wanglab/gogpt-training-data huggingface dataset:
Protein: Morphogenetic regulator of filamentous growth protein 1 (Q07684)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcriptional regulator with a general role in all morphogenetically distinct forms of filamentous growth, namely haploid invasive growth, biofilm formation, and diploid pseudohyphal growth. May control FLO11 gene expression as part of a promoter-bound complex with FLO8 and MSS1.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22984072}.
Interaction partners:
- Transcription activator MSS11
- Flocculation protein FLO1
- Homeobox protein YOX1
- Homeobox protein YHP1
Sequence:
MYQGPPQPPPQAVPMPYIVNNNTPPYPNGNINFPPTAQQNIPPTVYPQQVPFPGQPQGGQFPQPSSEQQVFNQLPQVTQTFHNSAQNTNATGGPGSGSMPMFTPVASFPHPMATAATAAAPLPRSASQASLSMLRVPYHVRKYLSNLAMLKLYEIINEVNTAMGKIGLLSFWTELISDIFTPDAVIRYSKKSMTDYREFEFIIPVFPVICSTLGRFGIVRMEVKVLQLKTQVLSNSTIFFNCPRVTFVYYYPDGSYITHFSQMKGAFDLDLKINWLDVSMHSFVPDIEWNAVERLLSDDTKSTEIEQIFRKLKQEDVKEQGNSFAENNATNVPPNFEAITQLRSYFDVFRNVSVFGTQEGLMRVMQISTVMSTLKNLRKFQIEKNIDSPVTALSAYIDADKKDSGSEPLHAKRRRNSGISPRTTTLGPNGNSNTSNEELPTSDVNDINKDMTKKKMKF
Protein: Predicted GPI-anchored protein 1 (Q5ACL7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Plays a role in cell wall stability and rigidity. Required for normal adhesion to host cells and for adherence during biofilm formation. Necessary for proper oxidative stress response.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MNFNKFLIIISCYLACVFALANQNDGGDDDSKTKKTTTWVWVTTTIGGQLATISTAYSQKFISTHSSEDAKSVASGEIGLGSLSGSVGGIKTYSQTTITNANIAPSNNNVFLGIESLYTGIVGGIVLILGLL
Protein: Zinc finger protein 254 (Bone marrow zinc finger 5) (BMZF-5) (Hematopoietic cell-derived zinc finger protein 1) (HD-ZNF1) (Zinc finger protein 539) (Zinc finger protein 91-like) (O75437)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MPGPPRSLEMGLLTFRDVAIEFSLEEWQHLDIAQQNLYRNVMLENYRNLAFLGIAVSKPDLITCLEQGKEPWNMKRHEMVDEPPGMCPHFAQDLWPEQGMEDSFQKAILRRYGKYGHENLQLRKGCKSVDEYKVNKEGYNGLNQCFTTAQSKVFQCDKYLKVFYKFLNSNRPKIRHTEKKSFKCKKRVKLFCMLSHKTQHKSIYHREKSYKCKECGKTFNWSSTLTNHRKIYTEEKPYKCEEYNKSPKQLSTLTTHEIIHAGEKLYKCEECGEAFNRSSNLTTHKIIHTGEKPYKCEECGKAFIWSSTLTEHKKIHTRKKPYKCEECGKAFIWSSTLTRHKRMHTGEKPYKCEECGKAFSQSSTLTTHKIIHTGEKRYKCLECGKAFKQLSTLTTHKIIHVGEKLYKCEECGKGFNRSSNLTTHKIIHTGEKPYKCEECGKAFIWSSTLTKHKRIHTREKPYKCEECGKAFIWSSTLTRHKRMHTGEKPYKCEECGKSFSQSSTLTTHKIIHTGEKPYKCEECGKAFNWSSTLTKHKIIHTEEKPYKCEKCGKAFKQSSILTNHKRIHTGEKPYKCEECGKSFNRSSTFTKHKVIHTGVKPYKCEECGKAFFWSSTLTKHKRIHTGEQPYKWEKFGKAFNRSSHLTTDKITHWREILQV
Protein: Mitochondrial import inner membrane translocase subunit Tim10 (Q9Y0V6)
Organism: Caenorhabditis elegans
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (Probable).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit Tim8
- Mitochondrial import inner membrane translocase subunit tim-13
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import inner membrane translocase subunit tim-22
- BHLH domain-containing protein
- Mitochondrial import receptor subunit TOM7 homolog
- Membrane insertase YidC/Oxa/ALB C-terminal domain-containing protein
- Uncharacterized protein F52C9.3
- HoloCentric chromosome binding Protein
Sequence:
MATDAQMAQVAELEVEMMSDMYRRMTNSCQAKCIATAFRESELTKGEAVCLDRCVAKYLDVHEKLGKRLTSMSQGDEAALQKIAQQ
Protein: Auxin response factor 4 (Q9ZTX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus.
Interaction partners:
- Probable transcription factor KAN2
- Protein ASYMMETRIC LEAVES 2
- Auxin-responsive protein IAA9
- Transcription factor AS1
- Transcription repressor KAN1
- Axial regulator YABBY 1
- Probable transcription factor KAN4
- RNA-dependent RNA polymerase 6
- Protein argonaute 7
- Axial regulator YABBY 5
Sequence:
MEFDLNTEIAEVEEEENDDVGVGVGGGTRIDKGRLGISPSSSSSCSSGSSSSSSSTGSASSIYSELWHACAGPLTCLPKKGNVVVYFPQGHLEQDAMVSYSSPLEIPKFDLNPQIVCRVVNVQLLANKDTDEVYTQVTLLPLQEFSMLNGEGKEVKELGGEEERNGSSSVKRTPHMFCKTLTASDTSTHGGFSVPRRAAEDCFAPLDYKQQRPSQELIAKDLHGVEWKFRHIYRGQPRRHLLTTGWSIFVSQKNLVSGDAVLFLRDEGGELRLGIRRAARPRNGLPDSIIEKNSCSNILSLVANAVSTKSMFHVFYSPRATHAEFVIPYEKYITSIRSPVCIGTRFRMRFEMDDSPERRCAGVVTGVCDLDPYRWPNSKWRCLLVRWDESFVSDHQERVSPWEIDPSVSLPHLSIQSSPRPKRPWAGLLDTTPPGNPITKRGGFLDFEESVRPSKVLQGQENIGSASPSQGFDVMNRRILDFAMQSHANPVLVSSRVKDRFGEFVDATGVNPACSGVMDLDRFPRVLQGQEICSLKSFPQFAGFSPAAAPNPFAYQANKSSYYPLALHGIRSTHVPYQNPYNAGNQSSGPPSRAINFGEETRKFDAQNEGGLPNNVTADLPFKIDMMGKQKGSELNMNASSGCKLFGFSLPVETPASKPQSSSKRICTKVHKQGSQVGRAIDLSRLNGYDDLLMELERLFNMEGLLRDPEKGWRILYTDSENDMMVVGDDPWHDFCNVVWKIHLYTKEEVENANDDNKSCLEQAALMMEASKSSSVSQPDSSPTITRV
Protein: Follicular dendritic cell secreted peptide (FDC secreted protein) (FDC-SP) (Q8NFU4)
Organism: Homo sapiens (Human)
Function: Can bind to the surface of B-lymphoma cells, but not T-lymphoma cells, consistent with a function as a secreted mediator acting upon B-cells.
Subcellular location: Secreted.
Interaction partners:
- Odontogenic ameloblast-associated protein
Sequence:
MKKVLLLITAILAVAVGFPVSQDQEREKRSISDSDELASGFFVFPYPYPFRPLPPIPFPRFPWFRRNFPIPIPESAPTTPLPSEK
Protein: Evasin P1090 (A0A090XBH9)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6, CXCL10, CXCL11 and CXCL13.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MEVKIFAFLQIAVLIAFSLHLASAGSKELSGPESSENSIEAAFCDTNCTEGTDGVWSGCSAGCFCVHVGNSTVGRCMTFNGVD
Protein: Dedicator of cytokinesis 6 (K7ESB7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASERRAFAHKINRTVAAEVRKQVSRERSGSPHSSRRCSSSLGVPLTEVVEPLDFEDVLLSRPPDAEPGPLRDLVEFPADDLELLLQPRECRTTEPGIPKDEKLDAQVRAAVEMYIEDWVIVHRRYQYLSAAYSPVTTDTQRERQKGLPRQVFEQDASGDERSGPEDSNDSRRGSGSPEDTPRSSGASSIFDLRNLAADSLLPSLLERAAPEDVDRRNETLRRQHRPPALLTLYPAPDEDEAVERCSRPEPPREHFGQRILVKCLSLKFEIEIEPIFGILALYDVREKKKISENFYFDLNSDSMKGLLRAHGTHPAISTLARSAIFSVTYPSPDIFLVIKLEKVLQQGDISECCEPYMVLKEVDTAKNKEKLEKLRLAAEQFCTRLGRYRMPFAWTAVHLANIVSSAGQLDRDSDSEGERRPAWTDRRRRGPQDRASSGDDACSFSGFRPATLTVTNFFKQEAERLSDEDLFKFLADMRRPSSLLRRLRPVTAQLKIDISPAPENPHFCLSPELLHIKPYPDPRGRPTKEILEFPAREVYAPHTSYRNLLYVYPHSLNFSSRQGSVRNLAVRVQYMTGEDPSQALPVIFGKSSCSEFTREAFTPVVYHNKSPEFYEEFKLHLPACVTENHHLLFTFYHVSCQPRPGTALETPVGFTWIPLLQHGRLRTGPFCLPVSVDQPPPSYSVLTPDVALPGMRWVDGHKGVFSVELTAVSSVHPQDPYLDKFFTLVHVLEEGAFPFRLKDTVLSEGNVEQELRASLAALRLASPEPLVAFSHHVLDKLVRLVIRPPIISGQIVNLGRGAFEAMAHVVSLVHRSLEAAQDARGHCPQLAAYVHYAFRLPGTEPSLPDGAPPVTVQAATLARGSGRPASLYLARSKSISSSNPDLAVAPGSVDDEVSRILASKGIDRSHSWVNSAYAPGGSKAVLRRAPPYCGADPRQLLHEELALQWVVSSSAVREAILQHAWFFFQLMVKSMALHLLLGQRLDTPRKLRFPGRFLDDITALVGSVGLEVITRVHKDVELAEHLNASLAFFLSDLLSLVDRGFVFSLVRAHYKQVATRLQSSPNPAALLTLRMEFTRILCSHEHYVTLNLPCCPLSPPASPSPSVSSTTSQSSTFSSQAPDPKVTSMFELSGPFRQQHFLAGLLLTELALALEPEAEGAFLLHKKAISAVHSLLCGHDTDPRYAEATVKARVAELYLPLLSIARDTLPRLHDFAEGPGQRSRLASMLDSDTEGEGDIAGTINPSVAMAIAGGPLAPGSRASISQGPPTASRAGCALSAESSRTLLACVLWVLKNTEPALLQRWATDLTLPQLGRLLDLLYLCLAAFEYKGKKAFERINSLTFKKSLDMKARLEEAILGTIGARQEMVRRSRERSPFGNPENVRWRKSVTHWKQTSDRVDKTKDEMEHEALVEGNLATEASLVVLDTLEIIVQTVMLSEARESVLGAVLKVVLYSLGSAQSALFLQHGLATQRALVSKFPELLFEEDTELCADLCLRLLRHCGSRISTIRTHASASLYLLMRQNFEIGHNFARVKMQVTMSLSSLVGTTQNFSEEHLRRSLKTILTYAEEDMGLRDSTFAEQVQDLMFNLHMILTDTVKMKEHQEDPEMLIDLMYRIARGYQGSPDLRLTWLQNMAGKHAELGNHAEAAQCMVHAAALVAEYLALLEDHRHLPVGCVSFQNISSNVLEESAISDDILSPDEEGFCSGKHFTELGLVGLLEQAAGYFTMGGLYEAVNEVYKNLIPILEAHRDYKKLAAVHGKLQEAFTKIMHQSSGWERVFGTYFRVGFYGAHFGDLDEQEFVYKEPSITKLAEISHRLEEFYTERFGDDVVEIIKDSNPVDKSKLDSQKAYIQITYVEPYFDTYELKDRVTYFDRNYGLRTFLFCTPFTPDGRAHGELPEQHKRKTLLSTDHAFPYIKTRIRVCHREETVLTPVEVAIEDMQKKTRELAFATEQDPPDAKMLQMVLQGSVGPTVNQGPLEVAQVFLAEIPEDPKLFRHHNKLRLCFKDFCKKCEDALRKNKALIGPDQKEYHRELERNYCRLREALQPLLTQRLPQLMAPTPPGLRNSLNRASFRKADL
Protein: UPF0729 protein C18orf32 (Putative NF-kappa-B-activating protein 200) (Q8TCD1)
Organism: Homo sapiens (Human)
Function: May activate the NF-kappa-B signaling pathway.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:29275994, ECO:0000269|PubMed:35107634}. Lipid droplet {ECO:0000269|PubMed:29275994}.
Interaction partners:
Sequence:
MVCIPCIVIPVLLWIYKKFLEPYIYPLVSPFVSRIWPKKAIQESNDTNKGKVNFKGADMNGLPTKGPTEICDKKKD
Protein: Acetylcholine receptor subunit alpha-like 2 (Nicotinic acetylcholine receptor alpha 2) (P17644)
Organism: Drosophila melanogaster (Fruit fly)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Nicotinic acetylcholine receptor alpha5, isoform I
- Nicotinic acetylcholine receptor alpha6, isoform E
- Nicotinic acetylcholine receptor alpha3, isoform B
- Acetylcholine receptor subunit alpha-like 1
- Nicotinic acetylcholine receptor alpha4, isoform C
- Nicotinic acetylcholine receptor alpha7, isoform E
- RIC3 acetylcholine receptor chaperone, isoform C
Sequence:
MAPGCCTTRPRPIALLAHIWRHCKPLCLLLVLLLLCETVQANPDAKRLYDDLLSNYNRLIRPVSNNTDTVLVKLGLRLSQLIDLNLKDQILTTNVWLEHEWQDHKFKWDPSEYGGVTELYVPSEHIWLPDIVLYNNADGEYVVTTMTKAILHYTGKVVWTPPAIFKSSCEIDVRYFPFDQQTCFMKFGSWTYDGDQIDLKHISQKNDKDNKVEIGIDLREYYPSVEWDILGVPAERHEKYYPCCAEPYPDIFFNITLRRKTLFYTVNLIIPCVGISYLSVLVFYLPADSGEKIALCISILLSQTMFFLLISEIIPSTSLALPLLGKYLLFTMLLVGLSVVITIIILNIHYRKPSTHKMRPWIRSFFIKRLPKLLLMRVPKDLLRDLAANKINYGLKFSKTKFGQALMDEMQMNSGGSSPDSLRRMQGRVGAGGCNGMHVTTATNRFSGLVGALGGGLSTLSGYNGLPSVLSGLDDSLSDVAARKKYPFELEKAIHNVMFIQHHMQRQDEFNAEDQDWGFVAMVMDRLFLWLFMIASLVGTFVILGEAPSLYDDTKAIDVQLSDVAKQIYNLTEKKN
Protein: Protein EAP1 (eIF4E-associated protein 1) (P36041)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Can regulate translation through binding to eIF4E. Competes with eIF4G and p20 for binding to eIF4E in vivo and inhibits cap-dependent translation in vitro. Plays a role in cell growth and is implicated in the TOR signaling cascade. Functions independently of eIF4E to maintain genetic stability and to attenuate GCN4 translation upon TOR inactivation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Protein SCP160
- ATP-dependent RNA helicase DHH1
- Protein SMY2
- SWIRM domain-containing protein YOR338W
- Eukaryotic initiation factor 4F subunit p150
- Cap-associated protein CAF20
- 5'-3' exoribonuclease 1
Sequence:
MELNDPSIISSSQFSGELSDSDTAAATHKSQQAISNLFQKLAKKGREEKPIGSVESSTDSSNISVATSGNNKESNKKKNKKTAMLNFSSLTDPITNYKPMDLQYKTYAYSMNELYHLKPSLASASYEEDPLISELVRSLPKRKFWRLRMGPPDQKHANNHHFNGNNGGGSWKAGYKNGKNDERRMSRTKNMQGGKRRSQQDDEEKKIDQEMLEMDKNLQLGGDVGHSIADFEDWKAKMKELELKKLSKSKGISNSTAIAPRESASHETPTDLRPVIPRGPSSITDFLNLKRQDKKEESSQQTPGIPVGQPSLSKTSIEQVNELETNSDLGKSSSSRFSSFFNKSATSLPSLDNNNQVPSSNVSVVNNDGNSTPHQSGSRLMSFFKESRSSTPNAESQLLSASDKDNGKMQTLPQFQQQPQQMQPMAFTQHPPNNNAFFNGLLNKGKSETSTPPPPPPGLIAHQGPQFPVMGVPPNFPQRMMPPPPGLVQFQKDSKDVNKKEDRQLRQNKNPNGTRNSKGKQEETATPDLPQQQYMPPPPPPGFFPMHPNFPNGPMPPLPQGFPIPPNGMLPVTGQQPQPPYPNMMLQGNFPPNFQQGFGSNSPMPIPSIINANGKNVTNQLPPGLNSKKNIK
Protein: SUMO-specific isopeptidase USPL1 (EC 3.4.22.-) (Ubiquitin-specific peptidase-like protein 1) (Q6DRC5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: SUMO-specific isopeptidase involved in protein desumoylation. Specifically binds SUMO proteins with a higher affinity for sumo2 and sumo3 which it cleaves more efficiently. Also able to process full-length SUMO proteins to their mature forms. Plays a key role in RNA polymerase-II-mediated snRNA transcription in the Cajal bodies (By similarity). Is a component of complexes that can bind to U snRNA genes (By similarity).
Subcellular location: Nucleus, Cajal body {ECO:0000269|PubMed:22878415}.
Interaction partners:
- PPPDE peptidase domain containing 2b.
- Interactor of little elongator complex ELL subunit 2
- Small ubiquitin-related modifier
- Small ubiquitin-related modifier
- SUMO-specific peptidase 5
- palmitoyl-protein hydrolase
- U5 small nuclear ribonucleoprotein 40 kDa protein
Sequence:
MNGEGTGIGAPTPALAGFLGKSKDRNASPGNCPWCLAKGQTNALRFYAVNLKETVLLCTNAVCLYPLVSRSLEEVRASLSKGGCKRSISSLPDISDDSCPPKRPREEKLDVLADVSEPCDAEVNDATLPDDTVKTQTFTDQQSAPAETISLDKTEEQPVSIEDIKEQPISHDATEGQPISIDQTEEQPVSILHTEEQPIVLDLIEVKPMSVDHSEEQPICIDNTKERPVSIVHTEEQSIVLDLFEVKPMSIAHTEEKPTSFDHIEEKPMSIAHTEEKPVSLVHTEDQHLSIDQTEEQPISIDPTEEQQPEELPAVSDEDVDLCERKEDCVSSTQDEMEEEVLESSSELVPVHSELFWKNEENMCWLDAMLVMLVHCRTIRGTPCRGIKLSDKLATVPCNDSVVWKLCWRYDKTCAYLQARKKQSEDKVLRVPAGVLVEAERRLSALRLSVFKLLQPTLKCEIGQQETPVFALPLLLRSDKWAQDIFQHTIRWEFKCTCCDFTVNESVEKTLTTLTCIVKDWHPLKANNRTQCNKCEHKNQRRKMVLEKLSSVFALHFVEGLPRKDLTKYGFTFQGFQYSVSTIIQYNKHLQHFVTWVRQSNGFWLELDDLKHPYSPTHKRLPFPSSEFHILFWETDSFKEEHSEVCLPTAPPEVPNAPDEHPPKLSDSVATDTCVISALTVEDTTASSIADTSIGSTTLLDTFEGLTHKDIVTLTLVNSESPKNEPRPMRPGFVSAPRHCPFEASNLLSGIPKTGSRLSTPPIPQKSSLVHKPEVAAAAVSKTHLQPTSLFQRHPSFQSTPIRPPPPLPPAPKPKPSLQYDKHEDLPVKPADMFGGFKTKKLANSQPKQISLPGGLNPSVKKTAGQEPISTTEALRLKLMKKLKAKKKKLAKLNQLLGNGGESVAKPDSTALSSPYSVTSSTTTYDSFDDQFLADLLSPATTVSNLSPDSTGLLEMLNNGQNGEQQNPAVATLAPEATLTCSSSTISPLDEYMQSGMCHTALENADFNSLDIFF
Protein: Fibronectin-binding protein A (FnbpA) (P14738)
Organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)
Function: Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding site localized within the 17 C-terminal residues of the gamma-chain of human Fg. Both plasma proteins (Fn and Fg) function as a bridge between bacterium and host cell. Promotes attachment to immobilized elastin peptides in a dose-dependent and saturable manner. Promotes attachment to both full-length and segments of immobilized human tropoelastin at multiple sites in a dose and pH-dependent manner. Promotes adherence to and aggregation of activated platelets independently of other S.aureus surface molecules. Is a critical mediator implicated in the induction of experimental endocarditis in rats with catheter-induced aortic vegetations, promoting both colonization and persistence of the bacterium into the host.
Subcellular location: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:11830639}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:11830639, ECO:0000305|PubMed:14769030}. Note=Anchored to the cell wall by sortase A. {ECO:0000305|PubMed:11830639, ECO:0000305|PubMed:14769030}.
Interaction partners:
- Immunoglobulin G-binding protein A
- Clumping factor A
- Extracellular matrix-binding protein ebh
- Serine-aspartate repeat-containing protein C
- Elastin-binding protein EbpS
- Alpha-hemolysin
- Serine-aspartate repeat-containing protein D
- Surface protein G
- Phospholipase C
Sequence:
MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSHVAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFKEVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKYYYDRGYTLTWDNGLVLYSNKANGNEKNGPIIQNNKFEYKEDTIKETLTGQYDKNLVTTVEEEYDSSTLDIDYHTAIDGGGGYVDGYIETIEETDSSAIDIDYHTAVDSEAGHVGGYTESSEESNPIDFEESTHENSKHHADVVEYEEDTNPGGGQVTTESNLVEFDEESTKGIVTGAVSDHTTVEDTKEYTTESNLIELVDELPEEHGQAQGPVEEITKNNHHISHSGLGTENGHGNYDVIEEIEENSHVDIKSELGYEGGQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTTPPIVPPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPAEPGKPVPPAKEEPKKPSKPVEQGKVVTPVIEINEKVKAVAPTKKPQSKKSELPETGGEESTNKGMLFGGLFSILGLALLRRNKKNHKA
Protein: Interferon-induced protein with tetratricopeptide repeats 3 (IFIT-3) (Glucocorticoid-attenuated response gene 49 protein) (GARG-49) (P49) (IRG2) (Q64345)
Organism: Mus musculus (Mouse)
Function: IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS-mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exhibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1B/p27. Normally, CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27 in the nucleus and exports it to the cytoplasm for ubiquitin-dependent degradation. IFIT3 sequesters COPS5 in the cytoplasm, thereby increasing nuclear CDKN1B/p27 protein levels. Up-regulates CDKN1A/p21 by down-regulating MYC, a repressor of CDKN1A/p21. Can negatively regulate the apoptotic effects of IFIT2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O14879}. Mitochondrion {ECO:0000250|UniProtKB:O14879}.
Interaction partners:
- Ubl carboxyl-terminal hydrolase 18
- Antiviral innate immune response effector IFIT1
- Interferon-induced protein with tetratricopeptide repeats 2
- Interferon-induced protein 44
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Signal transducer and activator of transcription 1
- Interferon-induced helicase C domain-containing protein 1
- Ubiquitin-like protein ISG15
- 2'-5'-oligoadenylate synthase-like protein 2
- 2'-5'-oligoadenylate synthase 2
Sequence:
MSEVNRESLEAILPQLKCHFTWNLFREGSMSSHMEDRVCNQVEHLNSEEKATMYDLLAYIKHLDGESKAALECLGQAEDLRKSEHNDQSEIRRLVTWGNYAWIYYHMGRLSEAQAYVDKVRQVCQKFANPYSMECPELECEEGWTRLKCGRNERAKMCFEKALEEKPKDPECSSGMAIAMFRLEEKPEKQFSVDALKQAMELNPQNQYLKVLLALKLLRMGEEAEGERLIKDALGKAPNQTDVLQKAAQFYKKKGNLDRAIELLGKALRSTVNNSPLYSLVMCRYREILEQLQNKGDADSSERRQRMAELRRLTMEFMQKTLQRRRSPLNSYSDLIDFPEVERCYQMVISKESPDVEEEDLYERYCNLQEYHRKSEDLAALECLLQFPRNERSIEKEEVKEQT
Protein: Mitochondrial import inner membrane translocase subunit TIM23 (Q59YG5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU364003}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU364003}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM17
- Mitochondrial import inner membrane translocase subunit TIM44
- Mitochondrial import inner membrane translocase subunit TIM50
- Cytochrome c oxidase subunit 4, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM21
- Mitochondrial import inner membrane translocase subunit TIM16
- Mitochondrial import inner membrane translocase subunit TIM14
- Presequence translocated-associated motor subunit PAM17
- Mitochondrial import inner membrane translocase subunit TIM22
- Heat shock protein SSC1, mitochondrial
Sequence:
MSWIFGKSSTNNDNNTTTTTNDQSSIKQTLGFDPKEVADVNTIISTPGAISASRLHPLAGLDKGIEYLDLEEEQLNTVEGSKGLIPSRSWTDDLCYGTGAVYLLGLGIGGLYGFQQGIKTLPESAPSKVKLNHILNNITKRGPFLGNSAGVLALTYNLIDSTIDGIREKHDDLNSVTAGALAGALFKSSAGLKPMAYSSVMMAGAAGIWCGLKRFLQE
Protein: Calcium-binding and spermatid-specific protein 1 (Q8C633)
Organism: Mus musculus (Mouse)
Function: Calcium-binding protein. Essential for maintaining the structural integrity of the sperm flagella.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q68FX6}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q68FX6}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:19208547, ECO:0000269|PubMed:33440775}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:33440775}. Note=Mostly cytoplasmic, but associated with the mitochondrial inner membrane during the last steps of spermatid differentiation (By similarity). Localizes to the principal piece of the sperm flagellum (PubMed:19208547, PubMed:33440775). {ECO:0000250|UniProtKB:Q68FX6, ECO:0000269|PubMed:19208547, ECO:0000269|PubMed:33440775}.
Interaction partners:
- Testicular spindle-associated protein SHCBP1L
Sequence:
MAEDGSPKIYSRPPRDNSKTPTEADIFFGADNTIPKSETTITSEGDHVTSVNDCTPDGDFSTTVNKLTPTKEKLKLEDDIEGCLKLTTLPEKEITTPTETPNSKPKGSITENFIPVKIGNTSSPVGTVSLIDFSSNTAKEDIFLTTIDTGEKEVVPTTEFSGTLEDSAADVEDASGFPDESTETDVPSSATSDAPDDGAVQVTDSFSPEAGVPPSTEKEVTTIPDITNIAEENVTEIKLIVSEDRPKTVTKLSDSEEEKFITVFELTNSAEKAKDNVEDPLNDEESTDGANDWMEKETASEAESHAVLLTAVESRYDFIVTASETDNVMEESHVNTTDLPENETTESVTNVTEELPSVTSIVDTLKDKEDLSTTNSGLFKLLKEEPDDLMM