wanglab/gogpt-training-data huggingface dataset:
Protein: Voltage-dependent T-type calcium channel subunit alpha (Q7YZR6)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
Interaction partners:
Sequence:
MLRQPVPELRSFQSLSKYAGGPRSVLGRRTSAITVNRRQSQSTRRHEDVEALGSIEGSKETLQLSEHGRLASSSEASPSRWEGRQIEWGNEEQIEEESELPYPGFAEPALRCFYQARPPRKWALQMVMSPWFDRITMAVIMINCVTLGMYRPCEDGPDCDTYRCQILDIIDNCIFVYFAFEMVIKIMALGFYGPAAYMSDTWNRLDFFIVMAGIAEFVLHEYLGGNINLTAIRTVRVLRPLRAVNRIPSMRILVNLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCVINLPKTISENQSALFNNVKLTRFYIPEDTSLEYICSQPDANGLHTCSNLPPYTVDGVKCNLTLDEYDKVTNDSCINWNIYYNECQVMQRNPFQGSVSFDNIGFAWVAIFLVISLEGWTDIMYYVQDAHSFWNWIYFVLLIVIGAFFMINLCLVVIATQFAETKRRETERMLQERKMLLNRDSISCTGSEIGGASSKEEGDTVYAAFVRFIGHTFRRTKRAAKKKYTAYMEERAERKSSERQQRRKSKLDDMATLSRIEEKAEDEEDETTITRENGDDQIEQNGDGVRIKRVKIEEEPKIKIGNGNSNGPHYKHSSSDEESDEDGEEDQVYDGEEAKKKSTPSKLWWFREKIQKFVICDHFTRGILVAILVNTLSMGVEYHQQPEILTVILEYSNLFFTALFALEMLLKIIASGLFGYLADGFNLFDGGIVALSVLELFQEGKGGLSVLRTFRLLRILKLVRFMPALRYQLVVMLRTMDNVTVFFGLLVLFIFIFSTLGMVLFGCKFCNHPDTGLQCTSAQVISSICECDRMNFDNFLFATVTVFQILTQEDWNMVLFNGMAQTNPWAALYFVALMTFGNYVLFNLLVAILVEGFQESKEEEKRQLEEDARKQAVEEEDERKRELELIIAKTTSPAFNNGVAPAECTCQRPSSPEESPSPRLLSANYHPSPERKHSANLDAIIDKRLVLRNSAPFDRSPVSEGRDDSRLNRHASLVLPVANGVPYRRQRVHSWSGLCHHFNPNCPVHGRRALIETYAREKFLEASQELKQALAEEEKRNEAKQNTFVRKLLKKTCLHNRTEFSLFLMGPKNPLRIKCLQTTQKKWFDYTVLFFIGINCITLAMERPSIPPDSFERQFLHISGYIFTVIFTGEMMMKVIANGCFIGQAAYFKDGWNILDGILVVISLINIAFELLATGDSPKIFGVIRVLRLLRALRPLRVINRAPGVKLVVMTLISSLKPIGNIVLICCTFFIIFGILGVQLFKGMMYHCIGPEVGNVTTKADCIEDYRNKWVNHRYNFDNLGQALMSLFVLSSKDGWVSIMYQGIDAVGVDVQPIENYNEWRMIYFISFLLLVGFFVLNMFVGVVVENFHKCKEALEKEMREKEKEKRLKRKLKRQKFEESMAGKRKKMERNYPYYHDYGHTRLFLHGIVTSKYFDLAIAAVIGINVISMAMEFYMMPMGLKYVLKALNYFFTAVFTLEAAMKLIALGFKRFFIEKWNRLDMFIVILSIAGIIFEEFEALELPINPTIIRVMRVLRIARVLKLLKMAKGIRSLLDTVGEALPQVGNLGSLFFLLFFIFAALGVELFGKLECSEDHPCDGLGEHAHFKNFGMAFLTLFRIATGDNWNGIMKDALRDDCDSSDHCETNCCVDPILAPCFFVIFVLISQFVLVNVVVAVLMKHLEESNKRDAEGPAEPTGENIENEITKSDDDEIVEEHEPLAIEHVKEGELDEEEETEEGPTTQIPDGHGGIKRLSMQVLEQELIEVERHLEERYRRASECLGGELQPLNPGEIEDLDDPEFRPRSRSHRPRARTNSALSNKSRGSHKSAL
Protein: Insulin receptor substrate 1 (IRS-1) (P35568)
Organism: Homo sapiens (Human)
Function: May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19639489}. Nucleus {ECO:0000269|PubMed:19639489}. Note=Nuclear or cytoplasmic localization of IRS1 correlates with the transition from proliferation to chondrogenic differentiation. {ECO:0000269|PubMed:19639489}.
Interaction partners:
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Insulin receptor
- Tyrosine-protein phosphatase non-receptor type 11
- Insulin
- Growth factor receptor-bound protein 2
- Insulin-like growth factor 1 receptor
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Insulin-like growth factor 1
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Insulin receptor substrate 2
Sequence:
MASPPESDGFSDVRKVGYLRKPKSMHKRFFVLRAASEAGGPARLEYYENEKKWRHKSSAPKRSIPLESCFNINKRADSKNKHLVALYTRDEHFAIAADSEAEQDSWYQALLQLHNRAKGHHDGAAALGAGGGGGSCSGSSGLGEAGEDLSYGDVPPGPAFKEVWQVILKPKGLGQTKNLIGIYRLCLTSKTISFVKLNSEAAAVVLQLMNIRRCGHSENFFFIEVGRSAVTGPGEFWMQVDDSVVAQNMHETILEAMRAMSDEFRPRSKSQSSSNCSNPISVPLRRHHLNNPPPSQVGLTRRSRTESITATSPASMVGGKPGSFRVRASSDGEGTMSRPASVDGSPVSPSTNRTHAHRHRGSARLHPPLNHSRSIPMPASRCSPSATSPVSLSSSSTSGHGSTSDCLFPRRSSASVSGSPSDGGFISSDEYGSSPCDFRSSFRSVTPDSLGHTPPARGEEELSNYICMGGKGPSTLTAPNGHYILSRGGNGHRCTPGTGLGTSPALAGDEAASAADLDNRFRKRTHSAGTSPTITHQKTPSQSSVASIEEYTEMMPAYPPGGGSGGRLPGHRHSAFVPTRSYPEEGLEMHPLERRGGHHRPDSSTLHTDDGYMPMSPGVAPVPSGRKGSGDYMPMSPKSVSAPQQIINPIRRHPQRVDPNGYMMMSPSGGCSPDIGGGPSSSSSSSNAVPSGTSYGKLWTNGVGGHHSHVLPHPKPPVESSGGKLLPCTGDYMNMSPVGDSNTSSPSDCYYGPEDPQHKPVLSYYSLPRSFKHTQRPGEPEEGARHQHLRLSTSSGRLLYAATADDSSSSTSSDSLGGGYCGARLEPSLPHPHHQVLQPHLPRKVDTAAQTNSRLARPTRLSLGDPKASTLPRAREQQQQQQPLLHPPEPKSPGEYVNIEFGSDQSGYLSGPVAFHSSPSVRCPSQLQPAPREEETGTEEYMKMDLGPGRRAAWQESTGVEMGRLGPAPPGAASICRPTRAVPSSRGDYMTMQMSCPRQSYVDTSPAAPVSYADMRTGIAAEEVSLPRATMAAASSSSAASASPTGPQGAAELAAHSSLLGGPQGPGGMSAFTRVNLSPNRNQSAKVIRADPQGCRRRHSSETFSSTPSATRVGNTVPFGAGAAVGGGGGSSSSSEDVKRHSSASFENVWLRPGELGGAPKEPAKLCGAAGGLENGLNYIDLDLVKDFKQCPQECTPEPQPPPPPPPHQPLGSGESSSTRRSSEDLSAYASISFQKQPEDRQ
Protein: ATP synthase mitochondrial F1 complex assembly factor 1 (Q811I0)
Organism: Mus musculus (Mouse)
Function: May play an essential role for the assembly of the mitochondrial F1-F0 complex.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34375736}; Peripheral membrane protein {ECO:0000305|PubMed:34375736}.
Interaction partners:
- ATP synthase F
- ATP synthase mitochondrial F1 complex assembly factor 2
- ATP synthase F
Sequence:
MAAVVSAAGGACPAVLQVAGLYRGLCAVRSRALGLGFVSPAQLRVFPVRRGSGLPPEGADGSGVSELEANPFYDRYRDKIQQLRRSDPAAFESRLEKRSEFRKQPVGHSKQSDFIKCMEQKTDALGKQPVSKGFTKDKTLSSVFNVEMVKDKTAEEIKQIWQQYFSAKDTVYAVIPKEKFDLIWNRAQSCPTFLCALPRRDGYEFFVGQWTGTELHFTALINIQTRGDAAASQLILYHYPELKEEKGIVLMTAEMDSTFLNVVEAQCIANQVQLFYATDRKEIYGLVETFNFRPNEFKYMSVIAELEQSGLGAELKRAQNQDKT
Protein: Solute carrier family 2, facilitated glucose transporter member 10 (Glucose transporter type 10) (GLUT-10) (F1R0H0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Facilitative glucose transporter required for the development of the cardiovascular system.
Subcellular location: Endomembrane system {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95528}.
Interaction partners:
- Transmembrane anterior posterior transformation 1a
Sequence:
MGCSVLLLTITVSTLGGLVFGYELGIISGALPQLQTHFSLGCVQQEAVVSALLIGSLFASIIGGWLIDRHGRRTSILLSNLLILAGSVILTTGTSFFALVIGRAVIGFAMTVSSMSCCIFVSEMVTPERRGLMVTLYEVGITVGILIAYAVNYIFNNVPLTGWRYMFGFAIIPSLIQLASIVLLPKQAEVFVIHDDDSRQADRLTEETETSNQHQQSEKYGVSDLFKSKDNMRRRTVIGVGLVLSQQFTGQPNVLFYASTILFSVGFQSNASAILASVGFGIVKVIATLLAMLCSDRAGRRSLLIGGCSMLAVGLILTGFLCRQSVIDTTKRCTSVGPHSNLTLSAEHDEGVGFSSQTLDVHEHLRSFSQSEDIYKWIIFTCLMAVVSAFSVSFGPMTWVVLSEIFPKDIRGRAFSFINCFNVGANLIVSFSFLSIIDVIGLSGVFLMYGVVGIAGVVFIYLVLPETKGKSLQDIDRELSQTRMIHRQELCSIFQRRRFSPGYQRVQLTSTAT
Protein: DnaJ heat shock protein family (Hsp40) member B1 (M0QXK0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREVRCQVGRCL
Protein: 26S proteasome non-ATPase regulatory subunit 2 homolog A (26S proteasome regulatory subunit RPN1a) (AtRPN1a) (26S proteasome regulatory subunit S2 homolog A) (Q9SIV2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). Required during embryogenesis. Required for optimal plant growth and stress responses. Required for innate immunity. Prevents JMJ27 accumulation in non-drought conditions.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:22577987}. Cytoplasm {ECO:0000269|PubMed:22577987}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 3 homolog A
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome non-ATPase regulatory subunit 1 homolog A
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 1 homolog B
- 26S proteasome regulatory subunit 6A homolog A
- 26S proteasome regulatory subunit 6A homolog B
Sequence:
MAPTQDPNSVGGGAKKDEATLKVPSKDPKKKDEKKDEDLSEEDLELKQNLELYVERVQDPNPELQKAALESMRQEIRASTSSMTSVPKPLKFLRPHYGTLKAFHETMADSDLKKYLSDILSVLALTMSADGERESLRFRLIGTEGDIGSWGHEYVRNLAGEIAQEYTKRQSEEASIDDLMELVQQIVAFHMKHNAETEAVDLLMDVEDLDLLLEHVDKTNFKRTCNYLTSAARYLPGPDDMLVLDISYMIYMKFEEYPNALQIALFLDNTQYVKQVFTSCTDLLKKKQFCYMIARHGITFELDDEMVADDDDREALQDIVNNTKLSEGYLTLARDIEVMEAKTPEDIYKAHLLDGRASSGASVDSARQNLAATFVNAFVNAGFGQDKLMTVPSDSTTGSSGNWLFKNKEHGKTSAAASLGMIQLWDVDSGLSQLDKYFHSNDNPIIAGALLGVGIVNCGIKNDCDPALALLGDYIDKEDSSVRIGAIMGLGISYAGSQNDQIRNKLSPILNDAKAPLDVIAFASLSLGMIYVGSCNEEVAQSIIFALMDRSEAELGDALTRFLPLGLGLLYLGKQESVEATAEVSKTFNEKIRKYCDMTLLSCAYAGTGNVLKVQDLLAQCGEHLEKGDIHQGPAVLGLAMVAMSEELGVDMEIRSLERMLQYGEQNIRRAVPLALGLLCISNPKVTVMDTLSRLSHDTDSEVAMSAIISLGLIGAGTNNARIAGMLRNLSSYYYKDMSLLFCVRIAQGLVHMGKGLLTLSPFHSERFLLSPTALAGIVTLLHACLDMKPIILGKYHYVLYFLVLAMQPRMMLTVDENLKPLSVPVRVGQAVDVVGQAGRPKTITGFQTHSTPVLLAAGERAELATDKYIPLSPILEGFIILKENPDYREE
Protein: Zinc finger and BTB domain-containing protein 10 (Zinc finger protein RIN ZF) (Q96DT7)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSFSEMNRRTLAFRGGGLVTASGGGSTNNNAGGEASAWPPQPQPRQPPPPAPPALQPPNGRGADEEVELEGLEPQDLEASAGPAAGAAEEAKELLLPQDAGGPTSLGGGAGGPLLAERNRRTLAFRGGGGGGLGNNGSSRGRPETSVWPLRHFNGRGPATVDLELDALEGKELMQDGASLSDSTEDEEEGASLGDGSGAEGGSCSSSRRSGGDGGDEVEGSGVGAGEGETVQHFPLARPKSLMQKLQCSFQTSWLKDFPWLRYSKDTGLMSCGWCQKTPADGGSVDLPPVGHDELSRGTRNYKKTLLLRHHVSTEHKLHEANAQESEIPSEEGYCDFNSRPNENSYCYQLLRQLNEQRKKGILCDVSIVVSGKIFKAHKNILVAGSRFFKTLYCFSNKESPNQNNTTHLDIAAVQGFSVILDFLYSGNLVLTSQNAIEVMTVASYLQMSEVVQTCRNFIKDALNISIKSEAPESVVVDYNNRKPVNRDGLSSSRDQKIASFWATRNLTNLASNVKIENDGCNVDEGQIENYQMNDSSWVQDGSPEMAENESEGQTKVFIWNNMGSQGIQETGKTRRKNQTTKRFIYNIPPNNETNLEDCSVMQPPVAYPEENTLLIKEEPDLDGALLSGPDGDRNVNANLLAEAGTSQDGGDAGTSHDFKYGLMPGPSNDFKYGLIPGTSNDFKYGLIPGASNDFKYGLLPESWPKQETWENGESSLIMNKLKCPHCSYVAKYRRTLKRHLLIHTGVRSFSCDICGKLFTRREHVKRHSLVHKKDKKYKCMVCKKIFMLAASVGIRHGSRRYGVCVDCADKSQPGGQEGVDQGQDTEFPRDEEYEENEVGEADEELVDDGEDQNDPSRWDESGEVCMSLDD
Protein: Submaxillary gland androgen-regulated protein 3A (Proline-rich protein 5) (Proline-rich protein PBI) (Q99954)
Organism: Homo sapiens (Human)
Function: May play a role in protection or detoxification.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKSLTWILGLWALAACFTPGESQRGPRGPYPPGPLAPPPPPCFPFGTGFVPPPHPPPYGPGRFPPPLSPPYGPGRIPPSPPPPYGPGRIQSHSLPPPYGPGYPQPPSQPRPYPPGPPFFPVNSPTDPALPTPAP
Protein: 3-methyl-2-oxobutanoate dehydrogenase subunit beta (EC 1.2.4.4) (Branched-chain alpha-ketoacid dehydrogenase E1 component subunit beta) (BCKADH E1-beta) (P9WIS1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).
Interaction partners:
- Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex
- 3-methyl-2-oxobutanoate dehydrogenase subunit alpha
- Multifunctional 2-oxoglutarate metabolism enzyme
- Probable dehydrogenase
- Dihydrolipoyl dehydrogenase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Ribose-phosphate pyrophosphokinase
- Uncharacterized protein Rv1734c
- NAD
- Probable soluble pyridine nucleotide transhydrogenase
Sequence:
MTQIADRPARPDETLAVAVSDITQSLTMVQAINRALYDAMAADERVLVFGEDVAVEGGVFRVTEGLADTFGADRCFDTPLAESAIIGIAVGLALRGFVPVPEIQFDGFSYPAFDQVVSHLAKYRTRTRGEVDMPVTVRIPSFGGIGAAEHHSDSTESYWVHTAGLKVVVPSTPGDAYWLLRHAIACPDPVMYLEPKRRYHGRGMVDTSRPEPPIGHAMVRRSGTDVTVVTYGNLVSTALSSADTAEQQHDWSLEVIDLRSLAPLDFDTIAASIQRTGRCVVMHEGPRSLGYGAGLAARIQEEMFYQLEAPVLRACGFDTPYPPARLEKLWLPGPDRLLDCVERVLRQP
Protein: Protein phosphatase 1 regulatory subunit 15A (Growth arrest and DNA damage-inducible protein GADD34) (Myeloid differentiation primary response protein MyD116 homolog) (O75807)
Organism: Homo sapiens (Human)
Function: Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing p53/TP53 phosphorylation on 'Ser-15'. Plays an essential role in autophagy by tuning translation during starvation, thus enabling lysosomal biogenesis and a sustained autophagic flux. Acts also a viral restriction factor by attenuating HIV-1 replication. Mechanistically, mediates the inhibition of HIV-1 TAR RNA-mediated translation.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:12556489, ECO:0000269|PubMed:21518769, ECO:0000269|PubMed:26742780}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:21518769}. Note=Associates with membranes via an N-terminal amphipathic intramembrane region. {ECO:0000269|PubMed:21518769}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 1
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Cyclic AMP-dependent transcription factor ATF-4
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 2
Sequence:
MAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLAIPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPGEEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVSPRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFLKAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFLKAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPPPPWAPPRLPLRLQRRLKRPETPTHDPDPETPLKARKVRFSEKVTVHFLAVWAGPAQAARQGPWEQLARDRSRFARRITQAQEELSPCLTPAARARAWARLRNPPLAPIPALTQTLPSSSVPSSPVQTTPLSQAVATPSRSSAAAAAALDLSGRRG
Protein: Tumor protein D55 (hD55) (Testis development protein NYD-SP25) (Tumor protein D52-like 3) (Q96J77)
Organism: Homo sapiens (Human)
Interaction partners:
- Tumor protein D53
- Tumor protein D52
- Tumor protein D54
Sequence:
MPHARTETSVGTYESHSTSELEDLTEPEQRELKTKLTKLEAEIVTLRHVLAAKERRCGELKRKLGLTALVGLRQNLSKSWLDVQVSNTYVKQKTSAALSTMGTLICRKLGGVKKSATFRSFEGLMGTIKSKVSGGKRAWP
Protein: Sialomucin core protein 24 (MUC-24) (Endolyn) (Multi-glycosylated core protein 24) (MGC-24) (MGC-24v) (Q9QX82)
Organism: Rattus norvegicus (Rat)
Function: Sialomucin that may play a key role in hematopoiesis. May be involved in cell adhesion. Promotes myogenesis by enhancing CXCR4-dependent cell motility. Positively regulates myoblast migration and promotes myoblast fusion into myotubes (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q04900}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q04900}. Lysosome membrane {ECO:0000269|PubMed:10620506}; Single-pass type I membrane protein {ECO:0000269|PubMed:10620506}. Endosome membrane {ECO:0000269|PubMed:10620506}; Single-pass type I membrane protein {ECO:0000269|PubMed:10620506}.
Interaction partners:
Sequence:
MSGASRGLFWAATCLAALCLSAAQSNSSASPNVTDPPTTTSKVVPTTLTTTKPPETCESFNSCVSCVNATLTNNITCVWLDCHEANKTYCSSELVSNCTQKTSTDSCSVIPTTPVPTNSTAKPTTRPSSPTPTPSVVTSAGATNTTVTPTSQPERKSTFDAASFIGGIVLVLGVQAVIFFLYKFCKSKERNYHTL
Protein: SH3 and cysteine-rich domain-containing protein 3 (Q96MF2)
Organism: Homo sapiens (Human)
Function: Required for normal excitation-contraction coupling in skeletal muscle and for normal muscle contraction in response to membrane depolarization. Required for normal Ca(2+) release from the sarcplasmic reticulum, which ultimately leads to muscle contraction. Probably functions via its effects on muscle calcium channels. Increases CACNA1S channel activity, in addition to its role in enhancing the expression of CACNA1S at the cell membrane. Has a redundant role in promoting the expression of the calcium channel CACNA1S at the cell membrane (By similarity). Slows down the inactivation rate of the calcium channel CACNA1C.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8BZ71}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q8BZ71}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8BZ71}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8BZ71}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:Q8BZ71}. Note=Co-localizes with CACNA1S and CACNA1C on T-tubules. {ECO:0000250|UniProtKB:Q8BZ71}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Ryanodine receptor 1
- Peptidyl-prolyl cis-trans isomerase FKBP1A
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent L-type calcium channel subunit alpha-1F
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent T-type calcium channel subunit alpha-1H
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent calcium channel subunit alpha-2/delta-1
Sequence:
MTEKEVLESPKPSFPAETRQSGLQRLKQLLRKGSTGTKEMELPPEPQANGEAVGAGGGPIYYIYEEEEEEEEEEEEPPPEPPKLVNDKPHKFKDHFFKKPKFCDVCARMIVLNNKFGLRCKNCKTNIHEHCQSYVEMQRCFGKIPPGFHRAYSSPLYSNQQYACVKDLSAANRNDPVFETLRTGVIMANKERKKGQADKKNPVAAMMEEEPESARPEEGKPQDGNPEGDKKAEKKTPDDKHKQPGFQQSHYFVALYRFKALEKDDLDFPPGEKITVIDDSNEEWWRGKIGEKVGFFPPNFIIRVRAGERVHRVTRSFVGNREIGQITLKKDQIVVQKGDEAGGYVKVYTGRKVGLFPTDFLEEI
Protein: Dihydropteroate synthase (DHPS) (EC 2.5.1.15) (Dihydropteroate pyrophosphorylase) (P9WND1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
Interaction partners:
- GTP cyclohydrolase 1
- Dihydroneopterin aldolase
- Dihydrofolate synthase/folylpolyglutamate synthase
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
- ATP-dependent zinc metalloprotease FtsH
- Inactive dihydropteroate synthase 2
- Bifunctional aminodeoxychorismate lyase / D-amino acid transaminase
- Probable conserved secreted protein
- Dihydrofolate reductase
- Thymidylate synthase ThyA
Sequence:
MSPAPVQVMGVLNVTDDSFSDGGCYLDLDDAVKHGLAMAAAGAGIVDVGGESSRPGATRVDPAVETSRVIPVVKELAAQGITVSIDTMRADVARAALQNGAQMVNDVSGGRADPAMGPLLAEADVPWVLMHWRAVSADTPHVPVRYGNVVAEVRADLLASVADAVAAGVDPARLVLDPGLGFAKTAQHNWAILHALPELVATGIPVLVGASRKRFLGALLAGPDGVMRPTDGRDTATAVISALAALHGAWGVRVHDVRASVDAIKVVEAWMGAERIERDG
Protein: Protein DWD HYPERSENSITIVE TO UV-B 1 (Q8GYY7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate receptor of a CUL4-RING E3 ubiquitin-protein ligase (CRL4) complex involved in the negative regulation of cellular responses to ultraviolet-B (UV-B) illumination, likely in coordination with RUP1. Interacts with COP1 and probably prevents the formation of active UVR8-COP1 complex, thus avoiding UVR8-COP1-mediated positive regulation of UV-B responses.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- WD repeat-containing protein RUP1
- AT3g05090/T12H1_5
- Pre-mRNA-processing factor 19 homolog 2
- Protein ALTERED SEED GERMINATION 2
- WD repeat-containing protein RUP2
- E3 ubiquitin-protein ligase COP1
- Protein pleiotropic regulatory locus 1
- Protein RAE1
- Protein HEAT STRESS TOLERANT DWD 1
- Cullin-4
Sequence:
MATLTEIATLEEKYIELCKMHGILPNTAILSAFFEAEVKKSRNQRCIMNLYVDRVKYDDYLPLLELCNEINTSEVQGIDLFVRSACSLEDHYALPLIRSVNQKLRVVHLHDSFGKNFWQDVFFQGLSCKVLNVRSMHIHKLNIVGEFTQLHTLILDKNRIVGFGEDCFSCMPKLTYLSMCDTLVSDLWTSAAALLKLPSLKELRFQIWISCSDSSPLNSESSPSSSTKDDINTFIESDPPVEADMWDVAEQMDPSLPVEETLHSMDFSYKIPEQDDLDSHVSVSAGLNGEVLMREKVRRGKMPYQPKDVSPVDTFTRQFGNVGLKYISSKASPICSEKHYRMYMINSLPKLQVLDNLAIRKSDRDKAIETYSANFEDLPYKRKKESVVRVLENREKRSSKGKSQNSYKRSLCAAKMGSPASPLLHSLPFLSSRIQQEDDNSRLCPRQFEYHPLDPSLMVFGTLDGEVVVLNHESGKIFRYIPSNGSQSTILGLCWLKIYPSMVIAGSANGSLKLYDIQKASSTVTTSSHSTSGSVTFDEFDQLTSVHANSTDQLFLASGYSKDVALYDIGRGTRLQVFANMHQEHINVVKFSNHSPFLFATSSFDKDVKLWDLRQEPSRPCYTASSTKGNVMVCFSPDDRYLLASAVDNEVRQLLTVDGRLHLNFEIVPRVSSMNYTRSYYMNGNDYIISGSCDENVIRVCCAQTGRRLRDVTLEGNGSDFSMMYVQSLRGDPFRDFNMSVLAAYARSSSLSEIVKVNLLASRDSTAEESHGLRSYPSSSMGG
Protein: Pyridoxal phosphate homeostasis protein (PLP homeostasis protein) (Proline synthase co-transcribed bacterial homolog protein) (Pyridoxal phosphate-binding protein) (O94903)
Organism: Homo sapiens (Human)
Function: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6.
Interaction partners:
- Pyridoxal kinase
- Purine nucleoside phosphorylase LACC1
- Pyridoxine-5'-phosphate oxidase
- Erlin-2
Sequence:
MWRAGSMSAELGVGCALRAVNERVQQAVARRPRDLPAIQPRLVAVSKTKPADMVIEAYGHGQRTFGENYVQELLEKASNPKILSLCPEIKWHFIGHLQKQNVNKLMAVPNLFMLETVDSVKLADKVNSSWQRKGSPERLKVMVQINTSGEESKHGLPPSETIAIVEHINAKCPNLEFVGLMTIGSFGHDLSQGPNPDFQLLLSLREELCKKLNIPADQVELSMGMSADFQHAVEVGSTNVRIGSTIFGERDYSKKPTPDKCAADVKAPLEVAQEH
Protein: Integrator complex subunit 6 (Q9W485)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing. Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5. May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:39032490}.
Interaction partners:
- Integrator complex subunit 3
- Integrator complex subunit 11
- Integrator complex subunit 1
- Integrator complex subunit 4
- Integrator complex subunit 7
- Integrator complex subunit 2
- Integrator complex subunit 9
- Integrator complex subunit 5
- Integrator complex subunit 12
- Protein asunder
Sequence:
MTIILFLVDTSSSMCQKAYVNGVQKTYLDIAKGAVETFLKYRQRTQDCLGDRYMLLTFEEPPANVKAGWKENHATFMNELKNLQSHGLTSMGESLRNAFDLLNLNRMQSGIDTYGQGRCPFYLEPSVIIVITDGGRYSYRNGVHQEIILPLSNQIPGTKFTKEPFRWDQRLFSLVLRMPGNKIDERVDGKVPHDDSPIERMCEVTGGRSYRVRSHYVLNQCIESLVQKVQPGVVLQFEPMLPKEATSATAGEAAGASTISGMGISSTSGAGPAPDIVFQPVKKMIYVQKHITQKTFPIGYWPLPEPYWPDSKAITLPPRDAHPKLKVLTPAVDEPQLVRSFPVDKYEIEGCPLTLQILNKREMNKCWQVIVTNGMHGFELPFGYLKAAPNFSQVHLYVLAYNYPALLPILHDLIHKYNMSPPSDLMYKFNAYVRSIPPYYCPFLRKALVNINVPYQLLQFLLPENVDNYLSPTIANQLKHIKNTAKQDQENLCMKVYKQLKQPKPPYRQVETGKLFTGAPLRRDLVRHPLLRDIFSKLHGEIDPVENYTIVVPQPTHQSSAKSHRNPFDIPRRDLVEEIAKMRETLLRPVSLVAKDSGHCLPIAEMGNYQEYLKNKDNPLREIEPTNVRQHMFGNPYKKDKHMVMVDEADLSDVAPMKSPNGNGPGGAPPGSPSGSGSPTGPGPSSPGSSPGGGSGPGMPGMPGMGGGMSGLMLGAGGSGGSSKKLDGTSRGRKRKAGPLPRSFEFRRSSTDSRSSSSGSESSTTGSAPGSPIPGATSSISGCDSAMGADGGPSSSCFDEDSNSNSSFVSSTSEASASDSGMSNSHLDPLRISFVFIEEETSDQDTPLNGYVHNFINGISDDAETGETEAVPGGASLPGASSANEPSSIGASPAVSATPATSVIPASNGSEVCSAVAAGSSSSISSSASSPGVLYVPLNGLTTHAAYSSNLGGPSSPLDNLSSLGGAAGGGGSGLLGVSKPGSLPLANGYGHGHSSAISPPSPLSLVPLSPLGTSTPAASSSGLSSSSAYFSHNDINDASEISRILQTCHNGTSSGSSVGAGASNSNLNGNGSTESGGGVSSDDHASLGGNSFDALKRTAGTAGSTAAGNPHYYWASGLNHHNNNNSSAAGAASGSTLSNNHNHRGHNNSSPNKLEVKINSSCGSSPTHNNGGMGSPGQSLPLIFTEEQREAARLHNVELRLQIFRDIRRPGRDYSQLLEHLNLVKGDQDMQSDFVDMCIVESLRFRRHRMASSIQEWWDRKQQLTAVGTNEATPSAEQAVAKS