wanglab/gogpt-training-data huggingface dataset:
Protein: DNA helicase (EC 3.6.4.12) (E9PU01)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone deacetylase 1
- Histone deacetylase 2
- GATA zinc finger domain containing 2A
- Metastasis-associated gene family, member 2
- DNA helicase
- Histone-binding protein RBBP7
- GATA zinc finger domain containing 2B
- RB-binding protein 4, chromatin-remodeling factor.
- Metastasis-associated protein MTA1
- Histone deacetylase 1
Sequence:
MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEDDPEEDLSEAETPKLKKKKKPKKPRDPKIPKSKRQKKERLLLCRQLGDSSGEGPEFVEEDEEAALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLEDWGMEDIDHVFSEEDYRTLTNYKAFSQFVRPLIAAKNPKIAVSKMMMVLGAKWREFSTNNPFKGSSGASVAAAAAAAVAVVESMVTATEVAPPPPPVEVPIRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPKKVAPLKIKLGGFGSKRKRSSSEDDDLDVESDFDDASINSYSVSDGSTSRSSRSRKKLRTAKKKKKGEEEVTAVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHMVCLDPDMEKAPEGKWSCPHCEKEGIQWEAKEDNSEGEEILEEVGGDPEEEDDHHMEFCRVCKDGGELLCCDTCPSSYHIHCLNPPLPEIPNGEWLCPRCTCPALKGKVQKILIWKWGQPPSPTPVPRPPDADPNTPSPKPLEGRPERQFFVKWQGMSYWHCSWVSELQLELHCQVMFRNYQRKNDMDEPPSGDFGGDEEKSRKRKNKDPKFAEMEERFYRYGIKPEWMMIHRILNHSVDKKGHVHYLIKWRDLPYDQASWESEDVEIQDYDLFKQSYWNHRELMRGEEGRPGKKLKKVKLRKLERPPETPTVDPTVKYERQPEYLDATGGTLHPYQMEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRRLKADVFKNMPSKTELIVRVELSPMQKKYYKYILTRNFEALNARGGGNQVSLLNVVMDLKKCCNHPYLFPVAAMEAPKMPNGMYDGSALIRASGKLLLLQKMLKNLKEGGHRVLIFSQMTKMLDLLEDFLEHEGYKYERIDGGITGNMRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKKKMMLTHLVVRPGLGSKTGSMSKQELDDILKFGTEELFKDEATDGGGDNKEGEDSSVIHYDDKAIERLLDRNQDETEDTELQGMNEYLSSFKVAQYVVREEEMGEEEEVEREIIKQEESVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDGSQEDRDWQDDQSDNQSDYSVASEEGDEDFDERSEAPRRPSRKGLRNDKDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRYGMPPQDAFTTQWLVRDLRGKSEKEFKAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLIRKKVQEFEHVNGRWSMPELAEVEENKKMSQPGSPSPKTPTPSTPGDTQPNTPAPVPPAEDGIKIEENSLKEEESTEGEKEVKPTAPEVTVECAQPPAPAPAPASGPGPTPGPAPAPEDDKAPAEPPEGEEKVEKAEVKERAEEPMETESKGTTEVEKAEEKSAVDLTPIVVEDKEEKKEEEEKKEVLLQNGETPKDLSDEKQKKNLKQRFMFNIADGGFTELHSLWQNEERAATVTKKTYEIWHRRHDYWLLAGIINHGYARWQDIQNDPRYAILNEPFKGEMNRGNFLEIKNKFLARRFKLLEQALVIEEQLRRAAYLNMSEDPSHPSMALNTRFAEVECLAESHQHLSKESMAGNKPANAVLHKVLKQLEELLSDMKADVTRLPATIARIPPVAVRLQMSERNILSRLANRAPEPPPQQVAQQQ
Protein: Ferredoxin-2, mitochondrial (Adrenodoxin-like protein) (Ferredoxin-1-like protein) (Q9CPW2)
Organism: Mus musculus (Mouse)
Function: Electron donor, of the core iron-sulfur cluster (ISC) assembly complex, that acts to reduce the persulfide into sulfide during [2Fe-2S] clusters assembly on the scaffolding protein ISCU (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9H1K1}. Mitochondrion matrix {ECO:0000250|UniProtKB:P10109}.
Interaction partners:
- Iron-sulfur cluster assembly enzyme ISCU
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Cysteine desulfurase
- LYR motif-containing protein 4
- Frataxin, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 4
Sequence:
MAASMARGVSARVLLRAAGGSWGPRAGHAAVTSRTFGTTGERRAGEEAADSPELPRDVVNVVFVDRSGKRIPVRGKVGDNVLYLAQRHGVDLEGACEASLACSTCHVYVSEAHLDLLPPPEEREDDMLDMAPLLQENSRLGCQIVLTPELEGVEFALPKITRNFYVDGHIPKPH
Protein: Vascular endothelial growth factor A, long form (L-VEGF) (Vascular permeability factor) (VPF) [Cleaved into: N-VEGF; VEGFA] (P15692)
Organism: Homo sapiens (Human)
Function: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity). Also binds the DEAR/FBXW7-AS1 receptor.
Subcellular location: [N-VEGF]: Cytoplasm {ECO:0000269|PubMed:15896327}. Nucleus {ECO:0000269|PubMed:15896327, ECO:0000269|PubMed:35455969}. Note=Cytoplasmic in normoxic conditions and localizes to the nucleus under hypoxic conditions. {ECO:0000269|PubMed:15896327, ECO:0000269|PubMed:35455969}.; SUBCELLULAR LOCATION: [VEGFA]: Secreted {ECO:0000269|PubMed:11563986, ECO:0000269|PubMed:11731620, ECO:0000269|PubMed:15896327}.; SUBCELLULAR LOCATION: [Isoform L-VEGF189]: Endoplasmic reticulum {ECO:0000269|PubMed:11731620}. Golgi apparatus {ECO:0000269|PubMed:11731620}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:11563986}.; SUBCELLULAR LOCATION: [Isoform VEGF121]: Secreted {ECO:0000269|PubMed:15896327}.; SUBCELLULAR LOCATION: [Isoform VEGF165]: Secreted {ECO:0000269|PubMed:15896327}.; SUBCELLULAR LOCATION: [Isoform VEGF189]: Secreted. Note=Cell-associated after secretion and is bound avidly by heparin and the extracellular matrix, although it may be released as a soluble form by heparin, heparinase or plasmin.
Interaction partners:
Sequence:
MTDRQTDTAPSPSYHLLPGRRRTVDAAASRGQGPEPAPGGGVEGVGARGVALKLFVQLLGCSRFGGAVVRAGEAEPSGAARSASSGREEPQPEEGEEEEEKEEERGPQWRLGARKPGSWTGEAAVCADSAPAARAPQALARASGRGGRVARRGAEESGPPHSPSRRGSASRAGPGRASETMNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR
Protein: Protocadherin beta-14 (PCDH-beta-14) (Q9Y5E9)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Protocadherin beta-16
Sequence:
MEIRGALDLRKRQVLIFLVLLGLSRAGTESAHYSVAEETEIGSFVANLARDLGLGVEELSSREARVVSDDNKKYLHLDLLTGNLLLNEKLDRDELCGSTEPCVLHFQVVLENPLQFFRFELCVKDINDHSPTFLDKEILIKISEGTTVGATFLMESAQDLDVGSNSLQNYTISPNSHFYIKIPDSSDRKIYPELVLDRALDYEQEAELRLTLTAVDGGSPPKSGTTLVLIKVLDINDNAPEFPQSLYEVQVPEDRPLGSWIATISAKDLDAGNYGKISYTFFHASEDIRKTFEINPISGEVNLRSPLDFEVIQSYTINIQATDGGGLSGKCTLLVKVMDINDNPPEVTISSITKRIPENASETLVALFSILDQDSGDNGRMICSIQDNLPFFLKPTFKNFFTLVSEKALDRESQAEYNITITVTDLGTPRLKTEYNITVLLSDVNDNAPTFTQTSYTLFVRENNSPALHIGSVSATDRDSGTNAQVNYSLLPPQDRHLPLASLVSINADNGHLFALRSLDYEALQEFEFRVGATDRGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLPLPEAAPAQAQADSLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAASVGRCSVPEGPFPGHLVDVSGTGTLSQSYQYEVCLTGGSGTNEFKFLKPIIPNFQVHDTGRNMGEIENFRNSFGLNIQ
Protein: Receptor-like protein 51 (AtRLP51) (Protein PUTATIVE DEVELOPMENTAL ORTHOLOG 1) (AtPDO1) (Protein SUPPRESSOR OF NPR1-1, CONSTITUTIVE 2) (Q9SN38)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in plant defense. Required for basal resistance against P.syringae pv. tomato DC3000.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20841424}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Negative regulator of systemic acquired resistance SNI1
- Protein SUPPRESSOR OF NPR1-1 CONSTITUTIVE 4
- SIT4 phosphatase-associated family protein
- At1g07990/T6D22_5
- SIT4 phosphatase-associated family protein
- SIT4 phosphatase-associated family protein
- Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1
Sequence:
MKPPSLPLLLLLLHLSATISAAPSLSPTPSPTTSPIPPHKPSSSSSPLDPKQLKALESLNIPTVKDPCNHRPTTKSTSSSVVTCDTSSPFRLVTSISFTNCSTDLSISTTALRALSPSLTSLSFLNCPSLSPPPRLPDSLHSFTAVSSFLRRRNGLSGVFLARLVNLTDLTVSSVPVSTSGLFVILGNMHEIVSLTISHANLSGNIPKSFHSNLTFIDLSDNLLKGSIPTSITLLSNLKSLNLSKNTISGDIPDSIGDLISLKNLSLSSNKLSGPIPDSISSIPELTHLDLSGNQLNGTIPRFISKMKYLTHLNLANNAFHGVLPFNASFIKNLEVFKIGGNSDLCYNHSVLSSKMKLGIAQCDKHGLPLSPPPQKEDSNSDYDYGNEDDTSEKKKEEHHGPNKVVLGVAIGLSSLVFLIIFMILLAKWCG
Protein: Probable urea active transporter 3 (Q9URY6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in active transport of urea.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane; Multi-pass membrane protein.
Interaction partners:
- Thiamine repressible genes regulatory protein thi5
- LIN1-like protein
Sequence:
MTETVLNQGYGYGIVIGLGFAFAIVMILVTYVLKRYVGEVQDSEHFTTASRSVKTGLISSAVVSSWTWPGTLLTSAGMAYEYGVCGSMWYSFAFTVQITFFTVIALQVKRVAPGAHTIVEIVKARFGQASHAVFLFYALGTNIIVSAMLLLGGSQAISAITGMHVVAAGFLLPLGVWLYTVSGGLKSTFLSDWTHTVIVYIVILITLFVAYTSSVHIGSIDKMYDLLTEVSKTNPSTGYKGSYLTVTNRDAVFVGWNIVIGGFATVFCDPSYGQKAIAAKPISAMKGYFAGGLAWLIVPWAMGSAAALSCLALTNNPVSVTYPDPVSSKQVSEGMPLLYGMTALMGKNGAAAGVLILFMASTSATSAELVAFSSVMTYDVYRNYFRPNASGKELVRVTHVFVTIFAVCMGALAVLFNYIGITISWIITFIGIALGPAVFGITLTLFWKKMNKYGMIIGCPMGSITGVVCWVGSCYKFSNGVVNKTTLNTPYANAVGNFTGLFSGLIYIVLISYFFPNKSDDLNNLNEKFVLGDDATAEEIVDAETEKKQLDRSLRIGIFVSWIIFFILVIIVPLPMYGSKYIFSKLFFRGWIIVIIIWTLIAALYITFYPLYESRDTIVYLCKLAIGKAKAPEPMNYVDAVEVEIESLSDDDKEKKANDFL
Protein: Myosin-9 (Cellular myosin heavy chain, type A) (Myosin heavy chain 9) (Myosin heavy chain, non-muscle IIa) (Non-muscle myosin heavy chain A) (NMMHC-A) (Non-muscle myosin heavy chain IIa) (NMMHC II-a) (NMMHC-IIA) (P14105)
Organism: Gallus gallus (Chicken)
Function: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8VDD5}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q8VDD5}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:Q8VDD5}. Note=Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells. {ECO:0000250|UniProtKB:P35579}.
Interaction partners:
- Myosin light polypeptide 6
- Actin, cytoplasmic 1
- Myosin regulatory light chain 2, smooth muscle major isoform
- Myosin regulatory light chain 2, smooth muscle minor isoform
- Actin, cytoplasmic 2
- Actin, aortic smooth muscle
- EF-hand domain-containing protein
- Myosin regulatory light chain 2B, cardiac muscle isoform
- Myosin regulatory light chain 2A, cardiac muscle isoform
- Myosin-11
Sequence:
MAQRDADKYLYVDKNIINNPLTQADWAAKKLVWVPSEKSGFEAASLKEEVGDEAIVELAENGKKVKVNKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPDEEQIGLLKVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYEQMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQNEGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIVGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERDLKITDVIIGFQACCRGYLARKAFAKRQQQLTAMKVLQRNCAAYLKLRNWQWWRLFTKVKPLLQVSRQEEEMMAKEEELIKVKEKQLAAENRLSEMETFQAQLMAEKMQLQEQLQAEAELCAEAEEIRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEDVIVLEDQNLKLAKEKKLLEDRMSEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSSDLHDQIAELQAQIAELKIQLSKKEEELQAALARVEEEAAQKNMALKKIRELESQITELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVTVLKKTLEDEAKTHEAQIQEMRQKHSQAIEELAEQLEQTKRVKANLEKAKQALESERAELSNEVKVLLQGKGDAEHKRKKVDAQLQELQVKFTEGERVKTELAERVNKLQVELDNVTGLLNQSDSKSIKLAKDFSALESQLQDTQELLQEETRLKLSFSTKLKQTEDEKNALKEQLEEEEEAKRNLEKQISVLQQQAVEARKKMDDGLGCLEIAEEAKKKLQKDLESLTQRYEEKIAAYDKLEKTKTRLQQELDDIAVDLDHQRQTVSNLEKKQKKFDQLLAEEKNISAKYAEERDRAEAEAREKETKALSLARALEEAIEQKAELERVNKQFRTEMEDLMSSKDDVGKSVHELEKAKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNQQAMKAQFDRDLLGRDEQNEEKRKQLIRQVREMEVELEDERKQRSIAVAARKKLELDLKDLESHIDTANKNRDEAIKHVRKLQAQMKDYMRELEDTRTSREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALAMEEKRRLEARIAQLEEELEEEQGNTEIINDRLKKANLQIDQMNADLNAERSNAQKNENARQQMERQNKELKLKLQEMESAVKSKYKATITALEAKIVQLEEQLDMETKERQAASKQVRRAEKKLKDILLQVDDERRNAEQFKDQADKANMRLKQLKRQLEEAEEEAQRANVRRKLQRELDDATETADAMNREVSSLKSKLRRGDLPFVVTRRLVRKGTGECSDEEVDGKAEAGDAKATE
Protein: HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (A0A8I5ZK23)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSALSPGLPDPFAKIVVDGSGQCHSTDTVKNTLDPKWNQHYDLYVGKTDSITISVWNHKKIHKKQGAGFLGCVRLLSNAISRLKDTGYQRLDLCKLNPSDTDAVRGQIVVSLQTRDRIGGGGSVVDCRGLLENEGTVYEDSGPGRPLSCLMEEPAPYTDGTGAAAGGGNCRFVESPSQDQRLLVQRLRNPEVRGSLQTPQNRPHGHQSPELPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPRDLNSVNCDELGPLPPGWEVRSTVSGRIYFVDHNNRTTQFTDPRLHHIMNHQCQLKEPSQPLQLPSEGSVEDEELPAQRYERDLVQKLKVLRHELSLQQPQAGHCRIEVSREEIFEESYRQIMKMRPKDLKKRLMVKFRGEEGLDYGGVAREWLYLLCHEMLNPYYGLFQYSTDNIYTLQINPDSSINPDHLSYFHFVGRIMGLAVFHGHYINGGFTVPFYKQLLGKPIQLSDLESVDPELHKSLVWILENDITPVLDHTFCVEHNAFGRILQHELKPNGRNVPVTEENKKEYVRLYVNWRFMRGIEAQFLALQKGFNELIPQHLLKPFDQKELELIIGGLDKIDLNDWKSNTRLKHCVADSNIVRWFWQAVETFDEERRARLLQFVTGSTRVPLQGFKALQGSTGAAGPRLFTIHLIDANTDNLPKAHTCFNRIDIPPYESYEKLYEKLLTAVEETCGFAVE
Protein: Cytochrome c oxidase assembly protein COX20, mitochondrial (B3KM21)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
Sequence:
MAAPPEPGEPEERKSLKLLGFLDVENTPCARHSILYGSLGSVVAGFGHFLFTSRIRRSCDVGVGGFILVTLGCWFHCRYNYAKQRIQERIAREEIKKKILYEGTHLDPERKHNGSSSN
Protein: Integrin alpha-3 (CD49 antigen-like family member C) (FRP-2) (Galactoprotein B3) (GAPB3) (VLA-3 subunit alpha) (CD antigen CD49c) [Cleaved into: Integrin alpha-3 heavy chain; Integrin alpha-3 light chain] (P26006)
Organism: Homo sapiens (Human)
Function: Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15611341, ECO:0000269|PubMed:32487760}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15611341}; Lipid-anchor {ECO:0000269|PubMed:15611341}. Cell projection, invadopodium membrane {ECO:0000269|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, filopodium membrane {ECO:0000269|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Note=Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. {ECO:0000269|PubMed:10455171}.
Interaction partners:
- Fibronectin
- Integrin beta-1
- CD151 antigen
- Integrin beta-5
- Integrin beta-4
- Integrin beta-3
- Focal adhesion kinase 1
- Integrin beta-6
- Integrin alpha-2
- CD9 antigen
Sequence:
MGPGPSRAPRAPRLMLCALALMVAAGGCVVSAFNLDTRFLVVKEAGNPGSLFGYSVALHRQTERQQRYLLLAGAPRELAVPDGYTNRTGAVYLCPLTAHKDDCERMNITVKNDPGHHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGSEDQRRMVGKCYVRGNDLELDSSDDWQTYHNEMCNSNTDYLETGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKEWDLSEYSYKDPEDQGNLYIGYTMQVGSFILHPKNITIVTGAPRHRHMGAVFLLSQEAGGDLRRRQVLEGSQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAIYVFMNQAGTSFPAHPSLLLHGPSGSAFGLSVASIGDINQDGFQDIAVGAPFEGLGKVYIYHSSSKGLLRQPQQVIHGEKLGLPGLATFGYSLSGQMDVDENFYPDLLVGSLSDHIVLLRARPVINIVHKTLVPRPAVLDPALCTATSCVQVELCFAYNQSAGNPNYRRNITLAYTLEADRDRRPPRLRFAGSESAVFHGFFSMPEMRCQKLELLLMDNLRDKLRPIIISMNYSLPLRMPDRPRLGLRSLDAYPILNQAQALENHTEVQFQKECGPDNKCESNLQMRAAFVSEQQQKLSRLQYSRDVRKLLLSINVTNTRTSERSGEDAHEALLTLVVPPALLLSSVRPPGACQANETIFCELGNPFKRNQRMELLIAFEVIGVTLHTRDLQVQLQLSTSSHQDNLWPMILTLLVDYTLQTSLSMVNHRLQSFFGGTVMGESGMKTVEDVGSPLKYEFQVGPMGEGLVGLGTLVLGLEWPYEVSNGKWLLYPTEITVHGNGSWPCRPPGDLINPLNLTLSDPGDRPSSPQRRRRQLDPGGGQGPPPVTLAAAKKAKSETVLTCATGRAHCVWLECPIPDAPVVTNVTVKARVWNSTFIEDYRDFDRVRVNGWATLFLRTSIPTINMENKTTWFSVDIDSELVEELPAEIELWLVLVAVGAGLLLLGLIILLLWKCGFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY
Protein: Netrin receptor DCC (Tumor suppressor protein DCC) (Q63155)
Organism: Rattus norvegicus (Rat)
Function: Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:8861902}; Single-pass type I membrane protein {ECO:0000269|PubMed:8861902}.
Interaction partners:
- Netrin-1
- Focal adhesion kinase 1
- Mitogen-activated protein kinase 1
- Caspase-9
- Netrin receptor UNC5A
- Draxin
- Netrin receptor UNC5D
- Proto-oncogene tyrosine-protein kinase Src
- Netrin receptor UNC5B
- Netrin receptor UNC5C
Sequence:
MENSLGCVWVPKLAFVLFGASLLSAHLQVTGFQIKPFTSLHFVSEPSDAVTMRGGNVLLNCSAESDRGVPVIKWKKDGLILALGMDDRKQQLPNGSLLIQNILHSRHHKPDEGLYQCEASLGDSGSIISRTAKVMVAGPLRFLSQTESITAFMGDTVLLKCEVIGDPMPTIHWQKNQQDLNPIPGDSRVVVLPSGALQISRLQPGDSGVYRCSARNPASTRTGNEAEVRILSDPGLHRQLYFLQRPSNVIAIEGKDAVLECCVSGYPPPSFTWLRGEEVIQLRSKKYSLLGGSNLLISNVTDDDSGTYTCVVTYKNENISASAELTVLVPPWFLNHPSNLYAYESMDIEFECAVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQSSAQLIVPKPAIPSSSILPSAPRDVVPVLVSSRFVRLSWRPPAEAKGNIQTFTVFFSREGDNRERALNTTQPGSLQLTVGNLKPEAMYTFRVVAYNEWGPGESSQPIKVATQPELQVPGPVENLHAVSASPTSILITWEPPAYANGPVQGYRLFCTEVSTGKEQNIEVDGLSYKLEGLKKFTEYTLRFLAYNRYGPGVSTDDITVVTLSDVPSAPPQNVSLEVVNSRSIKVSWLPPPSGTQNGFITGYKIRHRKTTRRGEMETLEPNNLWYLFTGLEKGSQYSFQVSAMTVNGTGPPSNWYTAETPENDLDESQVPDQPSSLHVRPQTNCIIMSWTPPLNPNIVVRGYIIGYGVGSPYAETVRVDSKQRYYSIERLESSSHYVISLKAFNNAGEGVPLYESATTRSITDPTDPVDYYPLLDDFPTSGPDVSTPMLPPVGVQAVALTHEAVRVSWADNSVPKNQKTSDVRLYTVRWRTSFSASAKYKSEDTTSLSYTATGLKPNTMYEFSVMVTKNRRSSTWSMTAHATTYEAAPTSAPKDLTVITREGKPRAVIVSWQPPLEANGKITAYILFYTLDKNIPIDDWIMETISGDRLTHQIMDLSLDTMYYFRIQARNAKGVGPLSDPILFRTLKVEHPDKMANDQGRHGDGGYWPVDTNLIDRSTLNEPPIGQMHPPHGSVTPQKNSNLLVITVVTVGVLTVLVVVIVAVICTRRSSAQQRKKRATHSASKRKGSQKDLRPPDLWIHHEEMEMKNIEKPAGTDPAGRGSPIQSCQDLTPVSHSQSESQMGSKSASHSGQDTEEAGSSMSTLERSLAARRATRTKLMIPMEAQSNNPAVVSAIPVPTLESAQYPGILPSPTCGYPHPQFTLRPVPFPTLSVDRGFGAGRTVSEGPTAQQQPMLPPAQPEHPSSEEAPSRTIPTACVRPTHPLRSFANPLLPPPMSAIEPKVPYTPLLSQPGPTLPKTHVKTASLGLAGKARSPLLPVSVPTAPEVSEESHKPTEDPASVYEQDDLSEQMASLEGLMKQLNAITGSAF
Protein: Phosphatidate phosphatase LPIN2 (EC 3.1.3.4) (Lipin-2) (Q99PI5)
Organism: Mus musculus (Mouse)
Function: Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the reticulum endoplasmic membrane. Plays important roles in controlling the metabolism of fatty acids at different levels. Acts also as a nuclear transcriptional coactivator for PPARGC1A to modulate lipid metabolism.
Subcellular location: Nucleus. Cytoplasm, cytosol. Endoplasmic reticulum membrane. Note=Translocates from cytosol to endoplasmic reticulum membrane with increasing levels of oleate.
Interaction partners:
- Phospholipid phosphatase 3
- Phospholipid phosphatase 2
- Diacylglycerol O-acyltransferase 1
- Diacylglycerol O-acyltransferase 2
- 2-acylglycerol O-acyltransferase 1
- Phosphatidate phosphatase LPIN3
- Phosphatidate phosphatase LPIN1
- 2-acylglycerol O-acyltransferase 2
- Choline/ethanolaminephosphotransferase 1
- Phosphatidate cytidylyltransferase 2
Sequence:
MNYVGQLAGQVLVTVKELYKGINQATLSGCIDVVVVRQQDGSYQCSPFHVRFGKLGVLRSKEKVIDIEINGSAVDLHMKLGDNGEAFFVEETEEEYEKLPAYLATSPIPTEDQFFKHIETPLVKSSGNERPAQSSDVSHTLESEAVFTQSSVKKKKRRRKKCKQDNRKEEQAASPVAEDVGDVGVSSDDEKRAQAARGSSNASLKEEDYKEPSLFHSGDNYPLSDGDWSPLETTYPQAVCPKSDSELEVKPSESLLRSEPHMEWTWGGFPESTKVTKRERYDYHPRTATITPSENTHFRVIPSEDSLIREVEKDATVEDTTCTIVKPKPRALCKQLSDAASTELPESPLEAPQISSLLDADPVPSPSAEAPSEPKPAAKDSPTKKKGVHKRSQHQGPDDIYLDDLKALEPEVAALYFPKSDTDPGSRQWPESDTFSGSQSPQSVGSAAADSGTECLSDSAMDLPDVTLSLCGGLSENGEISKEKFMEHIITYHEFAENPGLIDNPNLVIRIYNRYYNWALAAPMILSLQVFQKSLPKATVESWVKDKMPKKSGRWWFWRKKESMIKQLPETKEGKSEVPPANDLPSNAEEPTSARPAENDTSSDEGSQELEESIKVDPITVETLSHCGTASYKKSLRLSSDQIAKLKLHDGPNDVVFSITTQYQGTCRCAGTIYLWNWNDKVIISDIDGTITKSDALGQILPQLGKDWTHQGIARLYHSINENGYKFLYCSARAIGMADMTRGYLHWVNDKGTILPRGPLMLSPSSLFSAFHREVIEKKPEKFKIECLNDIKNLFAPSRQPFYAAFGNRPNDVYAYTQVGVPDCRIFTVNPKGELIQERTKGNKSSYHRLSELVEHVFPLLSKEQNSAFPCPEFSSFCYWRDPIPDLDLDDLA
Protein: DNA excision repair protein, putative (Q57UN8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- DNA-direcetd RNA polymerase II, subunit 9, putative
- Plastid-encoded RNA polymerase subunit alpha
- DNA damage-binding protein 1
- RNA polymerase-like protein
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II, putative
- DNA repair helicase/translocase XPB-R
- Uncharacterized protein
Sequence:
MADELSQLGVNWVEESLLRQDVEANVEARADAAAAADEAELQRRWAALEEVERTVANIQEQLSKVVAPVGTAAHKIVEEKESASVLQFSLLKAQRELESRAKALRSWQIECEARQRRRVEEAKQRKQVTEQEAVMARMRNRLSRTLQPVADVQGLQEGVGSAERVPASTNHHDYHDRLTTGMGSTPQVWWNGRIGTPNGAASVTHSNISTPSRRQRLSSSTSADVPLTPAQYSCGPVLPSAYRVTLTPSDVRSKLQKYADDSDLSIYSARCRKRKRLEGALAGLAALEAGVATANGEIKEEDTDEDSGVVVKCEGIGMSSFPKVKTEGSAHEKSGTSLLDAIDVDALMEESDDVAVEVLQKVKKEKRASAGGRKHRERENTTQNFTDRHDSIEVLRGISLASSIYQKLFDHQRDGLRWLLNLHRQRVGGILGDDMGLGKTIQIAAMLNALNHSNQLRGPSLIVTPVTVLRQWVAEMHRWAPYVRTCVMHASSASTISREKLIDSVRGTPAVLLTTYAAVREHCRLLHNACFQYVILDEGHKISNPEATVTIAAKSFPTPHRLILSGTPVQNTLKELWCLFDFVKPGLLGTLRRFEEEFEVPINASKNIRASPLALATAAETARVLHESISPFLLRRLKKQVMSDSLPEKYERVIRCPLSDSQLEAYVDLLSSSRVQRLMSNTLSYTQLMGGLDRDGRDASGCLHIAGKRFQLMRDKENKGVVRHELFCVMHELRQICNHVDIFHMRQAKDFNYTDDMENNFFLDVVNAPTATARKAGGKGTTHFSMRSNRPVNYEGSSKLQTLRQLLKLWQRGGQRALVFSQTRAMLDIIENMCEQESLTYIRMDGTTNSLRRQELMDRFNEDDRIVVALLTTRVGGVGVNLIGADRVVIFDPDWNPVTDEQARERAWRIGQTRDVGVYRLISSGTVEEAVLRRQLAKTYVTEKVLHDPKLQRFFYEQGSLSESFYLGVEYDSRVPLGKKHIVAAQELFPLLKEEHNNEEVFALTAVGHERRIRGTEEESGGASVRAKSETEKTAAASVYRVCAPRELFPSATTTSRTSSSNISETSLLQDLVDGNHVRISGVDSTAQRLACTSASHAMLRVSNVIRTFEHQTQEAFARLPRVEGS
Protein: Collagen alpha-1(XXV) chain (Alzheimer disease amyloid-associated protein) (AMY) (CLAC-P) [Cleaved into: Collagen-like Alzheimer amyloid plaque component (CLAC)] (Q9BXS0)
Organism: Homo sapiens (Human)
Function: Inhibits fibrillization of amyloid-beta peptide during the elongation phase. Has also been shown to assemble amyloid fibrils into protease-resistant aggregates. Binds heparin.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=After proteolytic cleavage, CLAC is secreted.
Interaction partners:
- Collagen alpha-1
- Furin
- Collectin-10
- Amyloid-beta precursor protein
Sequence:
MLLKKHAGKGGGREPRSEDPTPAEQHCARTMPPCAVLAALLSVVAVVSCLYLGVKTNDLQARIAALESAKGAPSIHLLPDTLDHLKTMVQEKVERLLAQKSYEHMAKIRIAREAPSECNCPAGPPGKRGKRGRRGESGPPGQPGPQGPPGPKGDKGEQGDQGPRMVFPKINHGFLSADQQLIKRRLIKGDQGQAGPPGPPGPPGPRGPPGDTGKDGPRGMPGVPGEPGKPGEQGLMGPLGPPGQKGSIGAPGIPGMNGQKGEPGLPGAVGQNGIPGPKGEPGEQGEKGDAGENGPKGDTGEKGDPGSSAAGIKGEPGESGRPGQKGEPGLPGLPGLPGIKGEPGFIGPQGEPGLPGLPGTKGERGEAGPPGRGERGEPGAPGPKGKQGESGTRGPKGSKGDRGEKGDSGAQGPRGPPGQKGDQGATEIIDYNGNLHEALQRITTLTVTGPPGPPGPQGLQGPKGEQGSPGIPGMDGEQGLKGSKGDMGDPGMTGEKGGIGLPGLPGANGMKGEKGDSGMPGPQGPSIIGPPGPPGPHGPPGPMGPHGLPGPKGTDGPMGPHGPAGPKGERGEKGAMGEPGPRGPYGLPGKDGEPGLDGFPGPRGEKGDLGEKGEKGFRGVKGEKGEPGQPGLDGLDAPCQLGPDGLPMPGCWQK