subunit LST8
- DEP domain-containing mTOR-interacting protein
- Rapamycin-insensitive companion of mTOR
- Regulatory-associated protein of mTOR
- Fanconi anemia group M protein homolog
- Serine/threonine-protein kinase ATR
- Proline-rich AKT1 substrate 1
Sequence:
MDPALSAVRLTVQEAIHILSSSEDAGHILSTLGTLKRYLGGTEDPVLPEEKEEFATVHFSAVLRCLVSKLSPGWLELSPGGQLERLWESFFLDGPPDQAFLVLMEAIESTAGPSFRLMKMAQLLDTFLSTGRVAALMEEQCRPQTKPSFPLFQETLLSKVVGLPDLLGNCLQRDNLTQFFPQNYFPLLGQEVVQALKAVVNFLQDGLDCSVSFVSRVLGKVCIQGRKREILSVLVPQLTVLTQDSCLWQRVCWRLVEQVPDRAVEAVLTGLVEAAPRPEVLSRLLGNLVVKNKKARFVVTRKLLLLQYQHTTPMVQSLLGYLALDSQRRPLLIQVLKELLETWGCSSAVRHTPLEQQCYISKAILVCLAHLGEPELQDIRDELLASMMAGVKCRLDSSLPPVRRLGMIVAEVISSRIHPEGPLLKFQYEDDEMSRELLALATPEPAGDCSSVSRGPSPAPVDTESPVEMPEKAVESDVPPTQPQGSDSELDSDDEFIPYDMSGDRELKSSKEPLYIRDCVEALTTSEDMERWEASLKGLEGLVYRSPTATREVSVELAKVLLHLEEKTCVAEFEQLRQSALVAVTVTDPEQVAKYLTSQFYGLNYSLRQRMDILDVLVLAAQALSRPKSLQRRSQHGPPVPGTMCSPALAVSQTGNVAAPDWQVVVEERIRSKTRRFSKGCPQRELSGVPNEFSSVAGYFFFPLLQHFDRPLVTFDLLGDDQLVLGRLTHTLASLMYLAVNTTVAVPMGKALLEFVWALRFHVDIYVRRGLLSAVSSVLLSVPTERLLGDLPDELLEARSWLADVAEKDVDEDCRELAVRALLLLERLKDKLLSSSSPQP
Protein: Beta-ureidopropionase (EC 3.5.1.6) (Beta-alanine synthase) (N-carbamoyl-beta-alanine amidohydrolase) (Q03248)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes a late step in pyrimidine degradation. Converts N-carbamoyl-beta-alanine (3-ureidopropanoate) into beta-alanine, ammonia and carbon dioxide. Likewise, converts N-carbamoyl-beta-aminoisobutyrate (3-ureidoisobutyrate) into beta-aminoisobutyrate, ammonia and carbon dioxide.
Subcellular location: Cytoplasm.
Interaction partners:
- Dihydropyrimidine dehydrogenase [NADP
- Dihydropyrimidinase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Aminoacylase-1A
Sequence:
MAGPEWQSLEQCLEKHLPPDDLSQVKRILYGKQTRNLDLPRKALEAASERNFELKGYAFGAAKEQQRCPQIVRVGLVQNRIPLPTSAPVAEQVSALHKRIEEIAEVAAMCGVNIICFQEAWNMPFAFCTREKLPWTEFAESAEDGLTTRFCQKLAKKHNMVVISPILERDRDHGGVLWNTAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSVNGAEIIFNPSATIGELSESMWPIEARNAAIANHCFTCALNRVGQEHYPNEFTSGDGKKAHHDLGYFYGSSYVAAPDGSRTPGLSRNQDGLLVTELNLNLCQQINDFWTFKMTGRLEMYARELAEAVKPNYSPNIVKEDLVLAPSSG
Protein: Antitoxin ParD1 (P9WIJ7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in E.coli neutralizes the effect of cognate toxin ParE1.
Interaction partners:
- Toxin ParE1
- Antitoxin ParD2
- Ribonuclease VapC30
- Probable transcriptional regulatory protein
- Toxin ParE2
- NAD-dependent protein deacylase
- HTH-type transcriptional regulator LrpA
- Transcriptional regulator Rv3488
- Possible transcriptional regulatory protein NadR
- Probable transcriptional regulatory protein
Sequence:
MGKNTSFVLDEHYSAFIDGEIAAGRYRSASEVIRSALRLLEDRETQLRALREALEAGERSGSSTPFDFDGFLGRKRADASRGR
Protein: Single-strand-selective monofunctional uracil-DNA glycosylase 1 (D6RIA4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEPVGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFG
Protein: Potassium channel subfamily K member (B8A573)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004221}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Perikaryon {ECO:0000256|ARBA:ARBA00004484}. Recycling endosome {ECO:0000256|ARBA:ARBA00004172}. Synaptic cell membrane {ECO:0000256|ARBA:ARBA00034109}.
Interaction partners:
Sequence:
MLQSLAGNSCVRLIQSNKSAWYFLFLVLGYVLYLIFGAVVFSSVELPYEDDLRQQLREIKRLFLQEHQCLSEERLERFLSKALEASNYGVSILNNASASWNWDFTSSLFFASTVLSTTGYGHTAPLSDGGKAFCIIYSVIGIPFTLLFLTAVVQRIMVYSTWRPIMYVHTRWGLSKPLVALVHATLLAVVAVSCFFLIPAAIFSALEENWNFLESFYFCFISLSTIGLGDYVPGEAFNQRFRELYKLGITVYLLLGLIAMLVVLETFCELQQLKQLRKMFYLKKEKPQDRLAIMEHDHLAFSSMPDATIHSPHEDKTEPFVDFPVLTSPGGDDPMIK
Protein: E3 ubiquitin-protein ligase SH3RF3 (EC 2.3.2.27) (Plenty of SH3s 2) (SH3 domain-containing RING finger protein 3) (SH3 multiple domains protein 4) (Q8TEJ3)
Organism: Homo sapiens (Human)
Function: Has E3 ubiquitin-protein ligase activity.
Interaction partners:
Sequence:
MLLGASWLCASKAAAAAAQSEGDEDRPGERRRRRAAATAAGAGEDMDESSLLDLLECSVCLERLDTTAKVLPCQHTFCRRCLESIVCSRHELRCPECRILVGCGVDELPANILLVRLLDGIRQRPRAGTSPGGSPPARPIPGQSAAPTLAGGGGGAAGSTPGSPVFLSAAAGSTAGSLRELATSRTAPAAKNPCLLPYGKALYSYEGKEPGDLKFNKGDIIVLRRKVDEQWYHGELHGTQGFLPASYIQCIQPLPHAPPQGKALYDFEMKDKDQDKDCLTFTKDEILTVLRRVDENWAEGMLGDKIGIFPLLYVELNDSAKQLIEMDKPCPAAASSCNASLPSDSGAVASVAPSPTLSSSGAVSAFQRRVDGKKNTKKRHSFTALSVTHRSSQAASHRHSMEISAPVLISSSDPRAAARIGDLAHLSCAAPTQDVSSSAGSTPTAVPRAASVSGEQGTPPKVQLPLNVYLALYAYKPQKSDELELHKGEMYRVLEKCQDGWFKGASLRTGVSGVFPGNYVTPVSRVPAGGAGPPRNNVVGGSPLAKGITTTMHPGSGSLSSLATATRPALPITTPQAHAQHPTASPPTGSCLRHSAQPTASQARSTISTAAHSAAQAQDRPTATVSPLRTQNSPSRLPATSLRPHSVVSPQHSHQPPVQMCPRPAIPLTSAASAITPPNVSAANLNGEAGGGPIGVLSTSSPTNTGCKLDEKKSEKKEKKSGLLKLLAGASTKKKSRSPPSVSPTHDPQVAVDALLQGAVGPEVSSLSIHGRAGSCPIESEMQGAMGMEPLHRKAGSLDLNFTSPSRQAPLSMAAIRPEPKLLPRERYRVVVSYPPQSEAEIELKEGDIVFVHKKREDGWYKGTLQRNGRTGLFPGSFVESF
Protein: Homeobox protein meis3-A (XMeis3) (Q5U4X3)
Organism: Xenopus laevis (African clawed frog)
Function: Caudalizing protein which is required to pattern the anterior/posterior (A/P) axis during central nervous system (CNS) formation. Inhibits anterior neural expression and acts as a transcriptional activator to induce posterior neural gene expression. Maintains a proper A/P balance required for hindbrain formation by activating the FGF/MAPK pathway, which modulates the planar cell polarity (PCP) pathway. Interacts with retinoid signaling during hindbrain patterning.
Subcellular location: Nucleus {ECO:0000255, ECO:0000305}.
Interaction partners:
Sequence:
MAQRYDEMLHYPTLDGMPLAGFGDAHTGRALQHHSLSQSAPYGSTGAGHRVPMPPGMGSNDGLKREKDEIYGHPLFPLLALVFEKCELATCSPRDNSGSFPGGDVCSSDSFNEDIAVFAKQVRTEKPLFSSNPELDSLMIQAIQVLRFHLLELEKVHDLCDNFCHRYITCLKGKMPIDLVIDDRDGSSKSDLEDFTGSCTSLSDQNNSWLRDHDETGSAHSGTPGPSSGGLASQSGDNSSEQGDCMDNSVASPSTGDDDDLDRDKKRNKKRGIFPKVATNIMRAWLFQHLSHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRTGQGGAPYSPDGQNMGGYVMDGQQHMGIRPPGFQGIPGDYTAAPSTMPMGFPPAGYTPAIPPHSAGLRHGPSLHSYLPGHPHHASMILPAGASPHHLVSAQSPADALLNGQNIDIHAH
Protein: Rab3 GTPase-activating protein non-catalytic subunit (Rab3 GTPase-activating protein 150 kDa subunit) (Rab3-GAP p150) (Rab3-GAP150) (Rab3-GAP regulatory subunit) (Q5U1Z0)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of the Rab3 GTPase-activating (Rab3GAP) complex composed of Rab3gap1 and Rab3gap2, which has GTPase-activating protein (GAP) activity towards various Rab3 subfamily members (RAB3A, RAB3B, RAB3C and RAB3D), RAB5A and RAB43, and guanine nucleotide exchange factor (GEF) activity towards RAB18 (By similarity). As part of the Rab3GAP complex, acts as a GAP for Rab3 proteins by converting active RAB3-GTP to the inactive form RAB3-GDP (By similarity). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones (By similarity). The Rab3GAP complex, acts as a GEF for RAB18 by promoting the conversion of inactive RAB18-GDP to the active form RAB18-GTP (By similarity). Required for recruiting and activating RAB18 at the endoplasmic reticulum (ER) membrane where it maintains proper ER structure (By similarity). Required for normal eye and brain development (By similarity). May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9733780}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2M9}. Note=In neurons, it is enriched in the synaptic soluble fraction. {ECO:0000269|PubMed:9733780}.
Interaction partners:
- Rab3 GTPase-activating protein catalytic subunit
- Ras-related protein Rab-18
- TBC1 domain family, member 20.
Sequence:
MACSIVQFCSFQDLQSARDFLFPQLREETPGALRRDPSKTSNWEDDSWGAWEETEPQEPEEEGNTSKTQKHSWLQECVLSLSPTSDLMVIAREQKAAFLVRKWKHSDKGKEEMQFAVGWSGSVSAEEGEYVTSALCIPLASQKRSSTGRPDWTCIVVGFTSGYVRFYTEGVLLLAQLLNEDRVLQLKCRTYEIPRHPGVTEQNEELSILYPAAIVTIDGFSLFQSLRACRNQVAKAAASGNENIQPPPLAYKKWGLQDIDTIIDHASIGIMTLSPFDQMKTASNIGGFNAAIKNSPPAMSQYITVGSSPFTGFFYALEGSTQPLLSHVALAVASKLTSALFSAASGWLGWKSKHEEETVQKQKPKMEPATPLAVRFGLPDSRRHGESICLSPCNTLAAVTDDFGRVILLDVARGIAIRMWKGYRDAQIGWIQIVEDLHERVPEKGDFSPFGNTQGPSRVAQFLVIYAPRRGILEVWSTQQGPRVGAFNVGKHCRLLYPGYKIMGLNNVTSQSWQPQTYQICLVDPVSASVKAVNVPFHLALSDKKSERAKDLHLVKKLAALLRAKSPRPDSFEAEIKELILDIKYPATKKQALESILASDRVSFSCLRNVTQTSMDTLKNQELESVDEGLLQFCASKLKLLHLYESVSQLNTLDFHSDTPFSDNDLAVLLRLDDKELLKLRALLEKYKQENTKATVRFSEDADGVLPVKTFLEYLDYEKDALSIRKTSEEECVALGSFFFWKCLHGESSTEDMCHTLESAGLSPQQLLSLLLSVWLSKEKDILDKPQSVCCLHTMLSLLSKMKVAIDETWDSQSVSPWWQQMRMACIQSENNGAALLSAHVGHSVAAQMSSSATDKKFSQMVLDADAEALTDSWEALSLDTEYWKLLLRQLEDCLILQTLLHSRASPPAAKASSPQTEPLPRLSVKKLLEGGKGGIADSVAKWIFKQDLSPELLKCANREKDVENPDEPREGIARSPPEVSEVETDLGAVPDLLRLAYEQFPCSLELDVLHAHCCWEYVVQWNKDPEEARFLVRSIEHLRHILNPHVQNGISLMMWNTFLVKRFSAATYLMDKVGKSPKDRLCRRDVGMSDTALTSFLGSCLDLLQTSLEADISRDEVQVPVLDTEDAWLSVEGPTSIVELALEQKPIHYPLVEHHSILCSILYAAMSFSLKSVKPLALFDSKGKNAFFKDLTSIQLLPSGEMDPNFISVRQQFLLKVVSAAVQAQHSKDKDPSARAADTHGQDLNWTALAVDLAHHLQVSEDVIRRHYVGELYSYGADLLGEEAILQVQDKEVLASQLLVLTGQRLAHALFHTQTKEGMELLARLPPTLCTWLKAMNPQDLQNTGVPVAATAKLVHKVMELLPEKHGQYSLALHLIEAVEAMATL
Protein: Mitochondrial transcription termination factor 4 (C9JX74)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARQTPHLGEQRRTTASLLRKLTTASNGGVIEELSCVRSNNYVQEPECRRNLVQCLLEKQGTPVVQGSLELERVMSSLLDMGFSNAHINELLSVRRGASLQQLLDIISEFILLGLNPEPVCVVLKKSPQLLKLPIMQMRKRSSYLQKLGLG
Protein: UDP-glucuronosyltransferase (EC 2.4.1.17) (F1QAF6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}. Membrane {ECO:0000256|RuleBase:RU362059}; Single-pass membrane protein {ECO:0000256|RuleBase:RU362059}.
Interaction partners:
- Cytochrome P450 1A
- Iodothyronine deiodinase
- Transthyretin
- Cytochrome P450 1A
- Iodothyronine deiodinase
- Cytochrome P450, family 3, subfamily A, polypeptide 65
- Cytosolic sulfotransferase 1
- Thyroglobulin.
- Thyroid hormone receptor beta
- Sulfotransferase
Sequence:
MRTLPVPAQGLLALLCLFSFESVQAGKVLVLPVDGSHWLSMKILVEELSNRGHEMVVLVPETSILIKKSGKYSTKTYPVSFTHDDLAENLKEIQNSALEKAPKLTDIVVNFRNLLQFLTMQSKTCEGLLYNEPLMKSLREMGFDAMLTDPFLPCGTIIADSFSIPAVYFLRLIPCRLDEAAAQCPSPPSFMPRYSSGFTDKMTFPQRLVNTLLTVVEGFLCRSMYESADELASKYLQKETTYAELLGHGAVWLLRYDFAFEFPRPQMPNMVQIGGINCVKRAPLTKELEEFVNGSGEHGFVVFTLGSMVSQLPEAKAREFFEAFRQIPQRVLWRYTGPVPENAPKNVKLMKWLPQNDLLGHPKVRAFVTHGGSHGIYEGICNGVPMVMLPLFGDQGDNAQRLVSRGVAESLTIYDVTSEKLLVALKKVINDKSYKEKMMKLSAIHRDRPIEPLDLAVFWTEFVMRHKGAEHLRPAAHDLNWIQYHSLDVIGFLLLILLTVIFVTVKSCMFCFRKCFKKSQKKKKA
Protein: Lamin-C (pG-IF) (Q03427)
Organism: Drosophila melanogaster (Fruit fly)
Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin (By similarity). In spermatocytes, regulates cytokinesis during meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:7593280}. Nucleus lamina {ECO:0000269|PubMed:18723885, ECO:0000269|PubMed:27402967}. Note=Nuclear periphery (PubMed:7593280). In premeiotic nuclei of primary spermatocytes, localization to the nuclear lamina depends on type-B lamin Lam. In spermatocytes, temporarily depleted between anaphase I and telophase I, and anaphase II and telophase II. {ECO:0000269|PubMed:27402967, ECO:0000269|PubMed:7593280}.
Interaction partners:
- Lamin-B receptor
- Barrier-to-autointegration factor
- AT03047p
- Lamin Dm0
- Inner nuclear membrane protein Man1
- Caspase drICE
- Otefin
- Nuclear pore complex protein Nup153
Sequence:
MSARRVTLNTRVSRASTSTPVGGASTSSRVGATSPTSPTRTSRQQEKEELQHLNDRLACYIDRMRNLENENSRLTQELNLAQDTVNRETSNLKAVYEKELAAARKLLDETAKEKAKLEIDIKRLWEENDDLKPRLDKKTKEATVAENNARLYENRYNEVNGKYNQSLADRKKFEDQAKELALENERLRRQLDDLRKQLEAETLARVDLENQNQSLREELAFKDQVHTQELTETRSRRQIEISEIDGRLSRQYEAKLQQSLQELRDQYEGQMRINREEIELLYDNEIQNLKAAANRAAQGSALATEEVRLMRTKIDGLNAKLQNLEDTNAGLNARIRELENLLDTERQRHNQYIASLEAELQRMRDEMAHQLQEYQGLMDIKVSLDLEIAAYDKLLCGEERRLNIESPGRPTTDSGISSNGSHLTASASSRSGRVTPSGRRSATPGISGSSAVKRRRTVIDESEDRTLSEYSVNAAAKGDLEIIEADVEGRFIKLHNKGTEEINLTGWQLTRIAGDEELAFKFSRGSKVLGGASVTIWSVDAGTAHDPPNNLVMKKKWPVANSMRSVLANADKEDVASYDRVRANVSSHTSRHRSSGTPSTGFTLGSGAGSTGVRSLFSLLF
Protein: Gamma-aminobutyric acid receptor exp-1 (Expulsion defective protein 3) (GABA(A) receptor) (G5ECJ0)
Organism: Caenorhabditis elegans
Function: GABA receptor that functions as an excitatory cation channel. Permeable to monovalent cations such as Na(+) and K(+). Has negligible divalent cation permeability. Does not act as a chloride channel. Mediates enteric muscle contractions required for defecation. Probably by regulating the defecation motor program, required for fatty acid uptake by intestinal cells.
Subcellular location: Synapse {ECO:0000269|PubMed:14555952}. Cell membrane {ECO:0000250|UniProtKB:P18505}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18505}.
Interaction partners:
- AcetylCholine Receptor
- AcetylCholine Receptor
- Ligand-Gated ion Channel
- Proton-gated ion channel subunit pbo-5
Sequence:
MSASILILATCHQVLADFNSYVVPQPHAQRDHRQDISQHYDYLMEENDEPLGRGAAPSKYRSSHGQAQHRPEMTESENFAQPNTESVFSSGGVDSYGETRDFLQFLRRIQYDHRQVPENEKGEATYVEVSVVVSNIRAVSEVTMDYALELFYRESWRDPRLQYDRKLFKNKTELALHESYTNFLWFPDTFVPNAIASKNPQRNSISHRSLLRLDETGKLLYSRRISLVCECTMDLTLFPFDKQLCKLGIESYGYTADHVVYKWSKGARTALELKKIRLPDFTIQEAYVTSQMESYATGNYSRLYVCFVFSRSSGFCFLQLIIPSTAVVITSWVSLWMETETEFQDMISIILAITFLIFSYNEMMPRVSYIKAMDIYLGVCFMIVFLSLIKLALVKYMRQKIMLTSDSGNSLREMSQMSTRQRLRARKTSNMNFRNNGGGSIPINEEHQQMLTVPNGEDKMANGDDKEANNNGKSHLSDMLEIRITQRTMHRFHWISQMLFFFGFVIFCLFYFLIYPNLHIVSVDPACDKNLAEWFADIY
Protein: Geranylgeranyl transferase type-1 subunit beta (EC 2.5.1.59) (Geranylgeranyl transferase type I subunit beta) (GGTase-I-beta) (Type I protein geranyl-geranyltransferase subunit beta) (P53610)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of proteins with the C-terminal sequence Cys-aliphatic-aliphatic-X. Known substrates include RAC1, RAC2, RAP1A and RAP1B.
Interaction partners:
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Sequence:
MAATEDDRLAGSGEGERLDFLRDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQVLPTEDRSNLDRCGFRGSSYLGIPFNPSKNPGTAHPYDSGHIAMTYTGLSCLIILGDDLSRVDKEACLAGLRALQLEDGSFCAVPEGSENDMRFVYCASCICYMLNNWSGMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFSEKELNRIKRWCIMRQQNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSLMEESGICKVHPALNVSTRTSERLRDLHQSWKTKDSKQCSDNVHISS
Protein: Protein NDRG3 (N-myc downstream-regulated gene 3 protein) (Q9UGV2)
Organism: Homo sapiens (Human)
Interaction partners:
- Serine/threonine-protein kinase 38-like
- N-myc proto-oncogene protein
Sequence:
MDELQDVQLTEIKPLLNDKNGTRNFQDFDCQEHDIETTHGVVHVTIRGLPKGNRPVILTYHDIGLNHKSCFNAFFNFEDMQEITQHFAVCHVDAPGQQEGAPSFPTGYQYPTMDELAEMLPPVLTHLSLKSIIGIGVGAGAYILSRFALNHPELVEGLVLINVDPCAKGWIDWAASKLSGLTTNVVDIILAHHFGQEELQANLDLIQTYRMHIAQDINQDNLQLFLNSYNGRRDLEIERPILGQNDNKSKTLKCSTLLVVGDNSPAVEAVVECNSRLNPINTTLLKMADCGGLPQVVQPGKLTEAFKYFLQGMGYIPSASMTRLARSRTHSTSSSLGSGESPFSRSVTSNQSDGTQESCESPDVLDRHQTMEVSC
Protein: Intraflagellar transport protein 27 homolog (Putative GTP-binding protein RAY-like) (Rab-like protein 4) (Q9BW83)
Organism: Homo sapiens (Human)
Function: Small GTPase-like component of the intraflagellar transport (IFT) complex B that promotes the exit of the BBSome complex from cilia via its interaction with ARL6. Not involved in entry of the BBSome complex into cilium. Prevents aggregation of GTP-free ARL6. Required for hedgehog signaling. Forms a subcomplex within the IFT complex B with IFT25. Its role in intraflagellar transport is mainly seen in tissues rich in ciliated cells such as kidney and testis. Essential for male fertility, spermiogenesis and sperm flagella formation. Plays a role in the early development of the kidney. May be involved in the regulation of ureteric bud initiation (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:25443296}. Cytoplasm {ECO:0000250|UniProtKB:Q9D0P8}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q9D0P8}. Note=Localizes to the sperm flagellum. {ECO:0000250|UniProtKB:Q9D0P8}.
Interaction partners:
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 25 homolog
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 70B
- Intraflagellar transport protein 22 homolog
- Intraflagellar transport protein 74 homolog
- Intraflagellar transport protein 57 homolog
- TRAF3-interacting protein 1
Sequence:
MVKLAAKCILAGDPAVGKTALAQIFRSDGAHFQKSYTLTTGMDLVVKTVPVPDTGDSVELFIFDSAGKELFSEMLDKLWESPNVLCLVYDVTNEESFNNCSKWLEKARSQAPGISLPGVLVGNKTDLAGRRAVDSAEARAWALGQGLECFETSVKEMENFEAPFHCLAKQFHQLYREKVEVFRALA
Protein: TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2) (P39429)
Organism: Mus musculus (Mouse)
Function: Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain. Isoform 2 does not seem to mediate activation of NF-kappa-B but inhibits isoform 1 activity. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE.
Subcellular location: Cytoplasm.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 1A
- Mitochondrial antiviral-signaling protein
- NF-kappa-B essential modulator
- Baculoviral IAP repeat-containing protein 2
- Mitogen-activated protein kinase kinase kinase 5
- Receptor-interacting serine/threonine-protein kinase 1
- TNF receptor-associated factor 1
- Tumor necrosis factor
- TNF receptor-associated factor 3
- Baculoviral IAP repeat-containing protein 3
Sequence:
MAAASVTSPGSLELLQPGFSKTLLGTRLEAKYLCSACKNILRRPFQAQCGHRYCSFCLTSILSSGPQNCAACVYEGLYEEGISILESSSAFPDNAARREVESLPAVCPNDGCTWKGTLKEYESCHEGLCPFLLTECPACKGLVRLSEKEHHTEQECPKRSLSCQHCRAPCSHVDLEVHYEVCPKFPLTCDGCGKKKIPRETFQDHVRACSKCRVLCRFHTVGCSEMVETENLQDHELQRLREHLALLLSSFLEAQASPGTLNQVGPELLQRCQILEQKIATFENIVCVLNREVERVAVTAEACSRQHRLDQDKIEALSNKVQQLERSIGLKDLAMADLEQKVSELEVSTYDGVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVVMKGPNDALLQWPFNQKVTLMLLDHNNREHVIDAFRPDVTSSSFQRPVSDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL
Protein: Envelope glycoprotein H (gH) (Q6SW67)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis (By similarity). In human cytomegalovirus, forms two distincts complexes to mediate viral entry, a trimer and a pentamer at the surface of the virion envelope. The gH-gL-gO trimer is required for infection in fibroblasts by interacting with host PDGFRA. The gH-gL-UL128-UL130-UL131A pentamer is essential for viral entry in epithelial, endothelial and myeloid cells via interaction with host NRP2.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04033, ECO:0000269|PubMed:23804643}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04033}.
Interaction partners:
Sequence:
MRPGLPSYLIILAVCLFSHLLSSRYGAEAVSEPLDKAFHLLLNTYGRPIRFLRENTTQCTYNSSLRNSTVVRENAISFNFFQSYNQYYVFHMPRCLFAGPLAEQFLNQVDLTETLERYQQRLNTYALVSKDLASYRSFSQQLKAQDSLGEQPTTVPPPIDLSIPHVWMPPQTTPHGWTESHTTSGLHRPHFNQTCILFDGHDLLFSTVTPCLHQGFYLIDELRYVKITLTEDFFVVTVSIDDDTPMLLIFGHLPRVLFKAPYQRDNFILRQTEKHELLVLVKKDQLNRHSYLKDPDFLDAALDFNYLDLSALLRNSFHRYAVDVLKSGRCQMLDRRTVEMAFAYALALFAAARQEEAGAQVSVPRALDRQAALLQIQEFMITCLSQTPPRTTLLLYPTAVDLAKRALWTPNQITDITSLVRLVYILSKQNQQHLIPQWALRQIADFALKLHKTHLASFLSAFARQELYLMGSLVHSMLVHTTERREIFIVETGLCSLAELSHFTQLLAHPHHEYLSDLYTPCSSSGRRDHSLERLTRLFPDATVPATVPAALSILSTMQPSTLETFPDLFCLPLGESFSALTVSEHVSYIVTNQYLIKGISYPVSTTVVGQSLIITQTDSQTKCELTRNMHTTHSITVALNISLENCAFCQSALLEYDDTQGVINIMYMHDSDDVLFALDPYNEVVVSSPRTHYLMLLKNGTVLEVTDVVVDATDSRLLMMSVYALSAIIGIYLLYRMLKTC
Protein: Cerberus (Cer) (Xcer) [Cleaved into: Cerberus long (Cer-L); Cerberus short (Cer-S)] (P70041)
Organism: Xenopus laevis (African clawed frog)
Function: Inhibits wnt, nodal/nr-1 and bmp signaling in the embryo to promote head formation and anterior neural induction. Within the endoderm, acts as an essential mediator of nodal/nr-1-induced cardiogenesis in the overlying mesoderm.
Subcellular location: Secreted {ECO:0000269|PubMed:8757128}.
Interaction partners:
Sequence:
MLLNVLRICIIVCLVNDGAGKHSEGRERTKTYSLNSRGYFRKERGARRSKILLVNTKGLDEPHIGHGDFGLVAELFDSTRTHTNRKEPDMNKVKLFSTVAHGNKSARRKAYNGSRRNIFSRRSFDKRNTEVTEKPGAKMFWNNFLVKMNGAPQNTSHGSKAQEIMKEACKTLPFTQNIVHENCDRMVIQNNLCFGKCISLHVPNQQDRRNTCSHCLPSKFTLNHLTLNCTGSKNVVKVVMMVEECTCEAHKSNFHQTAQFNMDTSTTLHH