wanglab/gogpt-training-data huggingface dataset:
Protein: Ras-related protein Rab5A (OsRab5A) (Protein GLUTELIN PRECURSOR 4) (Protein GLUTELIN PRECURSOR ACCUMULATION 1) (Q0ILQ6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Plays an important role in intracellular trafficking of seed storage proteins to the protein storage vacuoles (PSVs). Participates in the transport of the proglutelins from the Golgi apparatus to the PSVs in endosperm. Functions cooperatively with VPS9A to regulate post-Golgi dense vesicle-mediated transport of storage proteins to the type II protein bodies (PBII) protein storage vacuoles in developing endosperm. Involved in the maintenance of the general structural organization of the endomembrane system in developing endosperm. Binds GTP in vitro. Forms a quaternary complex with the two glutelin zipcode RNA-binding proteins RBP-L and RBP-P, and the membrane trafficking factor NSF. This quaternay complex carries glutelin mRNAs for active transport on endosomes to the cortical endoplasmic reticulum membrane, and enables endosome-mediated glutelin mRNA transport in endosperm cells.
Subcellular location: Prevacuolar compartment membrane {ECO:0000269|PubMed:21105928, ECO:0000269|PubMed:21825104}; Lipid-anchor {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:21105928, ECO:0000269|PubMed:21825104}; Lipid-anchor {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:21825104}; Lipid-anchor {ECO:0000305}. Protein storage vacuole membrane {ECO:0000269|PubMed:21825104}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- phosphatidylinositol 3-kinase
- Vacuolar protein sorting-associated protein 9A
- phosphatidylinositol 3-kinase
- Os06g0687100 protein
- Os03g0666500 protein
- Guanosine nucleotide diphosphate dissociation inhibitor
- Guanosine nucleotide diphosphate dissociation inhibitor
- Guanosine nucleotide diphosphate dissociation inhibitor
- Guanosine nucleotide diphosphate dissociation inhibitor
- Os03g0842700 protein
Sequence:
MAANPGNKIRNAKLVLLGDVGTGKSSLVLRFVKGQFVEFQESTIGAAFFSQTLAVNDETVKFEIWDTAGQERYHSLAPMYYRGAAAAIVVYDITNAASFTRAKKWVQELQAQGNPNTIMALAGNKADMVEARQVPAEEAKTYAQENGLFFMETSAKTAINVNDVFHEIAKRLLQGQQAQDTPAGMVLNQRPAERMVSSSSCCS
Protein: 7-dehydrocholesterol reductase (7-DHC reductase) (EC 1.3.1.21) (Cholesterol-5,6-epoxide hydrolase subunit DHCR7) (EC 3.3.2.11) (Sterol Delta(7)-reductase) (O88455)
Organism: Mus musculus (Mouse)
Function: 7-dehydrocholesterol reductase of the cholesterol biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien-3beta-ol, two intermediates in that pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UBM7}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lathosterol oxidase
- Delta
- Squalene monooxygenase
- Lanosterol 14-alpha demethylase
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Cholesterol 25-hydroxylase
- Lanosterol synthase
- Sterol O-acyltransferase 1
- Sterol O-acyltransferase 2
Sequence:
MASKSQHNAPKVKSPNGKAGSQGQWGRAWEVDWFSLASIIFLLLFAPFIVYYFIMACDQYSCSLTAPALDIATGHASLADIWAKTPPVTAKAAQLYALWVSFQVLLYSWLPDFCHRFLPGYVGGVQEGAITPAGVVNKYEVNGLQAWLITHILWFVNAYLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMIKGYLFPTSAEDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQQELYGHVTNSMILVNVLQAIYVLDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPNALGILLLGLVGYYIFRMTNHQKDLFRRTDGRCLIWGKKPKAIECSYTSADGLKHHSKLLVSGFWGVARHFNYTGDLMGSLAYCLACGGGHLLPYFYIIYMTILLTHRCLRDEHRCANKYGRDWERYTAAVPYRLLPGIF
Protein: Necdin-like protein isoform 4 (A0A0S2Z442)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSEQSKDLSDPNFAAEAPNSEVHSSPGVSEGVPPSATLAEPQSPPLGPTAAPQAAPPPQAPNDEGDPKALQQAAEEGRAHQALEEALHLRGRAEAHH
Protein: adenylate cyclase (EC 4.6.1.1) (X2JAA1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNKKNTYKTPYRERFRRCNLEYTNERLWEQSYLKARCKELHLEEEYMKYKIRLMISSLTVFVPMLILLIVALQVIIWSFTEYTKYIYINAIFDLGSLILVTGLLSINFFEDFVIRHRWVMTFTSTLSAYVVVLGDIAFNTYYYYKSNWPLNTLYDVFVLCMIYMFLPIPSSKAAALLAISVSLTYVIYFIHFMAFNEHNVAKYVHGLDIVSIDFFHYLGFNMMGIFFRIMNDTMVRSSFLDRYQFITEEIWLRQARRQESLLLDSILPPQIAKPIQKSIKEKIIQPDNDFYHLGTSRTAENFMSIQIHNDVSILYADLVNYTQLTTTLTVEKLVKVLHDLYARFDLAALSFKVQRIKFLGDCYYCVAGLGESDPDHATMAVSLGISMIANIKEV
Protein: Gastrin [Cleaved into: Gastrin-71 (Gastrin component I); Gastrin-52 (G52); Big gastrin (Gastrin component II) (Gastrin-34) (G34); Gastrin (Gastrin component III) (Gastrin-17) (G17); Gastrin-14 (G14); Gastrin-6 (G6)] (P01350)
Organism: Homo sapiens (Human)
Function: Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine.
Subcellular location: Secreted.
Interaction partners:
- Gastrin/cholecystokinin type B receptor
- Cholecystokinin
- Somatostatin
- Cholecystokinin receptor type A
- Gastrin-releasing peptide
- Pro-glucagon
- Secretin
- Pancreatic polypeptide prohormone
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MQRLCVYVLIFALALAAFSEASWKPRSQQPDAPLGTGANRDLELPWLEQQGPASHHRRQLGPQGPPHLVADPSKKQGPWLEEEEEAYGWMDFGRRSAEDEN
Protein: Large ribosomal subunit protein P3 (60S acidic ribosomal protein P3) (P1/P2-like) (P3A) (O24413)
Organism: Zea mays (Maize)
Function: Plays an important role in the elongation step of protein synthesis.
Interaction partners:
- 60S ribosomal protein L5-1
- Large ribosomal subunit protein eL39
- 60S ribosomal protein L3-1
- Putative inactive leucine-rich repeat receptor-like protein kinase
- 60S ribosomal protein L27a-3
- 60S ribosomal protein L27a-2
- 60S ribosomal protein L13a-1
- 60S ribosomal protein L13a-1
- Ribosomal protein L37
- Large ribosomal subunit protein P1
Sequence:
MGVYTFVCRNNGGEWTAKQHSGEIEASAATPYELQRRLVAAASAADSRYGVQSSFSMVTPSSAVFQVIVGAVGGGAMMVSGGGGGGAAASGGAAAEAPKEEKKEEEKEESDDDMGFSLFD
Protein: Ankyrin repeat and protein kinase domain-containing protein 1 (EC 2.7.11.1) (Q8BZ25)
Organism: Mus musculus (Mouse)
Interaction partners:
- Tetratricopeptide repeat protein 12
- D
- Catechol O-methyltransferase
- D
Sequence:
MVPHRARRLLNPMAVGPLAQQLGSLTVFTRDDFEEEWHLVASGGFSKVFQARHKRWRTQYAIKCSPCLQKETTSSEVTCLFEEAVKMEKIKFQHIVSIYGVCKQPLGIVMEFMASGSLEKTLPTHSLCWPLKLRIIHETSLAMNFLHSIKPPLLHLDLKPGNILLDNNMHVKISDFGLSKWMEQSTQKQYIERSALRGTLSYIPPEMFLENNKAPGPEYDVYSFAIVIWEILTQKKPYAGLNMMTIIIRVAAGMRPSLQDVSDEWPEEVHQMVNLMKRCWDQDPKKRPCFLNVAVETDMLLSLFQSPMTDPGCEALTQKVSCKPSLSQPHKVSKEVNQEIADSVSSDSLKWILQLSDSKSLVASDVYENRVTPLHFLVAGGSLEQVRLLLSHDVDVDCQTASGYTPLLIATQDQQPDLCALLLAHGADTNLADEDGWAPLHFAAQNGDDHTARLLLDHGALVNAREHEGWTPLHLAAQNNFENVARLLVSRQADLSPHEAEGKTPLHVAAYFGHIGLVKLLSGQGAELDAQQRNLRTPLHLAVERGKVRAIQHLLKCGALPDALDHSGYSPLHIAAARGKDLIFKMLLRYGASLELRTQQGWTPLHLATYKGHLEIIHQLAKSHVDLDALGSMQWTPLHLAAFQGEEGVMLALLQCGANPNAAEQSGWTPLHLAVHKGTFLGITHLLEYGADIHACNKVGWTPAHLAALKGNTAILKVLVKAAAQVDVKGGVSCTPLQLAIHSPK
Protein: Glyoxylate carboligase (EC 4.1.1.47) (Tartronate-semialdehyde synthase) (P0AEP7)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the condensation of two molecules of glyoxylate to give 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
Interaction partners:
- 2-hydroxy-3-oxopropionate reductase
- Hydroxypyruvate isomerase
- 2-hydroxy-3-oxopropionate reductase
- Malate synthase G
- Ureidoglycolate lyase
- Glycolate oxidase iron-sulfur subunit
- Isocitrate lyase
- Glyoxylate/hydroxypyruvate reductase B
- Glyoxylate/hydroxypyruvate reductase A
- Glycolate oxidase subunit GlcE
Sequence:
MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGNIGVCLGTSGPAGTDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAEIEFDPDMYEPLPVYKPAASRMQIEKAVEMLIQAERPVIVAGGGVINADAAALLQQFAELTSVPVIPTLMGWGCIPDDHELMAGMVGLQTAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTEGRKIVHIDIEPTQIGRVLCPDLGIVSDAKAALTLLVEVAQEMQKAGRLPCRKEWVADCQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPKRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFDMDYCVQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVPVVVEVILERVTNISMGSELDNVMEFEDIADNAADAPTETCFMHYE
Protein: Large ribosomal subunit protein bL17 (50S ribosomal protein L17) (P0AG44)
Organism: Escherichia coli (strain K12)
Function: Requires L15 for assembly into the 50S subunit.
Interaction partners:
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS13
- Elongation factor Tu 1
- Large ribosomal subunit protein uL6
- GTP pyrophosphokinase
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein bL33
- DNA-directed RNA polymerase subunit alpha
- Large ribosomal subunit protein uL14
Sequence:
MRHRKSGRQLNRNSSHRQAMFRNMAGSLVRHEIIKTTLPKAKELRRVVEPLITLAKTDSVANRRLAFARTRDNEIVAKLFNELGPRFASRAGGYTRILKCGFRAGDNAPMAYIELVDRSEKAEAAAE
Protein: Insulin-like growth factor 1 (Insulin-like growth factor I precursor) (Insulin-like growth factor IL) (Q90VV9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU000406}.
Interaction partners:
- Insulin
- Tyrosine-protein kinase receptor.
- Tyrosine-protein kinase receptor.
- Insulin-like growth factor-binding protein 3
- Tyrosine-protein kinase receptor
- Tyrosine-protein kinase receptor.
- Insulin
- Insulin-like growth factor-binding protein 1
- Insulin-like growth factor-binding protein 2-A
- Appetite-regulating hormone isoform X1
Sequence:
MSSGHFFQGHWCDVFKCTMRCLPSTHTLSLVLCVLALTPATLEAGPETLCGAELVDTLQFVCGDRGFYFSKPTGYGPSSRRSHNRGIVDECCFQSCELRRLEMYCAPVKTGKSPRSLRAQRHTDIPRTPKKPISGHSHSSCKEVHQKNSSRGNTGGRNYRM
Protein: Potassium voltage-gated channel subfamily C member 3a isoform X3 (Potassium voltage-gated channel, Shaw-related subfamily, member 3a) (Voltage-gated potassium channel Kv3.3a variant 1) (E1AZA4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- FAU ubiquitin-like and ribosomal protein S30 fusion a ubiquitously expressed
- FAU ubiquitin-like and ribosomal protein S30 fusion b
- Fructose-bisphosphate aldolase C-A
- Sodium channel protein
Sequence:
MLSSVCVSSFKGRKGGNKSSNKACYSADMTCPSDSEKIVINCGGIRHETYRSTLKTLPGTRLSWLTEPDAFSNFDYDPKSDEFFFDRHPNTFAFILNYYRTGKLHCPSDVCGPLFEEELAFWGIDETDVEACCWMNYRQHRDAEEALDSFETPEPDPPEDDPALTGGADGDLKRLCLQEDGRNPSRWSTWQPWVWALFEDPYSSKYARYVAFGSLLFILISISTFCLETHEAFNTIYNKTENVTVGNVTREEVVFEVVTDNWLTYVEGVCVVWFTIEVFTRVIFCPDKAEFFKSSLNIIDFVAILPFYLEMALSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGADPDDPTASAHTAFKNIPIGFWWAVVTMTTLGYGDMYPETWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKNKHIPRAPQPGSPNYCKPDALAMATASPHRIMGNVLGSMVVSGSMAGDCPLAQEEIIEINRADSKQNGDAANAALANEDCPTIDQVLGPDDRSPATGGLGTGTGRERYPHDRACFLLSTGEFRTTDSNVRKDAAGARPVSPGEEWFKPEGPLLQQDLNANSASSWIKP
Protein: Maternal DNA replication licensing factor mcm3 (EC 3.6.4.12) (Maternal minichromosome maintenance protein 3) (mMCM3) (xMCM3) (P1 homolog) (XRLF subunit beta) (p100) (P49739)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. The existence of maternal and zygotic forms of mcm3 and mcm6 suggests that specific forms of mcm2-7 complexes may be used during different stages of development.
Subcellular location: Nucleus {ECO:0000269|PubMed:7758114, ECO:0000269|PubMed:7760937, ECO:0000269|PubMed:7760938, ECO:0000269|PubMed:8816774, ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}. Chromosome {ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}.
Interaction partners:
Sequence:
MDYGGGFEDHELREAQREYLDFLDDDQDQGLYHGKVRDMIGSNEHRLIVNLNDVRRKNDKRANLMLNDAFAETIAFQRALKDLVASIDATYAKQFEEFSVGFEGSFGSKHVSPRTLTASLLGSLVCVEGIVTKCSLVRPKVMRSVHYCPATKKTLERKYSDLTSLEAFPSSSIYPTKDEENNPLETEYGLSTYKDHQTLSIQEMPEKAPAGQLPRSVDIIADDDLVDKCKPGDRVQIVGIYRCLPSKQGGFTSGTFRTILLANNIKLMSKEIAPTFSADDVAKIKKFCKAHSKDIFEHLSKSLAPSIHGHEYIKKAILCMLLGGNEKVLENGTRIRGDINVLLIGDPSVAKSQLLRYVLHTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDMDRTAIHEVMEQGRVTIAKAGIQARLNARCSVLAAANPVYGRYDQYRTPMENIGLQDSLLSRFDLLFIVLDKMDADNDQEIADHVLRMHRYRTPGEQDGYALPLGCSVEIFATDDPNASDVTDQELQIYEKHDNLLHGPRKNKSKIVSMQFIRKYIHVAKLIKPVLTSEAADYISQEYAKIRNHDQINNDSARTMPVTARALETMIRLSTAHAKVRMSKTIERQDAETALELVQFAYFKKVLAKEKKKTDKDLHDENLSQDTLSQESVRKSSRRAGKIADSQDDSMDPYSFSEQDSSLNENLSQSLRPQRKKAESQDGKRSLSQNRTKEFKAALLKAFKSSRSQSVAVSQLLELINKGNPEPFERSEVKEALDNMQNDNQVMVSEDVVFLI
Protein: C2 domain-containing protein (Q385X5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDRPTKEATSVPSAQEVRLHVDILRGRNYPQTEDDPCACSTYARLILYDSLLKETIGSVYESPLQEGSNTPFYNTSTEYELPPSTEMVVLVVQVVETTRRPEPYIMFYGSCRISTVKSGKNEETVVLIHTDPVTQPEEAEAEVKQVVGDGLPCPNLSFRLHVKRRRPGEVNAEDHSDAVLSSAPVLDGSYPIIPKNSQYVWFNLASDRKWSEAFTNALVSEWRKQAMVSSAEGALPDIGESYAKVQGASRKKEPSKREIYVPTSINTVADIIVTQWNCCRSHEVLSWLRLSGEAFSRGERLCSFSREDVMNFRRKRKEQIYLLQDLAISSLLLVGESELRDTIDHLWIHFAIGVDHDPSRGTALPYEARKRMKEAGFEDADKVALHSSFLNFLVPSLAQDQCDEMVTADLNAAAREPDLANIVNKFASSHAGTLQTSVSEMKFTAALLECVGAMLDTLTEVEVSRALKMFKPCVISAHQRLKSGAKEKLRNAIASYGGQRDKFTYRPGGGIKIDHLDRLGRRKKEIHFR
Protein: Structural DNA-binding protein p10 (p10) (Q89769)
Organism: African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV)
Function: May play a role in genome packaging through direct interaction with viral DNA. Binds to ssDNA and dsDNA with the same apparent affinity in vitro.
Subcellular location: Virion {ECO:0000269|PubMed:30185597}. Note=Found in association with the viral nucleoid. {ECO:0000269|PubMed:30185597}.
Interaction partners:
Sequence:
MPTKAGTKSTANKKTTKGSSKSGSSRGHTGKTHASSSMHSGMLYKDMVNIARSRGIPIYQNGSRLTKSELEKKIKRSK
Protein: Cell division control protein 31 (Nuclear pore protein CDC31) (Nucleoporin CDC31) (P06704)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the spindle pole body (SPB) half-bridge. At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication. Also involved in connection with the protein kinase KIC1 in the maintenance of cell morphology and integrity. May play a role in vesicle-mediated transport, in a VPS13-dependent manner.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:10684247}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:8188750}. Note=Spindle pole body, SPB half- bridge (PubMed:8188750). Interacts with the nuclear pore complex (NPCs) at the nucleus envelope (PubMed:10684247). {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:8188750}.
Interaction partners:
- SAGA complex subunit SUS1
- Protein SFI1
- Nuclear mRNA export protein SAC3
- Cell division control protein KAR1
- 26S proteasome complex subunit SEM1
- Nuclear mRNA export protein THP1
- Nucleoporin NUP1
- DNA repair protein RAD4
- Spindle pole body assembly component MPS3
- Spindle pole body component 110
Sequence:
MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKREILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTDS
Protein: Nucleolar GTP-binding protein 2 (Q7JXU4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU364023}.
Interaction partners:
- Guanine nucleotide-binding protein-like 3 homolog
- Nucleolar GTP-binding protein 1
- Ribosome biogenesis protein NSA2 homolog
- Probable ribosome biogenesis protein RLP24
- Ribosome biogenesis protein NOP53
- Ribosome production factor 2 homolog
- Uncharacterized protein, isoform A
- RRM domain-containing protein
- Ribosomal L1 domain-containing protein CG13096
- Protein SDA1 homolog
Sequence:
MPKVRSTPGKPRTQGFNHSNHSMNPERPKSGLKGVAHPRTKGTIKRLQMYRNFKAKRDRTGKILTPAPFQGRLPAGTMARVEPTPKWFSNSRVISQTALQKFQDEIGKAVKDPYQVIMKPSQLPVTLLNEAAKYKRVHLLDTESFDSTFGPKKQRKRVSLKVRDLEDLSKAADDQADKYDSAKDLDLIREDTGEKKAVRDWVFGAGQSKRIWNELHKVVDASDVLLQVLDARDPMGTRSKYIEEFLRKEKPHKHLFFILNKVDLVPVWVTQRWVAILSAEYPTIAFHASLQHPFGKGALINLFRQLGKLHLDKKQISVGFIGYPNVGKSSVINALRSKKVCKVAPIAGETKVWQYITLMKRIFLIDCPGVVYPTAETDTEKVLKGVVRVELVTNPEDYVDSLLKRVRPEYISKNYKIEHWNTSTHFLEQLAQKTGKLLKGGEPDVTVTARMVLNDWQRGKLPFYVPPEGFAVPKSQEGKEEEVVAEDPNEDAKSEAPTFVSESVKKAREFKQIQDFRKIRVGLEYEQEDVKDLDHIDLELLEQQKAERAAKKKARIHNLGEEDEESSDGADEFYSEDEYNEDLQRVVHKKAKSKKPQQLAITSSGKFRVAKIQPGDSDGAGSSDDDGPSTSKAPRLTAKQKRSLERSQKRKKIGSNFYETTNVKNRNRNKKKDA
Protein: DnaJ heat shock protein family (Hsp40) member C7 (A0A6I8PS32)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XKREAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDPNNIFKAFFGGPGGFSFEANYQPLFS
Protein: Notch-regulated ankyrin repeat-containing protein (Q7Z6K4)
Organism: Homo sapiens (Human)
Function: Downstream effector of Notch signaling. Involved in the regulation of liver cancer cells self-renewal. Involved in angiogenesis acting downstream of Notch at branch points to regulate vascular density. Proposed to integrate endothelial Notch and Wnt signaling to control stalk cell proliferation and to stablilize new endothelial connections during angiogenesis. During somitogenesis involved in maintenance of proper somite segmentation and proper numbers of somites and vertebrae. Required for proper anterior-posterior somite patterning. Proposed to function in a negative feedback loop to destabilize Notch 1 intracellular domain (NICD) and down-regulate the Notch signal, preventing expansion of the Notch signal into the anterior somite domain (By similarity).
Interaction partners:
- Neurogenic locus notch homolog protein 1
- Recombining binding protein suppressor of hairless
- Hairy/enhancer-of-split related with YRPW motif protein 1
- E3 ubiquitin-protein ligase DTX1
- Protein jagged-1
- Transcription factor HES-5
- Delta-like protein 4
- Mastermind-like protein 1
- Neurogenic locus notch homolog protein 3
Sequence:
MSQAELSTCSAPQTQRIFQEAVRKGNTQELQSLLQNMTNCEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAFGGHQDIVLYLITKAKYAASGR
Protein: Carboxypeptidase M (CPM) (EC 3.4.17.12) (P14384)
Organism: Homo sapiens (Human)
Function: Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12457462}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12457462}.
Interaction partners:
- B1 bradykinin receptor
Sequence:
MDFPCLWLGLLLPLVAALDFNYHRQEGMEAFLKTVAQNYSSVTHLHSIGKSVKGRNLWVLVVGRFPKEHRIGIPEFKYVANMHGDETVGRELLLHLIDYLVTSDGKDPEITNLINSTRIHIMPSMNPDGFEAVKKPDCYYSIGRENYNQYDLNRNFPDAFEYNNVSRQPETVAVMKWLKTETFVLSANLHGGALVASYPFDNGVQATGALYSRSLTPDDDVFQYLAHTYASRNPNMKKGDECKNKMNFPNGVTNGYSWYPLQGGMQDYNYIWAQCFEITLELSCCKYPREEKLPSFWNNNKASLIEYIKQVHLGVKGQVFDQNGNPLPNVIVEVQDRKHICPYRTNKYGEYYLLLLPGSYIINVTVPGHDPHITKVIIPEKSQNFSALKKDILLPFQGQLDSIPVSNPSCPMIPLYRNLPDHSAATKPSLFLFLVSLLHIFFK
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2 (G protein subunit beta-2) (Transducin beta chain 2) (P54313)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62879}. Cell membrane {ECO:0000250|UniProtKB:P62879}.
Interaction partners:
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
- Phosducin-like protein
Sequence:
MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYAFTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Protein: Immunoglobulin heavy variable 3-33 (Ig heavy chain V-III region HIL) (Ig heavy chain V-III region KOL) (P01772)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MEFGLSWVFLVALLRGVQCQVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVIWYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAR
Protein: Prefoldin subunit 5 (H3BPF6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAQSINITELNLPQLEMLKNQLDQEVEFLSTSIAQLKVVQTKYVEAKDCLNVLNKSNEDGISLCRPGWSAMMYVPGKLHDVEHVLIDVGTGYYVEKTAEDAKDFFKRKIDFLTKQMEKIQPALQEKHAMKQAVMEMMSQKIQQLTALGAAQATAKA
Protein: Secreted frizzled-related protein 5 (sFRP-5) (Q9XSC1)
Organism: Bos taurus (Bovine)
Function: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP5 may be involved in determining the polarity of photoreceptor, and perhaps other, cells in the retina. Inhibits Wnt8 signaling, in vitro.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt-2
Sequence:
MRAAAGGARAAVLALLLGALHGAPARGEEYDYYGWQTEPLHGRSYSKPPQCLDIPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDRPIYPCRSLCEAVRAGCAPLMEAYGFPWPEMLHCHKFPLDNDLCIAVQFGHLPATAPPVTKICAQCEMEHSADGLMEQMCSSDFVVKMRIKEIKIENGDRKLIGAQKKKKLLKSGPLKRKDTKRLVLHMKNSAGCPCPQLDSLAGSFLVMGRKVDGQLLLMAVYRWDKKNKEMKFAVKFMFSYPCSLYYPFFYGAAEPH