wanglab/gogpt-training-data huggingface dataset:
Protein: ATP synthase F(1) complex subunit gamma, mitochondrial (ATP synthase F1 subunit gamma) (F-ATPase gamma subunit) (Q91VR2)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05631}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05631}; Matrix side {ECO:0000250|UniProtKB:P05631}.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
Sequence:
MFSRASVVGLSACAVQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGTGSLALYEKADIKAPEDKKKHLIIGVSSDRGLCGAIHSSVAKQMKNEVAALTAAGKEVMIVGVGEKIKGILYRTHSDQFLVSFKDVGRKPPTFGDASVIALELLNSGYEFDEGSIIFNQFKSVISYKTEEKPIFSLNTIATAETMSIYDDIDADVLQNYQEYNLANLIYYSLKESTTSEQSARMTAMDNASKNASDMIDKLTLTFNRTRQAVITKELIEIISGAAALD
Protein: Deoxynucleotidyltransferase terminal-interacting protein 1 (Terminal deoxynucleotidyltransferase-interacting factor 1) (TdIF1) (TdT-interacting factor 1) (Q9H147)
Organism: Homo sapiens (Human)
Function: Increases DNTT terminal deoxynucleotidyltransferase activity (in vitro). Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription. Binds DNA and nucleosomes; may recruit HDAC1 complexes to nucleosomes or naked DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:11473582, ECO:0000269|PubMed:16371131}.
Interaction partners:
- Mitotic deacetylase-associated SANT domain protein
- Histone deacetylase 1
- Transcriptional-regulating factor 1
- DNA nucleotidylexotransferase
- Histone deacetylase 2
- Zinc finger protein 541
Sequence:
MGATGDAEQPRGPSGAERGGLELGDAGAAGQLVLTNPWNIMIKHRQVQRRGRRSQMTTSFTDPAISMDLLRAVLQPSINEEIQTVFNKYMKFFQKAALNVRDNVGEEVDAEQLIQEACRSCLEQAKLLFSDGEKVIPRLTHELPGIKRGRQAEEECAHRGSPLPKKRKGRPPGHILSSDRAAAGMVWKPKSCEPIRREGPKWDPARLNESTTFVLGSRANKALGMGGTRGRIYIKHPHLFKYAADPQDKHWLAEQHHMRATGGKMAYLLIEEDIRDLAASDDYRGCLDLKLEELKSFVLPSWMVEKMRKYMETLRTENEHRAVEAPPQT
Protein: GDNF family receptor alpha-like (Q6SJE0)
Organism: Mus musculus (Mouse)
Function: Brainstem-restricted receptor for GDF15 which regulates food intake, energy expenditure and body weight in response to metabolic and toxin-induced stresses. Upon interaction with its ligand, GDF15, interacts with RET and induces cellular signaling through activation of MAPK- and AKT- signaling pathways.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6UXV0}; Single-pass membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
Interaction partners:
- Growth/differentiation factor 15
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Glial cell line-derived neurotrophic factor
- Persephin
Sequence:
MLVFIFLAVTLSSENESSSQTNDCAHLIQKCLIDANGCEQSWRSMEDTCLTPGDSCKINNSLHCNLSIQALVEKNFQFKECLCMDDLHCTVNKLFGKKCTNKTDNMEKDNKDKWNLTTTPFYHGFKQMQSCLEVTEACVGDVVCNAQLALYLKACSANGNLCDVKHCQAAIRFFYQNMPFNTAQMLAFCDCAQSDIPCQQSKETLHSKPCALNIVPPPTCLSVIHTCRNDELCRTHYRTFQTECWPHITGKCHEDETCISMLGKQDLTCSGSESCRAAFLGTFGTVLQVPCACRGVTQAEEHVCMIFQHMLHSKSCFNYPTPNVKDISSYEKKNSKEITLTGFNSFFNGELLYVVVCMAVTCGILFLVMLKLRIQSEKRDPSSIEIAGGVIIQ
Protein: Protein phosphatase 1H (EC 3.1.3.16) (Q9ULR3)
Organism: Homo sapiens (Human)
Function: Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:22586611}. Cytoplasm {ECO:0000269|PubMed:22586611}.
Interaction partners:
- RILP-like protein 2
Sequence:
MLTRVKSAVANFMGGIMAGSSGSEHGGGSCGGSDLPLRFPYGRPEFLGLSQDEVECSADHIARPILILKETRRLPWATGYAEVINAGKSTHNEDQASCEVLTVKKKAGAVTSTPNRNSSKRRSSLPNGEGLQLKENSESEGVSCHYWSLFDGHAGSGAAVVASRLLQHHITEQLQDIVDILKNSAVLPPTCLGEEPENTPANSRTLTRAASLRGGVGAPGSPSTPPTRFFTEKKIPHECLVIGALESAFKEMDLQIERERSSYNISGGCTALIVICLLGKLYVANAGDSRAIIIRNGEIIPMSSEFTPETERQRLQYLAFMQPHLLGNEFTHLEFPRRVQRKELGKKMLYRDFNMTGWAYKTIEDEDLKFPLIYGEGKKARVMATIGVTRGLGDHDLKVHDSNIYIKPFLSSAPEVRIYDLSKYDHGSDDVLILATDGLWDVLSNEEVAEAITQFLPNCDPDDPHRYTLAAQDLVMRARGVLKDRGWRISNDRLGSGDDISVYVIPLIHGNKLS
Protein: Patched-related, isoform E (A0A0B4KEC6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTCGISCVDKTLNKSFYHLGICIAKHPGYFIIIPVLLTLLCMTGYQQLKYQIDPEYLFSPIAGEGKTERAIVEQYFKVNYTHRFNVGRITRPGK
Protein: Inositol-3-phosphate synthase 1 (IPS 1) (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase) (MI-1-P synthase) (MIP synthase) (Q6AYK3)
Organism: Rattus norvegicus (Rat)
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11986}.
Interaction partners:
- Inositol monophosphatase 1
- Inositol monophosphatase 2
- Type II inositol 3,4-bisphosphate 4-phosphatase
- Inositol polyphosphate-4-phosphatase type I A
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol polyphosphate-1-phosphatase.
Sequence:
MEPAAEILVDSPDVIFGPEAIEARYEYRTTRVSREGGVLRVRPTATRFTFRTARQVPRLGVMLVGWGGNNGSTLTAAVLANRLRLTWPTRTGRKEANYYGSLTQAGTVNLGLDGDGREVFVPFSALLPMVAPNDLVFDGWDISSLNLAEAMRRAQVLDCGLQEQLWPHMESLRPRPSVYIPEFIAANQTARADNLIPGTRAQQLEQIRKDIRDFRSSAGLDKVIVLWTANTERFCEVVPGRNDTAENLLRTIQLGLEVSPSTLFAVASILEGCAFLNGSPQNTLVPGALELASQRHVFVGGDDFKSGQTKVKSVLVDFLIGSGLKTMSIVSYNHLGNNDGQNLSAPLQFRSKEVTKSSVVDDMVQSNRVLYAPGEEPDHCVVIKYVPYVGDSKRALDEYTSELMLGGTNTLVLHNTCEDSLLAAPIMLDLVLLTELCQRVSFCTDSDPEPQGFHPVLSVLSFLFKAPLVPPGSPVVNALFRQRSCIENIFRACVGLPPQNHMLLEHKMERPFPGIKPEEVKATSPLPCKKESTPATNGCTGDANGHTQAPTPELSTA
Protein: Ethylene induced calmodulin binding protein (F4KCL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MARKKKSVSFSHLDIARNEGNKIISFSVHAYSDRLGFVDSLFDYESLRSLLVDFWVYPSMVDRRSFGSITPPLQLDMEQLLSEAQHRWLRPTEICEILQNYHKFHIASESPTRPASGSLFLFDRKVLRYFRKDGHNWRKKKDGKTIREAHEKLKVGSIDVLHCYYAHGEANENFQRRCYWMLEQYYYRKASSHWVLVATLSLFSFGYLRPSWVRHLMHIVFVHYLEVKGNRTSIGMKENNSNSVNGTASVNIDSTASPTSTLSSLCEDADTVLVQGIVNKQVPSYDHLLNLKLEIAMVGHLLLACVMFHRFMGTESEKMQPSNTDSMLVEENSEKGGRLKAEHIRNPLQTQFNWQDDTDLALFEQSAQDNFETFSSLLGSENLQPFGISYQAPPSNMDSEYMPVMKILRRSEDSLKKVDSFSKWAIKELGEMEDLQMQSSRGDIAWTTVECETAAAGISLSPSLSEDQRFTIVDFWPKSAKTDAEVEVMVIGTFLLSPQEVTKYNWSCMFGEVEVPAEILVDGVLCCHAPPHTAGHVPFYVTCSNRFACSEVREFDFLSGSTQKINATDVYGTYTNEASLQLRFEKMLAHRDFVHEHHIFEDVGDKRRQISKIMLLKEEKEYLLPGTYQRDSTKQEPKGQLFRELFEEELYIWLIHKVTEEGKGPNILDEDGQGILHFVAALGYDWAIKPVLAAGVNINFRDANGWSALHWAAFSGREETVAVLVSLGADAGALTDPSPELPLGKTAADLAYANGHRGISGFLAESSLTSYLEKLTVDSKENSPANSCGEKAVQTVSERTAAPMTYGDVPEKLSLKDSLTAVRNATQAADRLHQVFRMQSFQRKQLCDIGDDEKIDISDQLAVSFAASKTKNPGQGDVSLSCAATHIQKKYRGWKKRKEFLLIRQRIVKIQAHVRGHQVRKQYRTVIWSVGLLEKIILRWRRKGNGLRGFKRNAVAKTVEPEPPVSAICPRIPQEDEYDYLKEGRKQTEERLQKALTRVKSMVQYPEARDQYRRLLTVVEGFRENEASSSASINNKEEEAVNCEEDDFIDIESLLNDDTLMMSISP
Protein: Probable myosin-binding protein 4 (F4INW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Membrane-anchored myosin receptors that define a distinct, plant-specific transport vesicle compartment.
Subcellular location: Endomembrane system {ECO:0000305|PubMed:23995081}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDSNLIFDQKVINGFAPVLTYAACEWFLILLMFIDALLSYLLVWFARYCRLQMPCFLCSKLLHPLHWRFLLCRNHRSEVSSYMSCQNHGNNLADCRGMCDDCLLSFTKMTGPNPDMNRLLLGKLGYDLLSRSHFAHPRSCSCCNKPWRTRHHTQRLIRLGSRGRNSSSKPNIPAPRHLTRRGSGGSLKKMRDHIATSGSEYVDVGSRDGMAHVGYTELKIHSDSESEFLFSDDDAFLHITDFNVEPSEKRTHKSRRRKSFDDKKMSNHKQPVLQDNQYKKIHVEDNETVESSMLGYNLENRTRQKQPVKAKEHDDVLSELITMSEARPFLLGSPRKYAAGVVTQNENEAEVSGSSSPSGGEFLSPSAENGASREIRIQEHDDSSDFSQNITSSAMEIEEFEAAIEQKESDHMDVSGSVANEPSSDEENEVEGDSKPLISNNMSDSLEQEQSGEEESEVNENNVAEEYFSNEEEDEVNGHTEPLTSKSESGSFAEEQSSEDEDGSNIYSVAKDHSSNEEDVDNEESEPMTSNNVTGVVKEEHSAKEEHGDHEETEPLTSLNISKEEPSLEHSDKDSLKITETRNTSNGSPELKHSASVESFVSISSDIEGESLVEVLKQQLEHGRKSLRDLNKEFEEERNASAIATNQAMAMITRLQEEKAALHMEALQYLRMMDEQAEHDMDALERANDVLADREKEIQDLEMELEYYRVKYPDEPREEILASMGILGNTEETNVTSPTDETSIKDSTDTKLTGSPSAEN
Protein: Histone deacetylase 5 (F4K1Z5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAMAGESSGKKIGDCDGKVAGNRQRKVGLIYDETMCKHDTPDGEDHPECPDRIRVIWEKLQLAGVSQRCVVLGSSKAEDKHLQLVHTKDHVNLVKSISTKQKDYRRNRIASQLNSIYLNGGSSEAAYLAAGSVVKLAEKVAEGELDCGFAIVRPPGHHAEADEAMGFCLFNNVAVAASFLLNERPDLGVKKILIVDWDVHHGNGTQKMFWKDPRVLFFSVHRHEYGGFYPAGDDGDYNMVGEGPGEGFNINVPWDQGRCGDADYLAAWDHILIPVAREFNPDVIFLSAGFDAAINDPLGGCCVTPYGYSVMLKKVGVELMEFAQGKIVLALEGGYNLDSIAKSSLACVQVLLEDKQIQGPPEAYPFESTWRVIQAVRKRLCTYWPSLADELSWKLINQKTPTPIILISSSDSETEDNAQGLLDQMSKLSIENPQGTLLENHQVEPASTSWRADLAKVDVWYASFGSNMWKPRFLCYIQGGQVDGLKKVCVGSMDKSPPKETVWETFPHRLFFGRESSVGWGVGGVAFTNPLANLIDQTHMCLYRITLEQFNDVLSQENGLNVDSDSPVFDLAALQLVDNKGSILEAPLNSWYGNVVCLGKERDIPILTMTCTLSAVEKFKSGEIPIRPPAKAYANTLIRGLVEGGRLSKEEAEAYIDKAVSKPL
Protein: Photosystem I assembly protein Ycf3 (O20031)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00439}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00439}.
Interaction partners:
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I iron-sulfur center
- Photosystem I reaction center subunit II
- Uncharacterized protein
- Photosystem I reaction center subunit III
- Photosystem I assembly protein Ycf4
- Photosystem II protein D1
- Cytochrome b6-f complex subunit 4
- Photosystem II CP43 reaction center protein
Sequence:
MPRTQRNDNFIDKTFTVVADILLKVLPTSQREKQAFSYYRNGMSAQAEGEYAEALQNYYEAMRLEVDAYDRSYILYNIGLIHTSNGEHGRALEYYYQALERNPSLSSALNNIAVIYHYRGEQAIENGQSEISQILFEKAADYWKEAIRLAPTNYIEALNWLKMTGRLTGLAT
Protein: Telomerase reverse transcriptase (EC 2.7.7.49) (Telomerase catalytic subunit) (Q06163)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Subcellular location: Nucleus. Chromosome, telomere.
Interaction partners:
- Telomere elongation protein EST1
- Telomere replication protein EST3
- ATP-dependent DNA helicase II subunit 1
- H/ACA ribonucleoprotein complex subunit NOP10
- H/ACA ribonucleoprotein complex subunit NHP2
- Cell division control protein 13
- ATP-dependent DNA helicase II subunit 2
- Ribonucleases P/MRP protein subunit POP6
- Protein STN1
- Replication factor A protein 1
Sequence:
MKILFEFIQDKLDIDLQTNSTYKENLKCGHFNGLDEILTTCFALPNSRKIALPCLPGDLSHKAVIDHCIIYLLTGELYNNVLTFGYKIARNEDVNNSLFCHSANVNVTLLKGAAWKMFHSLVGTYAFVDLLINYTVIQFNGQFFTQIVGNRCNEPHLPPKWAQRSSSSSATAAQIKQLTEPVTNKQFLHKLNINSSSFFPYSKILPSSSSIKKLTDLREAIFPTNLVKIPQRLKVRINLTLQKLLKRHKRLNYVSILNSICPPLEGTVLDLSHLSRQSPKERVLKFIIVILQKLLPQEMFGSKKNKGKIIKNLNLLLSLPLNGYLPFDSLLKKLRLKDFRWLFISDIWFTKHNFENLNQLAICFISWLFRQLIPKIIQTFFYCTEISSTVTIVYFRHDTWNKLITPFIVEYFKTYLVENNVCRNHNSYTLSNFNHSKMRIIPKKSNNEFRIIAIPCRGADEEEFTIYKENHKNAIQPTQKILEYLRNKRPTSFTKIYSPTQIADRIKEFKQRLLKKFNNVLPELYFMKFDVKSCYDSIPRMECMRILKDALKNENGFFVRSQYFFNTNTGVLKLFNVVNASRVPKPYELYIDNVRTVHLSNQDVINVVEMEIFKTALWVEDKCYIREDGLFQGSSLSAPIVDLVYDDLLEFYSEFKASPSQDTLILKLADDFLIISTDQQQVINIKKLAMGGFQKYNAKANRDKILAVSSQSDDDTVIQFCAMHIFVKELEVWKHSSTMNNFHIRSKSSKGIFRSLIALFNTRISYKTIDTNLNSTNTVLMQIDHVVKNISECYKSAFKDLSINVTQNMQFHSFLQRIIEMTVSGCPITKCDPLIEYEVRFTILNGFLESLSSNTSKFKDNIILLRKEIQHLQAYIYIYIHIVN
Protein: Tetraspanin-33 (Tspan-33) (Penumbra) (hPen) (Proerythroblast new membrane) (Q86UF1)
Organism: Homo sapiens (Human)
Function: Plays an important role in normal erythropoiesis (By similarity). It has a role in the differentiation of erythroid progenitors (By similarity). Regulates maturation and trafficking of the transmembrane metalloprotease ADAM10. Negatively regulates ligand-induced Notch activity probably by regulating ADAM10 activity. Mediates docking of ADAM10 to zonula adherens by interacting with ADAM10 and, in a PDZD11-dependent manner, with the zonula adherens protein PLEKHA7.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26686862}; Multi-pass membrane protein {ECO:0000305}. Cell junction, adherens junction {ECO:0000269|PubMed:30463011}. Cytoplasm {ECO:0000269|PubMed:30463011}. Note=Is localized to zonula adherens by PLEKHA7 by a PDZD11-dependent interaction. {ECO:0000269|PubMed:30463011}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 10
- PDZ domain-containing protein 11
- Pleckstrin homology domain-containing family A member 7
- Afadin
- Hematopoietic progenitor cell antigen CD34
- Apoptosis regulator Bcl-2
- Non-selective voltage-gated ion channel VDAC1
- Bcl-2 homologous antagonist/killer
- Apoptosis regulator BAX
- Complement component C8 alpha chain
Sequence:
MARRPRAPAASGEEFSFVSPLVKYLLFFFNMLFWVISMVMVAVGVYARLMKHAEAALACLAVDPAILLIVVGVLMFLLTFCGCIGSLRENICLLQTFSLCLTAVFLLQLAAGILGFVFSDKARGKVSEIINNAIVHYRDDLDLQNLIDFGQKKFSCCGGISYKDWSQNMYFNCSEDNPSRERCSVPYSCCLPTPDQAVINTMCGQGMQAFDYLEASKVIYTNGCIDKLVNWIHSNLFLLGGVALGLAIPQLVGILLSQILVNQIKDQIKLQLYNQQHRADPWY
Protein: Growth hormone receptor (GH receptor) (Somatotropin receptor) [Cleaved into: Growth hormone-binding protein (GH-binding protein) (GHBP) (Serum-binding protein)] (P19756)
Organism: Sus scrofa (Pig)
Function: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to, and activates the JAK2/STAT5 pathway.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P10912}; Single-pass type I membrane protein {ECO:0000255}. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway. {ECO:0000250|UniProtKB:P19941}.; SUBCELLULAR LOCATION: [Growth hormone-binding protein]: Secreted {ECO:0000250|UniProtKB:P10912}. Note=Complexed to a substantial fraction of circulating GH. {ECO:0000250|UniProtKB:P10912}.
Interaction partners:
- Tyrosine-protein kinase JAK2
- Somatotropin
- Tyrosine-protein kinase
- Prolactin
- Tyrosine-protein kinase
- Insulin-like growth factor 1
- Leptin
- Pro-epidermal growth factor
Sequence:
MDLWQLLLTLAVAGSSDAFSGSEATPAVLVRASQSLQRVHPGLETNSSGKPKFTKCRSPELETFSCHWTDGVRHGLQSPGSIQLFYIRRSTQEWTQEWKECPDYVSAGENSCYFNSSYTSIWIPYCIKLTSNGGTVDQKCFSVEEIVQPDPPIGLNWTLLNISLTGIHADIQVRWEPPPNADVQKGWIVLEYELQYKEVNETQWKMMDPVLSTSVPVYSLRLDKEYEVRVRSRQRNSEKYGEFSEVLYVTLPQMSPFACEEDFRFPWFLIIIFGIFGLTVILFLLIFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIHDNYKHEFYSDDSWVEFIELDIDDPDEKTEGSDTDRLLNNDHEKSLTILGAKEDDSGRTSCYEPDILETDFNANDVCDGTAEVAQPQRLKGEADLLCLDQKNQNNSPSNDAAPATQQPSVILAEENKPRPLIISGTDSTHQTAHTQLSNPSSLANIDFYAQVSDITPAGSVVLSPGQKNKAGISQCDMHLEVVSPCPANFIMDNAYFCEADAKKCIAMAPHVEVESRLAPSFNQEDIYITTESLTTTAGRSATAECAPSSEMPVPDYTSIHIVQSPQGLVLNATALPLPDKEFLSSCGYVSTDQLNKIMP
Protein: Bcl-2-binding component 3, isoforms 1/2 (JFY-1) (p53 up-regulated modulator of apoptosis) (Q9BXH1)
Organism: Homo sapiens (Human)
Function: Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis. Promotes partial unfolding of BCL2L1 and dissociation of BCL2L1 from p53/TP53, releasing the bound p53/TP53 to induce apoptosis. Regulates ER stress-induced neuronal apoptosis (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11463391, ECO:0000269|PubMed:11463392, ECO:0000269|PubMed:11572983}. Note=Localized to the mitochondria in order to induce cytochrome c release.
Interaction partners:
Sequence:
MARARQEGSSPEPVEGLARDGPRPFPLGRLVPSAVSCGLCEPGLAAAPAAPTLLPAAYLCAPTAPPAVTAALGGSRWPGGPRSRPRGPRPDGPQPSLSLAEQHLESPVPSAPGALAGGPTQAAPGVRGEEEQWAREIGAQLRRMADDLNAQYERRRQEEQQRHRPSPWRVLYNLIMGLLPLPRGHRAPEMEPN
Protein: Protein TFG (TRK-fused gene protein) (Q92734)
Organism: Homo sapiens (Human)
Function: Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:27813252}. Note=Localizes to endoplasmic reticulum exit site (ERES), also known as transitional endoplasmic reticulum (tER) (PubMed:21478858, PubMed:27813252). {ECO:0000269|PubMed:21478858, ECO:0000269|PubMed:27813252}.
Interaction partners:
- High affinity nerve growth factor receptor
- Tropomyosin alpha-3 chain
- Protein transport protein Sec31A
- Protein transport protein Sec16A
- Nucleoprotein TPR
- Protein SEC13 homolog
- ALK tyrosine kinase receptor
- Kinesin-1 heavy chain
- Kinesin light chain 1
- Echinoderm microtubule-associated protein-like 4
Sequence:
MNGQLDLSGKLIIKAQLGEDIRRIPIHNEDITYDELVLMMQRVFRGKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFVNGQPRPLESSQVKYLRRELIELRNKVNRLLDSLEPPGEPGPSTNIPENDTVDGREEKSASDSSGKQSTQVMAASMSAFDPLKNQDEINKNVMSAFGLTDDQVSGPPSAPAEDRSGTPDSIASSSSAAHPPGVQPQQPPYTGAQTQAGQIEGQMYQQYQQQAGYGAQQPQAPPQQPQQYGIQYSASYSQQTGPQQPQQFQGYGQQPTSQAPAPAFSGQPQQLPAQPPQQYQASNYPAQTYTAQTSQPTNYTVAPASQPGMAPSQPGAYQPRPGFTSLPGSTMTPPPSGPNPYARNRPPFGQGYTQPGPGYR
Protein: T-cell factor 7 isoform C (Q5PU93)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPQLNGGGGDDLGANDEMIAFKDEGDHEEKIRESAFTESDLADLKSSLVSETEISQSPAVIRRGQQDEQRIYSDKREHLDDVPKHHDGGMYKAPYSGYPFLMLPEPYLPNGPVSPPSNKVSVVQQGMHPLTPLLPYEHFNPSPTHMPTDGGQKPGVHRHQTQEISGFYSLPQGQITPSMNWFSHSLMLQSGMHPTGIPHPAIVPPSGKQEHDQFDRSIYNKSHAEAKREKEPKKPVIKKPLNAFMLYMKEMRAKVIAECTLKESAAINQILGRRWHALTREEQAKYYELARKERQLHVQLYPSWSARDNYVSALGKKKRRKRDKQQDSSTGPGSPKKCRARFGLNQQTDWCGPCR
Protein: Chorion protein S16 (P22977)
Organism: Drosophila melanogaster (Fruit fly)
Function: Chorion membrane (egg shell) protein; plays a role in protecting the egg from the environment.
Subcellular location: Secreted {ECO:0000269|PubMed:2509714}.
Interaction partners:
- Chorion protein S19
- Chorion protein S36
- Chorion protein S18
- Chorion protein S38
- Vitelline membrane protein Vm34Ca
- IP19005p
- Chorion protein S15
- Femcoat
- Uncharacterized protein
- Vitelline membrane protein Vm26Aa
Sequence:
MSATLRLLCLMACCVALAVANRPNYGGSGYGASYGDVVKAAETAEAQASALTNAAGAAASAAKLDGADWNSLNRYGWEQGRPLLAKPYGPLDPLYAAALPPRSFVAEVDPVFKKSQYGGSYGENAYLKTDAKLGVVAI
Protein: Phenylethanolamine N-methyltransferase (PNMTase) (EC 2.1.1.28) (Noradrenaline N-methyltransferase) (A0A5F8AH41)
Organism: Macaca mulatta (Rhesus macaque)
Function: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor. Other substrates include phenylethanolamine, octopamine and normetanephrine.
Interaction partners:
- Dopamine beta-hydroxylase
- catechol O-methyltransferase
- Amine oxidase
- Amine oxidase
- Tyrosine 3-monooxygenase
Sequence:
MSGADRIPAAGAAPDSASGRAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRCLAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLREEPGAFNWSMYSQYACLIEGKGESWQEKERQLRARVKRVLPIDVHQPQPLGTGSPAPLPADTLVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLMVVPVSEEEVREALVRSGYEVRDLRTYIMPAHLQTGVDDVKGIFFAWAQKVGL
Protein: Sk-tropomodulin (Tropomodulin-4) (tropomodulin 4 (Muscle)) (Q9PUQ6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Nebulin.
- Actinin alpha 3b
- Tropomyosin 2
- Tropomyosin 4a
- Fast skeletal muscle myosin light polypeptide 3
- Actin alpha 1, skeletal muscle b.
- Myosin, heavy polypeptide 2, fast muscle specific isoform X1
- Dystrophin
Sequence:
MSKSDPRDIDEDAILRGLSAEELEQLDIELQELDPENTTLPAGFRQRDQTKKSPTGPFDRFALMDYLEKQAIEHKDRDDLVPFTGEKRGKAFVPKPGSGQIPADEQITLEPELEEALRNATDAEMCDIAAILGMYTLMSNKQYYDALNTTGKIANTEGINSVVKPDVYKIYPEEPPNDTNVEETLRYIQKNDNRLQEVNLNNIPDIPIPTLKEIFEAMKRNTHVLCLSIAGTRSNDPVAYAIAEMLQANKNLQSLNIESNFITAQGMMAIVKALRKNSTLIEIKIDNQRQKLGDSVEMEIASMLEKNSSIIKIGYHFTQQGPRARAAMAITRNNDILRQQRVR
Protein: Derlin (Q8IKV3)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363059}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363059}.
Interaction partners:
Sequence:
MNFILYIAVIIIYLTNIHCKNVYNIKKLSGKNNYKYNKISNNVKRLSNMNPPYYKRKDYLNIRMNKKTIQNFHTTNQNIHYKKFKNFVNKSKNKNKLYYLYIPNNDTNSIKGKKNKQNNKVLEIYFQQKKLLAQYFNNLKSSFIYKLKNTKIITKLFLSSSLLILTLNVIGLKPEDIALHSKRVLRAFEFYRIYTSALFYGDISLYVLTNIYMLYVQSNQLENILGSSEMLSYYISQISILSIICSYIKKPFYSTALLKSLLFVNCMLNPYQKANLIFGININNMYLPYLSILIDIIHAQNLKASISGLLGVTSGSIYYLLNIYLYDNYNKKVFKIPKFLETYLDSYDTIEIIQ
Protein: Calcium-activated chloride channel regulator 4 (EC 3.4.-.-) (Calcium-activated chloride channel family member 4) (hCLCA4) (Calcium-activated chloride channel protein 2) (CaCC-2) (hCaCC-2) (Chloride channel accessory 4) [Cleaved into: Calcium-activated chloride channel regulator 4, 110 kDa form; Calcium-activated chloride channel regulator 4, 30 kDa form] (Q14CN2)
Organism: Homo sapiens (Human)
Function: May be involved in mediating calcium-activated chloride conductance.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Apical cell membrane {ECO:0000250}. Secreted {ECO:0000250}. Note=The C-terminus 30 kDa form is anchored to the membrane. The N-terminus 110 kDa form is released from the membrane triggered by an unknown stimulus. {ECO:0000250}.
Interaction partners:
- Anoctamin-2
- Anoctamin-1
- Calcium-activated chloride channel regulator 1
- Calcium-activated chloride channel regulator 2
- Cystic fibrosis transmembrane conductance regulator
- Membrane-spanning 4-domains subfamily A member 12
Sequence:
MGLFRGFVFLLVLCLLHQSNTSFIKLNNNGFEDIVIVIDPSVPEDEKIIEQIEDMVTTASTYLFEATEKRFFFKNVSILIPENWKENPQYKRPKHENHKHADVIVAPPTLPGRDEPYTKQFTECGEKGEYIHFTPDLLLGKKQNEYGPPGKLFVHEWAHLRWGVFDEYNEDQPFYRAKSKKIEATRCSAGISGRNRVYKCQGGSCLSRACRIDSTTKLYGKDCQFFPDKVQTEKASIMFMQSIDSVVEFCNEKTHNQEAPSLQNIKCNFRSTWEVISNSEDFKNTIPMVTPPPPPVFSLLKISQRIVCLVLDKSGSMGGKDRLNRMNQAAKHFLLQTVENGSWVGMVHFDSTATIVNKLIQIKSSDERNTLMAGLPTYPLGGTSICSGIKYAFQVIGELHSQLDGSEVLLLTDGEDNTASSCIDEVKQSGAIVHFIALGRAADEAVIEMSKITGGSHFYVSDEAQNNGLIDAFGALTSGNTDLSQKSLQLESKGLTLNSNAWMNDTVIIDSTVGKDTFFLITWNSLPPSISLWDPSGTIMENFTVDATSKMAYLSIPGTAKVGTWAYNLQAKANPETLTITVTSRAANSSVPPITVNAKMNKDVNSFPSPMIVYAEILQGYVPVLGANVTAFIESQNGHTEVLELLDNGAGADSFKNDGVYSRYFTAYTENGRYSLKVRAHGGANTARLKLRPPLNRAAYIPGWVVNGEIEANPPRPEIDEDTQTTLEDFSRTASGGAFVVSQVPSLPLPDQYPPSQITDLDATVHEDKIILTWTAPGDNFDVGKVQRYIIRISASILDLRDSFDDALQVNTTDLSPKEANSKESFAFKPENISEENATHIFIAIKSIDKSNLTSKVSNIAQVTLFIPQANPDDIDPTPTPTPTPTPDKSHNSGVNISTLVLSVIGSVVIVNFILSTTI