wanglab/gogpt-training-data huggingface dataset:
Protein: 30 kDa adipocyte complement-related protein (Adiponectin d) (Adiponectin, C1Q and collagen domain containing) (Q8K3R4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Adiponectin receptor 1
- Adiponectin receptor 2
- Cadherin-13
- Complement factor D
- Resistin
- Leptin
- Resistin-like gamma
- Insulin-1
- Insulin-2
- Peroxisome proliferator-activated receptor gamma
Sequence:
MLLLQALLFLLILPSHEGITATEGPGALVPPPKETCAGWMAGIPGYPGHNGIPGRDGRDGTPGEKGEKGDAGVLGPKGDPGDAGMTGAEGPRGFPGTPGRKGEPGEAAYMYHSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSMLLHLEVGDQVWLQVYGEGDNNGLYADNVNDSTFTGFLLYHDTN
Protein: Uncharacterized protein, isoform A (Q8IPX4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
- Accessory gland-specific peptide 26Ab
- Aquarius
- Uncharacterized protein
Sequence:
MIKWKIFVPAILYLQSSMAMRAFHGACPSNMTAVGDLDMDRFKGKWYTHSIYPHLSLRVEKCQSTDFIEKEENKFSVVARELNTQTGTVKMRKADILNVEPEFGRYVLGTTSTAFPEGVLMYVLDTDYVNFAIRFMCFDASKIFSFHWAVIQTRKRLPSTQVIHMAQYFGKSAGLVIGDMSKVPQESCPYDT
Protein: Malate dehydrogenase, chloroplastic (EC 1.1.1.37) (Chloroplastic malate dehydrogenase) (Chloroplastic MDH) (cpNAD-MDH) (Plastidic NAD-dependent malate dehydrogenase) (pNAD-MDH) (Q9SN86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments (Probable). Plays a key role in the metabolism of dark chloroplasts and non-green plastids. Essential for embryo viability. Plays an essential role in heterotrophic metabolism in embryos, and autotrophic metabolism in photosynthetic tissues as well.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:12766230, ECO:0000269|PubMed:24198233, ECO:0000269|PubMed:24453164, ECO:0000269|PubMed:9774405}.
Interaction partners:
- Malate synthase
- Citrate synthase 4, mitochondrial
- Malate dehydrogenase, chloroplastic
- Citrate synthase 2, peroxisomal
- Citrate synthase 3, peroxisomal
- Citrate synthase 5, mitochondrial
- Citrate synthase 1, peroxisomal
- Fumarate hydratase 2
- NAD-dependent malic enzyme 2, mitochondrial
- Fumarate hydratase 1, mitochondrial
Sequence:
MATATSASLFSTVSSSYSKASSIPHSRLQSVKFNSVPSFTGLKSTSLISGSDSSSLAKTLRGSVTKAQTSDKKPYGFKINASYKVAVLGAAGGIGQPLSLLIKMSPLVSTLHLYDIANVKGVAADLSHCNTPSQVRDFTGPSELADCLKDVNVVVIPAGVPRKPGMTRDDLFNINANIVKTLVEAVAENCPNAFIHIISNPVNSTVPIAAEVLKKKGVYDPKKLFGVTTLDVVRANTFVSQKKNLKLIDVDVPVIGGHAGITILPLLSKTKPSVNFTDEEIQELTVRIQNAGTEVVDAKAGAGSATLSMAYAAARFVESSLRALDGDGDVYECSFVESTLTDLPFFASRVKIGKNGLEAVIESDLQGLTEYEQKALEALKVELKASIDKGVAFANKPAAAAAN
Protein: LexA repressor (EC 3.4.21.88) (Q9L4P1)
Organism: Staphylococcus aureus (strain COL)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
Sequence:
MRELTKRQSEIYNYIKQVVQTKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM
Protein: Vacuolar protein sorting-associated protein 18 homolog (P59015)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport pathways. Believed to act as a core component of the putative HOPS endosomal tethering complex which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion (By similarity). May be involved in vesicle trafficking to the hepatocyte apical membrane and play a role in development of the intra-hepatic biliary tree. May target endosomes to the pigment granule in melanocytes. Essential for early embryonic development.
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q9P253}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9P253}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9P253}. Lysosome membrane {ECO:0000250|UniProtKB:Q9P253}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9P253}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9P253}. Note=Cytoplasmic, peripheral membrane protein associated with early endosomes and late endosomes/lysosomes.
Interaction partners:
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 33A
- Vacuolar protein sorting-associated protein 41 homolog
- VPS39 subunit of HOPS complex.
- Vacuolar protein sorting-associated protein 8 homolog
- Vacuolar fusion protein CCZ1 homolog
- Vacuolar protein sorting-associated protein 33B
- Vesicle transport through interaction with t-SNAREs 1A
- Vesicle transport through interaction with t-SNAREs 1B
Sequence:
MASILDQYEDSQNIRQHSRMSTANIGITHSGFVNVRLEEEKPIFTKQRIDFSPPEKINQFSVCNNQLCMSLGKDTLLRIDLGKPDQPNQIELGRKDDSKVHRLFLDPTGSHLVICLTTNECVYLNRNTQKVRGLSRWRGHLIESIGWNKLIGSETNTGPILVGTSQGIIFEAEISASEGSLFNTNPDQYFRQVHYLEEDGKPAPVCCLEVERGLETKYFIIATTRKRLFQFVGKLAEGSEQQGFSSIFAQNQDLLPSFQEFPVNMGYSEITFYTSKLRSRPKTFAWMMGNGVLYGQLDYVRPDSLLSDVQVWEYTQDIDLNFVKPISIVLTQFHFLLLLPDRVRGICTLNGQVVHEDVFPEKFGTLQKMIKDPITGLVWIYTEKAVFRYHIQKEARDVWQMYMNMNKFDLAKEYCKDRPECLDMVLAKEAEHCFQNKRYLESAKCYALTQNYFEEIALKFIEAKQEEALKEFLIKKLVNLKPSEKTQITLLVTWLTELYLNRLGQLEADEGKQHLFLETREEFRTFLKSPKHKDCFYNNRSTIYDLLASHGDVDNMVYFSVIMQDYERVISHYCQHDDYSAALDVLSKHCDDKLFYKFSPVLMQHIPKKVVDAWIQMGNRLDPKNLIPALVNYSQMGSMQQINETIRYMEFCVYELDVKEEAIHNYLLSLYAKHKPDALLWYLEQAGTHVSDIHYDLKYALRLCSEHGYLQACVLVYKIMELYEEAVDLALKVDVDLAKSCADLPEDDEELRKKLWLKIARHVVQEEKDVKKAMNCLSSCNLLKIEDILPFFPDFVTIDHFKEAICSSLEEYNKHIEELKQEMEEATESAKRIREDIQEMRNKYGVVESQEKCATCDFPLLNRPFYLFLCGHMFHYDCLLQEVIPHLSVYKQNKLDELQKKLAATTQTTKARHKPREEDTVSLGKGQGSREQIKSDIDDIIACECVYCGELMIKSIDKPFIDPQKFDQEMSSWL
Protein: COBRA-like protein 7 (Q8GZ17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Protein trichome birefringence-like 13
- Transmembrane 9 superfamily member 9
- Vacuolar protein sorting-associated protein 60.1
- Transmembrane 9 superfamily member 8
- Carbohydrate-binding X8 domain-containing protein
- NADH-Ubiquinone/plastoquinone
- Cellulose synthase-like protein B4
- F-box protein PP2-B13
- L-type lectin-domain containing receptor kinase IV.2
- F-box protein PP2-B10
Sequence:
MDSAPNFIPRLLLLSLLIVSIPLTSSQSDANTTNPSPSPPSDSDLCNGVFVSYTHTKGSKIPPNDTANQPYRFESVITVLNHGRDELKSWRVFVKFAHREILVSASNAVLSDGSSLPVSVENGTVFAGYPSSDLKSAIQTAGDVTQMQARVELVGTQFGVAPPNVPLPKNITLATDGWKCPKATQKGTNVLQVCCIPDPDYDNREIIDNEFLPRKDGDLTIMYDVVRSYSSNYMAQVTMENHNPLGRLDNWKLSFDWMRDEFIYTMKGAYPSIVDSSDCVDGPQAKHYQDLDFSNVLSCARRPTVIDLPPTKYNDSTFGLIPFCCRNGTILPRSMDPSKSSSVFQMQVYKMPPDLNISALSPPQNWRINGTLNPDYKCGPPVRVSPSQFVDPSGLPSNRTAFASWQVVCNITQPKDASPRCCVSFSAYFNDSIVPCKTCACGCSSNKAARACSATAPSLLLPQQALLVPFENRTELTVAWAYLKQRPVPNPMPCGDNCGVSINWHLATDYRGGWTARVTVFNWGETDFVDWFTAVQMKNAAPGFEKAYSFNASTIGINGKNNTIFMEGLPGLNYLVAERDGENPLKNPRIPGKQQSVMSFTKKLTPGINVPGGDGFPSKVFFNGEECSLPTILPMRSSQHRKHISVFLLALPVLALLILRA
Protein: Ferredoxin--NADP reductase, root isozyme 1, chloroplastic (EC 1.18.1.2) (Root FNR 1) (AtRFNR1) (Q9M0V6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Maintains the supply of reduced ferredoxin under non-photosynthetic conditions.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Ferredoxin--nitrite reductase, chloroplastic
- Assimilatory sulfite reductase
- Ferredoxin-3, chloroplastic
- Ferredoxin-2, chloroplastic
- Probable ferredoxin-4, chloroplastic
- Cytochrome b6-f complex iron-sulfur subunit, chloroplastic
- Anamorsin homolog
- Ferredoxin-1, chloroplastic
- Pentatricopeptide repeat-containing protein DOT4, chloroplastic
- Photosystem I reaction center subunit IV A, chloroplastic
Sequence:
MALSTTPSQMSVALPTRIDGSSRSMIKVQSISFTDKSWGPPLLRLDSKSRSLGVKKRSTICMSLQQSSKSKVLVTPLELEDPKETPLNLFRPKEPYTATIVSVERIVGPQAPGETCHIVIDHDGNVPYWEGQSYGVIPPGENPKKPGAPHNVRLYSIASTRYGDSFDGKTASLCVRRAIYYDPETGKEDPSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDDPKATHIMIATGTGVAPYRGYLRRMFMENVPNFKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMYVQDKIEEYSDEIFKLLDNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWEQKLTQLRKNKQWHVEVY
Protein: Protein EARLY STARVATION 1, chloroplastic (AtESV1) (Protein REDUCED GRAVITROPIC 1) (F4I9G2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds preferentially to highly ordered alpha-glucans, such as starch and crystalline maltodextrins. Involved in the organization of the starch granule matrix, thus influencing starch turnover by modulating the accessibility of starch polymers to modifying and degrading enzymes involved in phosphorylation, hydrolyzes and synthesis, including starch synthases (SSI and SSIII), starch phosphorylases (PHS1), isoamylase, beta-amylase, glucan water dikinase (GWD) and phosphoglucan water dikinase (PWD). Prevents GWD- and PWD-mediated starch phosphorylation, and subsequent degradation. Required for the control of starch degradation in leaves and starch distribution in nonphotosynthetic parts (e.g. cells immediately adjacent to veins, columella cells of root caps, stems, flowers and siliques) by limiting the hasty depletion of starch reserves during the night. Promotes gravitropic responses, negative in shoots but positive in roots, by maintaining starch granules (statoliths) accumulation in hypocotyls and roots columella, especially in dark conditions and in the endodermis, where starch is formed from transported glucose-6-phosphates.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:27207856, ECO:0000269|PubMed:29681129, ECO:0000269|PubMed:34367195}. Plastid stroma {ECO:0000269|PubMed:34367195}. Note=Binds to starch granules in chloroplasts and plastids. {ECO:0000269|PubMed:27207856, ECO:0000269|PubMed:29681129, ECO:0000269|PubMed:34367195}.
Interaction partners:
- Copper-binding family protein
- At5g07400
- AT1G56000 protein
- Spectrin beta chain, brain
- Zinc finger, C3HC4 type
- Protein cereblon
- AP-1 complex subunit gamma-2
- Pirin-like protein 2
- Formin-like protein 20
- Ankyrin repeat-containing protein ITN1
Sequence:
MSEMAASSAISLLDIKLRRFGVGASNHELRLTKWFKGDQAGAPTRRFTCFADMLAPIRRSEKSEERRFDQKMSAHGAGIKTSSSAVPFASPKSRFLSKQEKFYPRCTPRLTGPQSRDTPPKRDTGIANEKDWGIDLLNENVNEAGTNEDGSSWFRESGHDLGDNGYRCRWSRMGGRSHDGSSEWTETWWEKSDWTGYKELGVEKSGKNSEGDSWWETWQEVLHQDEWSNLARIERSAQKQAKSGTENAGWYEKWWEKYDAKGWTEKGAHKYGRLNEQSWWEKWGEHYDGRGSVLKWTDKWAETELGTKWGDKWEEKFFSGIGSRQGETWHVSPNSDRWSRTWGEEHFGNGKVHKYGKSTTGESWDIVVDEETYYEAEPHYGWADVVGDSTQLLSIQPRERPPGVYPNLEFGPSPPPEPDLPPDQPQ
Protein: Translation initiation factor (F4JW44)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MPKRKAKECVKLTEEDRNDEKRIRIEEKKEDFVDEEVERQIAAIRAIRDVEIEQMLTALRLLRSYFTEEQLHTPVLDFFKENLPDLSISRNEETGEIELKWRDENGDSFAGNENGVDMNYSILKRLSMRFTDLYSRSSLGGYDLPDNVKANLLGTDNPQLDNLVFQGTSENQMLPGHDAFQTPGVNGQRLSFGMTPKTLRLPKAGEMMLSVHGSPLGVYKEDHNMGAINEENS
Protein: Serine protease K12H4.7 (Q9VS02)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD06929p
- GEO09379p1
Sequence:
MLFIGGVLRPLGVGLLLLGLLAPISGMGFRRGRLTKGFLGEPSKIPTLQRSLHSEDLWFEQRLDHFKSSDKRTWQQRYFVNADFYRNDSSAPVFLMIGGEGEASAKWMREGAWVHYAEHFGALCLQLEHRFYGKSHPTADLSTENLHYLSSEQALEDLASFVTAMKVKFNLGDGQKWIAFGGSYPGSLAAWAREKYPELIYGSISSSGPLLAEVDFKEYFEVVKASLAAYKPECVDAVTRSFAQVEILLKHMIGQRSLDEKFKTCTPIKDSIENDLDMANFFENLAGNFAGVVQYNKDNSPHATITIDDICDVMLNTTAGPPVTRLGLVNDMLLKESNTTCLDYKYDKMVADMKNVSWDSETAKGMRQWTYQTCHEFGFYQTSDNPADTFGDRFGVDFFIRQCMDVFSKNMNAKFLKLVVSATNDNYGALKPKTTNVLYVHGSIDPWHALGLVKSTNAALPTIYIEGTAHCANMYEPVKTDPPQLVAARNKILKFLAKLLDGYTSALI
Protein: Glycogen synthase kinase 3 (EC 2.7.11.26) (O77344)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Protein phosphatase PPM5, putative
- Uncharacterized protein
- Gametocyte-specific protein
Sequence:
MKNWPIDEDINIYEEKNHTNNKNYVNNFEMSDQKDEEEYSHSSNRSEDEDEERTIDNEINRSPNKSYKLGNIIGNGSFGVVYEAICIDTSEQVAIKKVLQDPQYKNRELMIMKNLNHINIIYLKDYYYTESFKKNEKNIFLNVVMEYIPQTVHKYMKYYSRNNQALPMFLVKLYSYQLCRALSYIHSKFICHRDLKPQNLLIDPRTHTLKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGSTNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGTPTEDQLKEMNPNYADIKFPDVKSKDLRKVFPKGTPDEAINLITQFLKYEPLKRLNPIEALADPFFDELRDPCIKLPKYIDKLPELFNFCKEEIQEMSMECRRKIIPKNVYEEFLMVDENDNNIINDTISNDFNESNLDTNNSNNKTHVIIES
Protein: Beta-adrenergic receptor kinase 1 (Beta-ARK-1) (EC 2.7.11.15) (G-protein-coupled receptor kinase 2) (Q99MK8)
Organism: Mus musculus (Mouse)
Function: Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them (By similarity). Key regulator of LPAR1 signaling (By similarity). Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor (By similarity). Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner (By similarity). Positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway by facilitating the trafficking of SMO into the cilium and the stimulation of SMO activity (By similarity). Inhibits relaxation of airway smooth muscle in response to blue light.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P26817}. Cell membrane {ECO:0000250|UniProtKB:P21146}. Postsynapse {ECO:0000250|UniProtKB:P26817}. Presynapse {ECO:0000250|UniProtKB:P26817}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Beta-arrestin-2
- Beta-arrestin-1
- ARF GTPase-activating protein GIT1
- Protein smoothened
- NADH-ubiquinone oxidoreductase chain 1
- Mu-type opioid receptor
- C-X-C chemokine receptor type 2
- Beta-2 adrenergic receptor
- Casein kinase I isoform epsilon
Sequence:
MADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFSQKLGYLLFRDFCLNHLEEAKPLVEFYEEIKKYEKLETEEERVVRSREIFDSYIMKELLACSHPFSKNATEHVQGHLVKKQVPPDLFQPYIEEICQNLRGDVFQKFIESDKFTRFCQWKNVELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEADMRFYAAEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKRPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGCLGRGAQEVKESPFFRSLDWQMVFLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDSDQELYRNFPLTISERWQQEVAETVFDTINAETDRLEARKKAKNKQLGHEEDYALGKDCIVHGYMSKMGNPFLTQWQRRYFYLFPNRLEWRGEGEAPQSLLTMEEIQSVEETQIKERKCLLLKIRGGKQFVLQCDSDPELVQWKKELRDAYREAQQLVQRVPKMKNKPRSPVVELSKVPLIQRGSANGL
Protein: Chloride channel protein ClC-Kb (Chloride channel Kb) (ClC-K2) (P51802)
Organism: Rattus norvegicus (Rat)
Function: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. May be important in urinary concentrating mechanisms.
Subcellular location: Basolateral cell membrane {ECO:0000250|UniProtKB:P51801}; Multi-pass membrane protein {ECO:0000255}. Note=Recruited to the plasma membrane in the presence of BSND protein, whereas remains in the Golgi in its absence. {ECO:0000269|PubMed:12761627}.
Interaction partners:
- Barttin
- ATP-sensitive inward rectifier potassium channel 1
- Solute carrier family 12 member 1-chloride cotransporter 1)
- Solute carrier family 12 member 3
Sequence:
MEEIVGLREGSPRKPVPLQELWRPCPRIRRNIQGSLEWLKERLFRVGEDWYFLVALGVLMALISYAMNFAIGRVVRAHKWLYREIGDGHLLRYLSWTVYPVALLSFSSGFSQSITPSSGGSGIPEVKTILTGVILEDYLDIKNFGAKVVGLSCTLATGSTIFLGKLGPFVHLSVMIAAYLGRVRTKTVGEPENKTKEMELLAAGAAVGVATVFAAPISGVLFSIEVMSSHFSVWDYWRGFFAATCGAFMFHLLAVFNSEQETITSIYKTSFPVDIPFDLPEIFFFVALGAICGILSCGYNYCQRTSLFFLKSNGFTSKLLATSKPLYSALAAVVLASITYPPGVGRFMASRLSMSEYLETLFDNNSWALMTKNSSPPWSAEPDPQNLWLEWCHPQMTVFGTLVFFLVMKFWMLILATTIPIPAGYFLPIFVYGAAIGRLFGEVLSLAFPEGIVAGGKVSPIMPGAYALAGAAAFSGAVTHTLSTALLAFEVSGQIVHALPVLMAVLAANAICQSYQPSFYDGTIIVKKLPYLPWIRGRKIGSHLVTVGHFMNCTLTTLAKDMPLEEVIKVVISTDVTQYPLVETTESQVLVGIVKRTHLVQSLHTDSASWAPGQQPCLQDILANGCPTQPVTLQLSTETSLHETHNLFELLNLQLLFVTSRGRAVGSVSWVELKKAISTLTNPPAPK
Protein: Protein BZZ1 (Q09746)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in endocytosis and trafficking to the vacuole. Functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress (By similarity).
Subcellular location: Cell tip {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, actin patch {ECO:0000250}.
Interaction partners:
- Actin-binding protein wsp1
- Verprolin
- Myosin-1
- Protein dip1
- Protein csh3
- Actin
- Epsin-1
- Actin cytoskeleton-regulatory complex protein end3
- Endocytosis protein end4
- Actin cytoskeleton-regulatory complex protein pan1
Sequence:
MSLETYKFSDELHDDFKVVDSWINNGAKWLEDIQLYYKERSSIEKEYAQKLASLSNKYGEKKSRKSSALSVGDTPAMSAGSLECASLTTWSKILDELTRSSKTHQKLSDDYSLDIAEKLKKLESHIEALRKVYDDLYKKFSSEKETLLNSVKRAKVSYHEACDDLESARQKNDKYREQKTQRNLKLSESDMLDKKNKYLLRMLVYNAHKQKFYNETLPTLLNHMQVLNEYRVSNLNEIWCNSFSIEKSLHDTLSQRTVEIQSEIAKNEPVLDSAMFGRHNSKNWALPADLHFEPSPIWHDTDALVVDGSCKNYLRNLLVHSKNDLGKQKGELVSLDSQLEGLRVDDPNSANQSFESKKASINLEGKELMVKARIEDLEVRINKITSVANNLEEGGRFHDFKHVSFKLPTSCSYCREIIWGLSKRGCVCKNCGFKCHARCELLVPANCKNGEPEVADDDAVDTSVTATDDFDASASSSNAYESYRNTYTDDMDSSSIYQTSLSNVKTEETTPAEPASKVDGVVLYDFTGEHEGVITASEGQEFTLLEPDDGSGWVRVKIDGTDGLIPASYVKLNDELNTSVTLDGDSSYVKALYAYTAQSDMELSIQEGDIIQVTNRNAGNGWSEGILNGVTGQFPANYVTDV
Protein: Fibronectin type III domain-containing protein 11 (Q9BVV2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSTHVAGLGLDKMKLGNPQSFLDQEEADDQQLLEPEAWKTYTERRNALREFLTSDLSPHLLKRHHARMQLLRKCSYYIEVLPKHLALGDQNPLVLPSALFQLIDPWKFQRMKKVGTAQTKIQLLLLGDLLEQLDHGRAELDALLRSPDPRPFLADWALVERRLADVSAVMDSFLTMMVPGRLHVKHRLVSDVSATKIPHIWLMLSTKMPVVFDRKASAAHQDWARLRWFVTIQPATSEQYELRFRLLDPRTQQECAQCGVIPVAACTFDVRNLLPNRSYKFTIKRAETSTLVYEPWRDSLTLHTKPEPLEGPALSHSV
Protein: Andropin (P21663)
Organism: Drosophila melanogaster (Fruit fly)
Function: Male-specific peptide with moderate activity against Gram-positive bacteria.
Subcellular location: Secreted.
Interaction partners:
- GH21475p
- DNA-binding protein modulo
- Odorant binding protein c
- Serpin 77Bb
Sequence:
MKYFVVLVVLALILAISVGPSDAVFIDILDKVENAIHNAAQVGIGFAKPFEKLINPK
Protein: Transcription termination factor 1 (TTF-1) (RNA polymerase I termination factor) (Transcription termination factor I) (TTF-I) (Q15361)
Organism: Homo sapiens (Human)
Function: Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q62187}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q62187}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q62187}. Note=May be localized to the nucleolus in an NPM1/B23-dependent manner. May be displaced from the nucleolus into the nucleoplasm in an CDKN2A/ARF-dependent manner. May shuttle back and forth from nucleoplasm to nucleolus. {ECO:0000250|UniProtKB:Q62187}.
Interaction partners:
- Bromodomain adjacent to zinc finger domain protein 2A
- Thyroid transcription factor 1-associated protein 26
- Protein kinase C beta type
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Protein kinase C gamma type
- cAMP-dependent protein kinase catalytic subunit gamma
- Protein kinase C alpha type
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
- Surfactant protein C
Sequence:
MEGESSRFEIHTPVSDKKKKKCSIHKERPQKHSHEIFRDSSLVNEQSQITRRKKRKKDFQHLISSPLKKSRICDETANATSTLKKRKKRRYSALEVDEEAGVTVVLVDKENINNTPKHFRKDVDVVCVDMSIEQKLPRKPKTDKFQVLAKSHAHKSEALHSKVREKKNKKHQRKAASWESQRARDTLPQSESHQEESWLSVGPGGEITELPASAHKNKSKKKKKKSSNREYETLAMPEGSQAGREAGTDMQESQPTVGLDDETPQLLGPTHKKKSKKKKKKKSNHQEFEALAMPEGSQVGSEVGADMQESRPAVGLHGETAGIPAPAYKNKSKKKKKKSNHQEFEAVAMPESLESAYPEGSQVGSEVGTVEGSTALKGFKESNSTKKKSKKRKLTSVKRARVSGDDFSVPSKNSESTLFDSVEGDGAMMEEGVKSRPRQKKTQACLASKHVQEAPRLEPANEEHNVETAEDSEIRYLSADSGDADDSDADLGSAVKQLQEFIPNIKDRATSTIKRMYRDDLERFKEFKAQGVAIKFGKFSVKENKQLEKNVEDFLALTGIESADKLLYTDRYPEEKSVITNLKRRYSFRLHIGRNIARPWKLIYYRAKKMFDVNNYKGRYSEGDTEKLKMYHSLLGNDWKTIGEMVARSSLSVALKFSQISSQRNRGAWSKSETRKLIKAVEEVILKKMSPQELKEVDSKLQENPESCLSIVREKLYKGISWVEVEAKVQTRNWMQCKSKWTEILTKRMTNGRRIYYGMNALRAKVSLIERLYEINVEDTNEIDWEDLASAIGDVPPSYVQTKFSRLKAVYVPFWQKKTFPEIIDYLYETTLPLLKEKLEKMMEKKGTKIQTPAAPKQVFPFRDIFYYEDDSEGEDIEKESEGQAPCMAHACNSSTLGGQGRWII
Protein: Neurexin-3-beta (Q18291)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MRQKFDDTGQYLTIWLVFTVSLFSVVDSIILTGAPDSYARYPKWAHSFENSLSMELKTRQSDGMLLYTDDGGTHGNFYSLTIVEGHIQLDFRLGDNSNEFGQRRPVNTIRIEEVRIDDDKWHTLTIFQSWENVKLELDYTLVFKILNQRSFVFGNILKNSDVFIGGLPPNMHMLPVMSSPLRRYARHLAVNVRNLMYRQYPQGVTSPQLLESVGTRTNEDDHCKSKSMSSREQFVCLNDGECYSSNDGPHCDCQFSDHDGRNCEIEKNDGELTFGGDEWVGYDVSLNISAAVRAKKENLTLTFKTVHGTSMLFYAGDEKSYLHVMLQDGAIIASSKFDGSDARIIRMFNSFPSQRYDDDSWHTIILERSLQMMTLIVDGRRDEIRQYAPELDWISNSFGFLGSIPKHNPSKEVNRVSFRGCMKKVRYDIDATRILLVNLADQSYGGSVVKTEGDISYSCKNPSQRSDVLSFTETSSYLTLPRWNSLSSGSLSFHFRTTSSDGLILYHGVMQHNATDYVAFELIDSHLFMIINLGSGVVRLQTTSMKVSDGEWHHVQLDRLSRTGSVIVDAIKIDFSTPGVSANLIIDDPIFIGNVPNNSLVYPSSVWSIALQKGYTGCIKNIRMNGVSTKIGQEFEASNSTGIELGCSLSNELDICEPNPCQNFGKCSKNLNSFDCDCSNTNFEGKQCELEQTAVEVNGEESKVHVLAHTKVSQVEHIKIRFRTTSSRGVLFDTGANGKNDKITVFLNDSQLNLFLQDSSTNNTFSWGKSLSDNHWHELQVRRLGQKLLLYLDGFWSHSIYLQNPISVEIDEVGAAFSVHSSAPPPRDEHFKGFLSKLVFNGNDYLAKTKMNSAQLSKSSSRESKGQRNVKTRIASISFTNSTGYVAFSSDKISGLTGSFRVQFKFQTLMRSALLFFTLPKHDYDQSFRLQMLNGRLKYTYRTSGQEFHTTSPKLPHRQHLSDMRWHNVLIYQDEKTHDHVLLVDNSSTTLIIDKIKKVESKMSGKLYFGSNPLGVSRPSNGFRGCISTLRINENALDLYEDADSRMKVNRGCSGPIARCIEDACANHGRCIQLWSSIRCDCSLTAHSGDRCQNPSTTVRFDGSPSAIFYEYAPNERPTTSKDYFVFSFRTTQPNGVLISIECAADQDYFTIFLNKGYLNAHYNLGNRDHTTSYHTRILNDGFPHVIKISRTEANMTIQVDKLPSLRYRPKRASDLVLLNMQTRISIGAAFNTRHLDQKRLLRHRRNTEIFDSYQGEISGVNVNGLMILDLYENGSNRIHTIGAPQTTAVSEQVSSESEEDDELAEMMMAHSIDENPNEALIESLAPSCLSLEEQQSCFIDTDDSTGFFSPVLPTVANFPTTRQTEHIDNEVTALITSSLAPQKTRPKSTPHFTVYPVRPTTPMGDTITTTMQAATVTDFPRTPLIMCSSLAVIIAIAAVVFFVFKCRQNPPNSEHYTMAMKSQSGYTAIAPELSPPMNHDRSNDSCTQPLLAKPHINGNGYEPLKGAVIANGNGATATMMRNGNGNGVAKKKDFKEWYV
Protein: N-acetyltransferase family 8 member 3 (EC 2.3.1.48) (Camello-like protein 3) (N-acetyltransferase CML3) (Q9JIY8)
Organism: Mus musculus (Mouse)
Function: Has histone acetyltransferase activity in vitro, with specificity for histone H4.
Subcellular location: Nucleus membrane {ECO:0000305|PubMed:25123547}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000305|PubMed:25123547}. Cytoplasm {ECO:0000305|PubMed:25123547}. Note=C-terminally tagged constructs localize to the nuclear membrane and perinuclear region. N-terminally tagged constructs show a punctate cytoplasmic distribution. {ECO:0000269|PubMed:25123547}.
Interaction partners:
- Cytosol aminopeptidase
- Aminopeptidase N
Sequence:
MAPYHIRKYQDSDHRSVVDLFRRGMEEHIPATFRHMLLLPRTLLLLLGVPLTLFLASGSWLLVLLSILTLFLSLWFLAKYTWEKHVMNCLHTDMADITRTYLSSHSSCFWVAESRGQTVGMVAARPVKDPLLQKKQLQLLHLSVSLQHRREGLGKAMVRTVLQFAQMQGFSEVVLSTSMLQYAALALYQGMGFQKTGETFYTYLSRLRKSPMINLKYSLTSREGDL