wanglab/gogpt-training-data huggingface dataset:
Protein: Preprotein translocase subunit SCY2, chloroplastic (Protein EMBRYO DEFECTIVE 2289) (F4IQV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in protein export. Probably interacts with other proteins to allow the postimport or conservative sorting pathway for inner membrane proteins in plastids. Central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:21051552}; Multi-pass membrane protein {ECO:0000269|PubMed:21051552}. Plastid, amyloplast membrane {ECO:0000269|PubMed:21051552}; Multi-pass membrane protein {ECO:0000269|PubMed:21051552}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:21051552}; Multi-pass membrane protein {ECO:0000269|PubMed:21051552}. Note=Predominantly localized to envelope membranes.
Interaction partners:
- Protein translocase subunit SECA2, chloroplastic
- Preprotein translocase subunit SECE1
- Transmembrane protein
- Protein TIC 40, chloroplastic
- Protein translocase subunit SECA1, chloroplastic
- Inner membrane protein ALBINO3
- ALBINO3-like protein 1, chloroplastic
- Protein TIC110, chloroplastic
- Chloroplast processing peptidase
Sequence:
MNSSQACFFHFSLRPISLSHPSYAFLSKRDPFLCSQPRKCLTTNLNMSRTRQGHSIQMNRRHLLMKERKSFSINYSDKFRDDSMSSEEMHTDALDVEIIPPDSQDIRNSQNSAVSNTLQDDRPKSFRNRFLDFVRISSVLNTAAERFFKSEIRRRLFVTAVLLVLSRVGYFIPLPGFDRRLIPQDYLSFVSGSVEELGEFGAEIKLSLFQLGLSPQIIASIIMQVLCHVLPSLVKLRKEGLDGHEKIKSYIWWLSFFFAIVEALVVAYTSLQYSVFAATAQVKHVMMTSSLLVCGAMTMTWLCDTISESGFGHGSSLIICVGILTGYTETLHKMLNQISGSFSNWLPYLLGLLGIFTVVTMFAVVVTEGCRKIKLQYYGFKLASASREGSPITEVEPYIPFNINPAGMQPVLTTTYLLAFPSILASILGSPFLLNMKEILNPESTVGAPPWVYYSIYAFFVFLFNIFDIANLPKEIADYLNKMGARIPNIKPGKATIEYLTKIQASTRFWGGLLLSFLATASTVLDHYLRSINQGFSIGFTSVLIIVGSIIELRRSYHAYNVMPSLSKALKRYGV
Protein: Poly (ADP-ribose) polymerase family, member 6 (A0A8I6A4Q9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDIKGQFWNDDDSEGDNESEEFLYGVQGSCAADLYRHPQLDADIEAVKEIYSENSVSIREYGTIDDVDIDLHINISFLDEEVSTAWKVLRTEPIVLRLRFSLSQYLDGPEPSIEVFQPSNKEGFGLGLQLKKILYMFTSQQWKHLSNDLLKTQQEKRHSWFKASGSIRKFRAGLSIFSPIPKSPSFPIIQDSMLKGKLGVPELRVGRLMNRSISCTMKNPKVEVFGYPPSPQAGLLCPQHVGLPPPARTSPLVSGHCKNIPTLEYGFLVQIMKYAEQRVPTLNEYCVVCDEQHVFQNGSMLKPAVCTRELCVFSFYTLGVMSGAAEEVATGAEVVDLLVAMCRAALESPRKSIIFEPYPSVVDPTDPKTLAFNPKKKNYERLQKALDSVMSIREMTQGSYLEIKKQMDKLDPLAHPLLQWIISSNRSHIVKLPLSRQLKFMHTSHQFLLLSSPPAKEARFRTAKKLYGSTFAFHGSHIENWHSILRNGLVNASYTKLQEWAKDSTGCLPRTSWSRDTTG
Protein: GPI-anchored hemophore PGA7 (Predicted GPI-anchored protein 7) (Repressed by TUP1 protein 6) (Q59UT5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: GPI-linked hyphal surface heme-binding protein involved in heme-iron utilization. Heme transfer occurs between PGA7, RBT5 and CSA2 supporting a model in which the 3 CFEM proteins cooperate in a heme-acquisition system and form a cross-cell wall heme-transfer cascade. The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:25275454}. Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- ferric-chelate reductase
- Siderophore transporter
- GPI-anchored hemophore RBT5
- Probable circularly permuted 1,3-beta-glucanase PGA52
- Cell wall protein IFF4
- Fth1p
Sequence:
MHFIFYLILLVSAADYGNFGTYPKVPKTASINGFADPIYDLLPDCAKECVKFSTSNTPCPYWDTGCFCVMPQWAGLVGQCVAQKCKGEDVASARFLATSLCSVVGANTWMMPASISSMLSTAAGDAKEVTTIEGKTAKSWVTAPGSAAGSVVSETGSASETGSSESAQSTTTGSSSTGSSSTDSSSSSSSSPSSSANFAVLQTGGIGSVILGFMMYLLV
Protein: Translocating chain-associated membrane protein 2 (Q924Z5)
Organism: Mus musculus (Mouse)
Function: Necessary for collagen type I synthesis. May couple the activity of the ER Ca(2+) pump SERCA2B with the activity of the translocon. This coupling may increase the local Ca(2+) concentration at the site of collagen synthesis, and a high Ca(2+) concentration may be necessary for the function of molecular chaperones involved in collagen folding. Required for proper insertion of the first transmembrane helix N-terminus of TM4SF20 into the ER lumen, may act as a ceramide sensor for regulated alternative translocation (RAT).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAFRRRTKSYPLFSQEFIIHNHADIGFCLVLCVLIGLMFEVTAKTAFLFILPQYNISVPTADSETVHYHYGPKDLVTILFYVVITIIFHAVVQEYILDKISKRLHLSKVKHSKFNESGQLLVFHLSAVAWCFYVIVTEGYLTNPRSLWEDYPHVYLSFQVKFFYLGQLAYWLHSLPELYFQKVRKEEVPRQLQYICLYLLHITGAYLLNLSRLGLILLLLQYSTEALFHMARLFHFADENNERLFNAWAAVFGVTRLFILTLAVLTIGFGLARVENQVFDPEKGNFNTLPCRLGMLLLVCVAQAWLMWRFIHSQLRHWREYWKEQSAKRRVSAVPRPPAKLLKREPGYHENGVVKAENGTSSRTKKLKSP
Protein: Pkp2 protein (Q562C0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
Sequence:
PEGDYPKANGLLDFDIFYNVTGCLRNMSSAGPDGRKVMRRCDGLIDSLVHYVRGTIADYQPDDKATENCVCILHNLSYQLEAELPEKYSQSIYMQNRNIQTNSNKSIGCFGSRSRKVKEQYQDTPMPEERSSPRGIEWLWHSIVIRMYLSLIAKSSRNYTQEASLGALQNLTAGSGPIPTSVARMVVQKENGLQHTRKMLHVGDPSVKKTAVSLLRNLSRNLSLQNEIAKETLPDLVSIIPDTVPSTDLLIETTASACYTLNNLMQNSYQNARDLLNTGGLQKIMTISIGEGYAPNKASKAASVLLYSLWAHTELHNAYKKAQFKKTDFVNSRTAKASHSLKD
Protein: Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) (SAICAR synthetase) (Q9UUB4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Phosphoribosylaminoimidazole carboxylase
- Bifunctional purine biosynthetic protein ADE1
- Adenylosuccinate lyase
- Amidophosphoribosyltransferase
- Phosphoribosylformylglycinamidine synthase
- Phosphoribosylglycinamide formyltransferase
- Tyrosine--tRNA ligase, cytoplasmic
- Uncharacterized protein C8E4.05c
- Argininosuccinate synthase
- Bifunctional purine biosynthesis protein ade10
Sequence:
MALLKTSLDAPFTKIATGKVRDLYECVEFPDDLLFVATDRISAYDFIMENGIPEKGKVLTKISEFWFDVLKPHVQTHLITSRWEELPPVITKHEELKDRSMLVKKYKILPIEAIVRGYITGSAWKEYQKQGTVHGLNVPTGMKEAEAFPEPLFTPSTKAAEGHDENIHPDEVSKIVGPELAKQVAETSVKLYKIARDVALKKGIIIADTKFEFGVDETTNKIVLVDEVLTPDSSRFWLASDYTVGKSPDSFDKQYLRNWLTANNLANKPNVSLPEDVVEATRRKYVEAYEMITGKKWSY
Protein: Meiotically up-regulated gene 118 protein (O94328)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Inner centromere protein pic1
- Chromosomal passenger complex protein bir1
- Aurora kinase
- Anaphase-promoting complex subunit 13
Sequence:
MMNKRKRVEELGETKHRQVRQRILQEHKNDILENLAFELSDKVRRLRSNASLLASTIRMRGEMRIAAIPRAQRNMHLRDLKNHLSCNVSATPWRTKIKEFYNLDELSSQKSARQPTKTVASSSSSSSKSTTVSKSSSKSQV
Protein: SWI/SNF complex subunit SWI3D (AtSWI3D) (Transcription regulatory protein SWI3D) (Q8VY05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of a multiprotein complex equivalent of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
Interaction partners:
- Chromatin structure-remodeling complex protein BSH
- At3g01890
- Actin-related protein 4
- SWI/SNF complex component SNF12 homolog
- Chromatin structure-remodeling complex protein SYD
- Armadillo repeat-containing protein LFR
- Actin-related protein 7
- High mobility group B protein 10
- Probable ATP-dependent DNA helicase CHR23
- Chaperone DnaJ-domain superfamily protein
Sequence:
MEEKRRDSAGTLAFAGSSGDSPASEPMPAPRRRGGGLKRKANALGGSNFFSSAPSKRMLTREKAMLASFSPVHNGPLTRARQAPSIMPSAADGVKSEVLNVAVGADGEKPKEEEERNKAIREWEALEAKIEADFEAIRSRDSNVHVVPNHCGWFSWEKIHPLEERSLPSFFNGKLEGRTSEVYREIRNWIMGKFHSNPNIQIELKDLTELEVGDSEAKQEVMEFLDYWGLINFHPFPPTDTGSTASDHDDLGDKESLLNSLYRFQVDEACPPLVHKPRFTAQATPSGLFPDPMAADELLKQEGPAVEYHCNSCSADCSRKRYHCPKQADFDLCTECFNSGKFSSDMSSSDFILMEPAEAPGVGSGKWTDQETLLLLEALEIFKENWNEIAEHVATKTKAQCMLHFLQMPIEDAFLDQIDYKDPISKDTTDLAVSKDDNSVLKDAPEEAENKKRVDEDETMKEVPEPEDGNEEKVSQESSKPGDASEETNEMEAEQKTPKLETAIEERCKDEADENIALKALTEAFEDVGHSSTPEASFSFADLGNPVMGLAAFLVRLAGSDVATASARASIKSLHSNSGMLLATRHCYILEDPPDNKKDPTKSKSCSADAEGNDDNSHKDDQPEEKSKKAEEVSLNSDDREMPDTDTGKETQDSVSEEKQPGSRTENSTTKLDAVQEKRSSKPVTTDNSEKPVDIICPSQDKCSGKELQEPLKDGNKLSSENKDASQSTVSQSAADASQPEASRDVEMKDTLQSEKDPEDVVKTVGEKVQLAKEEGANDVLSTPDKSVSQQPIGSASAPENGTAGGNPNIEGKKEKDICEGTKDKYNIEKLKRAAISAISAAAVKAKNLAKQEEDQIRQLSGSLIEKQLHKLEAKLSIFNEAESLTMRVREQLERSRQRLYHERAQIIAARLGVPPSMSSKASLPTNRIAANFANVAQRPPMGMAFPRPPMPRPPGFPVPGSFVAATTMTGSSDPSPGSDNVSSV
Protein: Uncharacterized zinc finger protein CG12744 (Q7JUR5)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Thioredoxin-like fold domain-containing protein
Sequence:
METALAEVQLSCLLCEQTFDATEKLDEHLPTHFPQPVSTGQTCDICGRTMRSSLELHQHYKRYHEAHVPNTEGHFQCQLCDKVFLLQDHLKVHVKIEHATDGYQPDEKSLDWQHYSPRSLDTTNDYKLDPILCPPPKRKYPPRSPFFNPNLWLGADNCFM
Protein: Vesicle-associated membrane protein 7 (VAMP-7) (Synaptobrevin-like protein 1) (Tetanus-insensitive VAMP) (Ti-VAMP) (P51809)
Organism: Homo sapiens (Human)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation.
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Late endosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000269|PubMed:17897319}; Single-pass type IV membrane protein {ECO:0000269|PubMed:17897319}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Note=In immature neurons expression is localized in vesicular structures in axons and dendrites while in mature neurons it is localized to the somatodendritic region. Colocalizes with LAMP1 in kidney cells. Localization to the endoplasmic reticulum membrane was observed in the intestine but not in liver or kidney (By similarity). {ECO:0000250}.
Interaction partners:
- Synaptosomal-associated protein 29
- Vesicle-associated membrane protein 8
- Syntaxin-4
- Synaptosomal-associated protein 23
- Syntaxin-7
- Syntaxin-17
- Vesicle-associated membrane protein 3
- Synaptosomal-associated protein 25
- Syntaxin-6
- Syntaxin-12
Sequence:
MAILFAVVARGTTILAKHAWCGGNFLEVTEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKHHSENKGLDKVMETQAQVDELKGIMVRNIDLVAQRGERLELLIDKTENLVDSSVTFKTTSRNLARAMCMKNLKLTIIIIIVSIVFIYIIVSPLCGGFTWPSCVKK
Protein: Cirrhosis, autosomal recessive 1A (Cirhin) (U3 small nucleolar RNA-associated protein 4 homolog) (UTP4 small subunit processome component) (Q6P125)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- UTP18 small subunit processome component.
- BMS1 ribosome biogenesis factor
- Programmed cell death 11.
- U3 small nucleolar RNA-interacting protein 2
- WD repeat domain 36
- Transducin beta-like 3.
- Nucleolar complex protein 4 homolog
- Small subunit processome component 20 homolog
- WD repeat domain 46.
- U3 small nucleolar RNA-associated protein 15 homolog
Sequence:
MGEFKVHRVRFFEYVPSGIRALAFNQHNERMAAAKMNGSVEIFHCSDRFFQEKIIPGREQAGIEGLTWVGERLFSAGLNGVITEYDLTNQRVKYTIDAYGGPIWAITGNQQGTHLAVGCEDGTVKLFEVTEDKIQFERNLDRQKGRIISLSWHPSGSKIAAGMMDMIQVFNVETGHSKHRILVDRGYGTSRGKECVVWSVVYLSDGTIISGDSVGMVKMWRDDTGTLIKSHNITKSDVLSLSVSQNEDSIVAGTSEGFVVQFQFLSMVLENNEKDWVRTRTFRNHTHDVRAVAEITTAVVSGGMDTQLVVRPLLDKHEVKSSASKLRKIQFPHRSLVSCARKAGTLLFQYPGHLELWRLGESEGEGIPGSSLLLKRKPEKLLHLKVKGEDHIRCSAVSPCGEWIAYSTTSSLRLYKLHCDSNNVSITKISKLPKVLGSASQLCFSSDSTHLFSASTQSSVHMVSLSQPECKFVATFKTKSGSHQAIHLLAASEDGKWLASANIDNEVHIYNLQTRKAHCTVPIYSSAVSAMAIHPTTNCLFMVHADQQIFEFSIEQKEYTDWSRLVQRQGLHRIWLERDTPCLNVTFNQKNPSHVILHDMYMFCIIDQSQPLPDSKSQFLNQLTLRSLPEEQRKSYSHAFKVCKTFKELLCVDVMGDQSLVVVERPLEDITAQLPAPIKQKKFAT
Protein: Secernin-1 (p50) (P83939)
Organism: Bos taurus (Bovine)
Function: Regulates exocytosis in mast cells. Increases both the extent of secretion and the sensitivity of mast cells to stimulation with calcium.
Subcellular location: Cytoplasm.
Interaction partners:
- Synaptotagmin-1
- Cytochrome P450 2A
- Transcription factor RelB
- Actin-related protein 2/3 complex subunit 3
- Uncharacterized protein
- Actin-related protein 2/3 complex subunit 4
Sequence:
MAVAPPSYCFVAFPPRAKDGLVVFGKNSARPRDEVQEVVYFSAADHEPESKVECTYISINQVPRTHAIVISRPAWLWGAEMGANEHGVCIANEAINAREPAAETEALLGMDLVRLGLERGATAKEALDVIVALLEEHGQGGNYYEDANSCHSFQSAFLIVDREEAWVLETVGKYWAAEKITEGVKCICNQLSLTTKIDAEHPELRSYAQSQGWWMGEDEFNFSEVFSPADDHLTCCSGRDTLEKQEESITVQTMIDVLRDKASGVCVDSESFLTTASVVSVLPQNGSSPCIHYFTGTPDPSRSIFKPFIFVDDVKLVPKAQSPCFGDDDPAKKEPRFQEKPDRRHELYKAHEWARAVLESDEEQGQKLRKTMLELEKQGLEAMEEILTSSDPLDPTEVGDLFYDCVDTEIKFFK
Protein: SNF1-like protein kinase ssp2 (EC 2.7.11.1) (O74536)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Serine/threonine protein kinase essential for release from glucose repression via the phosphorylation of scr1 upon glucose deprivation. Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes. The complex phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, leading to transcriptional activation through TBP recruitment to the promoters (By similarity). Regulates proper cell cycle exit and sexual differentiation. Regulates also ste11 levels under nitrogen deprivation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22375066}. Nucleus {ECO:0000269|PubMed:22140232, ECO:0000269|PubMed:22375066}. Note=Nuclear translocation occurs under nitrogen and glucose starvation conditions and depends on Thr-189 phosphorylation by ssp1 (PubMed:22375066). {ECO:0000269|PubMed:22375066}.
Interaction partners:
- 5'-AMP-activated protein kinase subunit gamma
- 5'-AMP-activated protein kinase subunit beta
- Serine/threonine-protein kinase ssp1
- High-affinity glucose transporter ght5
- Serine/threonine-protein kinase atg1
- High-affinity glucose transporter ght2
- Probable high-affinity hexose transporter ght7
- High-affinity glucose transporter ght1
- High-affinity hexose transporter ght4
- High-affinity gluconate transporter ght3
Sequence:
MQPQEVDLMENSTMRNGARVLPPEAISKRHIGPYIIRETLGEGSFGKVKLATHYKTQQKVALKFISRQLLKKSDMHMRVEREISYLKLLRHPHIIKLYDVITTPTDIVMVIEYAGGELFDYIVEKKRMTEDEGRRFFQQIICAIEYCHRHKIVHRDLKPENLLLDDNLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVINGKLYAGPEVDVWSCGIVLYVMLVGRLPFDDEFIPNLFKKVNSCVYVMPDFLSPGAQSLIRRMIVADPMQRITIQEIRRDPWFNVNLPDYLRPMEEVQGSYADSRIVSKLGEAMGFSEDYIVEALRSDENNEVKEAYNLLHENQVIQEKSHLSKSKRVDSFLSVSPPAFSEYTSELQKKSKQELIDPTLEGPRWTVSDPPTYAKQTIDSNICVLVPTAEKNKLEMRTLADAASAVDTSQSTRKKSRRNKWHFGVRCRGDAPEILLAVYRALQRAGAQFTVPKPVNGKYRSDMYTIKSRWEIPHCKREGKNTYAYIELQLYEVMPGCFMLDVKSNGYKDIYSHPERTADHGMDDLKSSFPFLDLCAMLVCKLFSA
Protein: Serpin family F member 2 (F7FHF3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Plasminogen
- Vitamin K-dependent protein C
- Fibrinogen alpha chain
- Fibrinogen gamma chain
- Fibrinogen beta chain
- Prothrombin
- Tissue-type plasminogen activator
- Aa1018
- Alpha-1-macroglobulin
- Thrombospondin-1
Sequence:
MFNRMRRSIFTSTGHELDGGWLRAKVLWEERARPCWLHWVEERGEQVGSGRTSCAALRSLKRNMALLRGLLVLSLSCLQGPSSMFSPVSAMDLPGQQPVSEQAQQKLPPLALLKLGNQDLGDHATLKRSPGDCKSAPTTEETRRLSQAMMAFTTDLFSLVAQTSTSSNLVLSPLSVALALSHLALGARNQTLENLQRVLHMNMGSCIPHLLSHFCQNLNPGTIRLAARIYLQKGFPIKDDFLEQSEKLFGAKPVKLTGRQEEDLMNINKWVKEATEGKIEDFLSELPDNTVLLLLNAIHFHGFWRTKFDPSLTQKDSFHLDEQFTVPVAMMHAQSYPLRWFLLEQPEIQVAHFPFQNNMSFVVIMPTYFGWNVSEVLANLTWDTLYQPSMREKPTKVRLPKLHLEQHLDLVATLSKLGLQDLFQSPDLRGISDQSLVVSSVQHQSTMELSEAGVEAAAATSTAMTRMSLSSFFLNRPFIFFIMEETIGIPLFVGSVRNPDPSAQPQPQEQQDSPDNRRLDQNDKADIPGGKTFAPDLKLVPRLEEDYPQFSSPK
Protein: WD repeat domain 27 (A0A3B3ITF5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MENPQDIFSSNGGCLSDIVIEKYLVESKESVSHVQLACSMQDCAFPLDGTELCIWNTKDPSHQLLILRGHHQPITAMAFGNKVNPLLICSASLDYVIMWNLDECREKVLQGLVPRGTVMGSLLGKVLCLQLSLDDHVVAVCAGNKIFMLDIEVWDHCTGSLIYSSSVLSAYPLLSLFIDAESRQLVTGCADGQLWIFSLMDGHHYRRVARVDLRKKTETFSTRRVKSGLCSQPEESQLPSTSALGKGEQVEVTFPVLRLAPCDLSLIPNSACGCLSSENTRCVWIGSSVGLFVFNLANLEVEAALYYKDFQSLSILLAGSCALRNRTADQKVLCLLASLFGGKIAVLEINPAALVRAQQCPSMGQSLSVPASSCVLPTSPLYLGIAKEKSTKAASEQRRATCPRLTAVPLVPVAVGVQSGPSAITDCENIFFPFFLC
Protein: GH26440p (RNA-binding protein) (RNA-binding protein 9, isoform F) (RNA-binding protein 9, isoform G) (RNA-binding protein 9, isoform H) (Q24474)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVEGQTAVQQQQQQPSGAGGASGVGSTTGSAGGPATANNVTNSQAQTNGGTTATTTAAAGAGSTTNAAVGQATANNAASNNNNNNNNTNNNNNNNATANNNNNNEPDPKTNLIVNYLPQTMSQDEIRSLFVSFGEVESCKLIRDKVTGQSLGYGFVNYVKQEDAEKAINALNGLRLQNKTIKVSIARPSSESIKGANLYVSGLPKNMTQSDLESLFSPYGKIITSRILCDNITGLSKGVGFIRFDQRFEADRAIKELNGTTPKNSTEPITVKFANNPSSNKNSMQPLAAYIAPQNTRGGRAFPANAAAGAAAAAAAAAIHPNAGRYSSVISRYSPLTSDLITNGMIQGNTIASSGWCIFVYNLAPDTEENVLWQLFGPFGAVQSVKVIRDLQSNKCKGFGFVTMTNYEEAVLAIQSLNGYTLGNRVLQVSFKTNKNKQT
Protein: Anterior gradient protein 2 homolog (AG-2) (mAG-2) (Protein Gob-4) (Secreted cement gland protein XAG-2 homolog) (O88312)
Organism: Mus musculus (Mouse)
Function: Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells. Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth (By similarity). Promotes cell adhesion (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:O95994}. Endoplasmic reticulum {ECO:0000269|PubMed:19359471}.
Interaction partners:
- Ly6/PLAUR domain-containing protein 3
- Mucin-2
- Calcium-activated chloride channel regulator 1
- SAM pointed domain-containing Ets transcription factor
- Zymogen granule membrane protein 16
Sequence:
MEKFSVSAILLLVAISGTLAKDTTVKSGAKKDPKDSRPKLPQTLSRGWGDQLIWTQTYEEALYRSKTSNRPLMVIHHLDECPHSQALKKVFAEHKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIVFVDPSLTVRADITGRYSNRLYAYEPSDTALLYDNMKKALKLLKTEL
Protein: Paraplegin, isoform A (Paraplegin, isoform C (EC 3.4.24.-)) (Q9W4W8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Prohibitin 1
- AFG3 like matrix AAA peptidase subunit 2, isoform A
- Prohibitin
- Caseinolytic protease chaperone subunit, isoform C
- Mitochondrial ribosomal protein L2
- ATP-dependent Clp protease proteolytic subunit
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein bL19m
- ATP-dependent zinc metalloprotease YME1L
Sequence:
MLKGLRHVRNALQRGGSQLIQLRSATGQPPRIGRELSLLQLSRRQVMQLQAEYKAIVGLIARSLQLTPKEVRLMHLRSLSSTAKPPTASDGKTEKHEQPEKGSAKAKDDSSKEKKSAVAAEDGDKSSRAAGEEAASTPTSSSTIGEPGEDPNKNSNENDEKMRSVLTKAVLWLFTIYMFVAFFSLLITPRSERPEGSTRYVSWNEFVHHMLAVGEVKELIIRPDMEMVTIILHEGAVIKGRKVSSTIFHMAVADANKFEEKLRDVEKRLGIKDGVPVTYDRQTDTTGRILMLLLVCALLMSIATRMKSIKSPLSMDSFNQMGRAKFTLVDPFDGGRGVLFRDVAGLSEAKQEVKEFVDYLKSPEKYQRLGAKVPRGALLLGPPGCGKTLLAKAVATEAQVPFLSMNGSEFIEMIGGLGAARVRDLFKEGKKRAPCIIYIDEIDAIGRQRSGTESMGQGSSGESEQTLNQLLVEMDGMATKEGVLMLASTNRADILDKALLRPGRFDRHILIDLPTLAERKEIFEKHLSSVKLESPPTTFSQRLARLTPGFSGADIANVCNEAALHAARNTQMEVSSKNLEYAVERLVGGTEKRSHALSLAERKVIAYHESGHALVGWMLPNSDILLKVTIVPRTSLALGFAQYTPSEQHLYSKEELFDKMCMALGGRAAENLVFNRITTGAQNDLEKVTKIAYSQIKKFGMNDTLGPIYVRDADETEGGGAMGSGGKKPFSRAMESMIDNEARHVVASAYQTTEGILTTHRDKLEKLAEALLEKETLDYDQVVQLIGPPPYDLGKRQVESVEFEQSLKNLSTDTDATKA
Protein: Fgr44p (Q5AND6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MPNNVSTVPAQGMNKNHTAIPSSLLTALSKQQDKLYILHLEKDLIKFIKNSVLGNIKQPEYIIQAQYLKNSYYRLLSHQLCQYYNLQHWNNTFNEIIVTPIPNFDYQQFIKAIESSDNNEGGEFVKIVSVAHKYKSENTATTTNNNTNTDAPEQPNKPAPIKKLMVRKIINKPVSDPTPGQAPGTPESEVSDLTKELDESKLISEDTGSSTPISESSENTTNNIESQRASKEALYMKLREEIFENNNEEEEEEEEEEEDGDYGTTDSQESNNRSYKTHNNFIKGRNHGNYSGYKTTPYQQQQLQHQPPMYNTIPMPVPYQFSPNSQGPPIPGMIYSPYYQPMMYGYAPNYPGAPTNNNNVVPAPKYDKETERRILNNPYIILPNDTKNGKNNNYSNKHTKHKKQFTNSNI
Protein: Heat shock factor protein 3 (HSF 3) (Heat shock transcription factor 3) (HSTF 3) (mHSF3) (D0VYS2)
Organism: Mus musculus (Mouse)
Function: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription of non-classical heat-shock genes such as PDZD2 and PROM2. Protects cells against heat shock and proteotoxic stress.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:19864465}. Nucleus {ECO:0000269|PubMed:19864465}. Note=Cytoplasmic under normal conditions. Translocates to the nucleus in response to heat shock. {ECO:0000269|PubMed:19864465}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19864465}. Note=Does not translocate to the nucleus in response to heat shock. {ECO:0000269|PubMed:19864465}.
Interaction partners:
- Heat shock factor protein 5
Sequence:
MEQFRKTMVPHFLTKLWILVDDAVLDHVIRWGKDGHSFQIVNEETFAREVLPKYFKHNKITSFIRQLNMYGSRKVFALQTEKTSQENKISIEFQHPLFKRGEACLLANIKRKVPTIKIEGASLYSDEFQKIVTEMQEFKDMQRKMDAKYTQMKQDYSNLYHEVTNLRKKYCAQQQLLTRVLHFILDLMSENHTVLKKRKRSLSFISEDSDSEWDHQYFRIPEDKKEAMEILKDGYELVEDKYKSLLDRVMPILKESKKLISSGDQPSGDDGEHPKVPVQDKPMNEESLTIQLDLTIPVLPEQITEESVEQEPKDISLELDLSSQDSILMKDKSDNLYNNIINRDKKDMHHTEGNLLELNSLLSRKALNYDSDHFSESLSLMKNEEEKSQLDLSGGKDNHMIQCMETPELFLLDEIPMCDFGENLQDYDRLLEDLKNPPNVISALCDHDYVTSNISTLQEDTIENSIPQLCMEANGESSVFPFLILNPVTNIF