wanglab/gogpt-training-data huggingface dataset:
Protein: Galactoside 2-alpha-L-fucosyltransferase Sec1 (EC 2.4.1.-) (Alpha(1,2)FT 3) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 3) (Secretory blood group protein 1) (P97353)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of alpha 1,2-linked fucose to ganglioside GM1 and galacto-N-biose (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:O09160}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O09160}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250|UniProtKB:O09160}.
Interaction partners:
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- Beta-1,4-galactosyltransferase 1
- Beta-1,3-galactosyltransferase 5
- Alpha-
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
- CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- Beta-1,3-galactosyltransferase 1
- N-acetyllactosaminide alpha-1,3-galactosyltransferase
Sequence:
MPSDSCLLSLTVLQRLRAICPPLSTFYLFFVIFVVSTIFHCHRRLGLVPAPWASPSLVVFPPRHMPREGMFTIRVKGRLGNQMGEYATLFALARMNGRLAFIPASMHSTLAPIFRISLPVLHSDTAKRIPWQNYHLNDWMEERYRHIPGHYVRFTGYPCSWTFYHHLRPEILKEFTLHDHVREEAQAFLRGLQVNGSQPSTFVGVHVRRGDYVRVMPKVWKGVVADRGYLEKALDRFRARYSSPVFVVTSDDMAWCRKSITASRGDVAFAGNGLQGSPAKDIALLMQCNHTVITLGTFGIWAAYLTGGDTVYLANFTQPNSPFHTVFKPEAAYLPEWVGIAADLGQPNTVGSGHASARAPKRHWGALL
Protein: Glutamate receptor-interacting protein 2 (xGRIP2) (xGRIP2.1) (A8E0R9)
Organism: Xenopus laevis (African clawed frog)
Function: Plays an important role in primordial germ cell (PGC) maintenance and efficiency of PGC migration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17320814, ECO:0000269|PubMed:17936745}.
Interaction partners:
Sequence:
MHFFQTILRWKTAKGQKSVTFKKDDGPYSKGNKDPAGNDLALVSRRQSIPEEFRGVTIVELIKKEGSTLGLTISGGTDKDGKPRVSNLRPGGLAARSDQLNIGDYIKSVNGINLTKLRHEEIISLLKNVGERVVLEVEYELPPGTPDNSSAIIPKTIEITLCKEGNSFGFVMRGGAHEDWHKSRALVVTYVRPGGPADREGTLKVGDRLLCVDGISLHNITHTDALSILRQCSQEGVFQIEYDVALMDTVTNASGPLLVEIAKTPGSTLGISLSTGTHRNKQVIVIDKVKPASVVDRCGALHPGDHILSIDGTSTEHCTQMEATQLLASIIENVKLEILPAHHSRLPLRPPETVKVQKSDHHHCWDPCVNYCHTPHPGHCKTPTWNPTSNQDYCKSLVAANFSSSSVAGTPGFSSQNSNTLPRTVHPMSPRTTMNRRRQKRKDHKSSLSLASSTVGPGGQIIHTESTEIILRGDPLNGFGIQLQGGIFATETLSSPPLIRFIEPDSPAERCGLLQVGDRLLSINGILTEDGTLEEANQLLRDAALSNKVALEIEFDVAESVVPSSGTFHVKLPKRKGVELGITISSSRKPGEPLIISDIKKGSVAHRTGTLEPGDKLLAIDNIRLDNCSMEDAVQILRQCEDLVKLKIRKDEDNSDEQETSGAIIYTVELKRYGGPLGITISGTEEPFDPIVISGLTKRGLAERTGAIHIGDRILAINNISLKGKPLSEAIHLLQMAGETVTLKIKKQTERIFPQRLSDSMNEGSDPEDDLTDSQKTSKLSEIYSTTVPSVDSALESWDGSGIDAGYGSQGTYVPQAVGISLHPHEWRTSRQKSNTPPVEHRKSYPFLDGSFNEQDWEKPTRYPSQPNGLETDHDDSFWRVFGEALEDLETCGQSELLREIEASIMTGSVQDLGLDSSQILLENSSQGGHVLFRRGSHHISSNSPKKENKLSQDARSKKEEVHNAQSLTTELLKVTVQKDMDTDDFGFSVSDGLLEKGVYVNMIRPGGPADRSGLKTYDQILQVNHVRTRDFDCCLTVPLLSDAGDRLDLVISRGLSIKAEEMGVEQIKGPLRMETQTSTKTL
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A (Protein MATERNAL EFFECT EMBRYO ARREST 4) (Q8RWA7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 8-B
- NADH dehydrogenase 1 beta subcomplex subunit 10-B
- NADH dehydrogenase iron-sulfur protein 8-A, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8-B, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2
- NADH dehydrogenase iron-sulfur protein 6
- NADH dehydrogenase 1 alpha subcomplex subunit 9
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
Sequence:
MTEAMIRNKPGMASVKDMPLLQDGPPPGGFAPVRYARRISNTGPSAMAMFLAVSGAFAWGMYQVGQGNKIRRALKEEKYAARRTILPILQAEEDERFVSEWKKYLEYEADVMKDVPGWKVGENVYNSGRWMPPATGELRPDVW
Protein: cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) (I1IPY7)
Organism: Brachypodium distachyon (Purple false brome) (Trachynia distachya)
Interaction partners:
- MADS-box domain-containing protein
Sequence:
MEQGKAALGWAARDASGHLSPYNFSRRVQKDDDVTIKVLFCGICHTDLHIIKNEWGNALYPIVPGHEVVGVVTDVGPGVKNFKAGETVGVGYFLDSCRTCDSCSKGHENYCPTLVLTSNGVDYDGATTQGGFSDVVVVNQDYVVRVPDTLPPDGAAPLLCAGVTVYSPMMQYGLNAPGKHLGVVGLGGLGHMAVKFGKAFGMKVTVISSSLRKREEALDRLGADDFLVSSDAEQMKAAAGAMDGIIDTVSAGHPIVPLLELLRPMGQMVVCGAPSEPLQLPAYAVITGGKRIAGNGVGSVRDCQAMLDFAGEHGITADVEVVKMDYVNTAVERLERNDVRYRFVIDVAGSLQQGGAA
Protein: PRP1 splicing factor N-terminal domain-containing protein (Q381L7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Spliceosome-associated protein, putative
- U5 small nuclear ribonucleoprotein component, putative
- Sm protein G
- RNA-binding protein, putative
- Sm protein B
- Small nuclear ribonucleoprotein E
- Sm protein F
- Splicing factor 3B subunit 1, putative
- Spliceosomal U5 snRNP-specific protein, putative
- PRP8 protein homologue
Sequence:
MSAAAPVLSTKVDKYEQVLAKYDWRSPFPPRGYQYGIGRGAKAFITSAELSATTGVSAPLLALGGEQSAMLDALDRLEERRHKRRREDVKGGATSREGKKPKLLLSMEDIATVGSGASNQSLVKRKARTEDMDVVDGYAFDDETAVVTASDLLRGRALAANQTLENILNMGSSSEQTTWITHSRALREMGMTKKAQQTLVEGSRLTGSKGPLIWKEQLQHLNDPAAQRQLLEQAVAACKTCEELWFLLLQYQPPHEQLHWLQKAVMACPASESLWLRILGYVTAPRDQRKIIRKALEVTPTLPSLWAMLARLEDYERGKAIFNAAAAEHPSMKIIIEGAKFEEFHLRGQVGSEKEGGNEQLHNAKIHSLVRQAAQRFLLMDEEKSRTEWLDAARVAVSERYILTSAYMLLHFVCDTGAATLTIPVTWLEDLAALVPDMWRAHDVLCAAWATMLIGRDAAVKGTNEAVTEKDVQIIGFALRSAPFTSLETAVSAVTRYISSTTVSYTSRVEDGMKKEGIKEEEEEEELGRPVATIQAAPPTCSTSATAASQCLPLPLVSVLLYTLFRAPAFNTIDVMLSVAKVFYDHHFYDGAHRVLMLAITRYPVNALLFTAAAKTKMAMGCRKGAEELLLKGTAIDPSDSDIAWVKLAVHRRSNREDIVPLLDEALVHFPTSERLWLMRLEAEGMKAQQLLEDAMARGSSTAPTINGLRRVYGKALSSEHCRLSPTIWCYAAVKLESNLFSDAGAARALLLEGLVVCEKGCQHLHHNGSTKRAEVRATFGLARCHVELRHAGSETALETVKEVLQQLPKVDGCFTVSVGELVALSIDLENPATRGRAAAQAVQHWRVRDPLVFSSVAKLYHAAGRHEKALEQAMKAVQMSKGRCGDAVALWLKLASMFTYRKIVMEKMGLTVKDESNEEETALQNGVLLAWLWKQLANGSSGGTSGSEAMEDMKGSTESATHSEPPKPNSGPLWIYVSKSRDPSNVTLLGFRDSVEVMLTQVVEMIKL
Protein: serralysin (EC 3.4.24.40) (E0SC29)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- serralysin
- Alkaline protease secretion ATP-binding protein aprD
- Membrane fusion protein
- Outer membrane exporter of proteases
- Alkaline proteinase inhibitor
Sequence:
MGKNLSLRQDDAQHALSANTSSAYNSVYDFLHYHDRGDGLTVNGKTSYSVDQAAAQITRENVSWNGTNVFGKSANLTFKFLQSVSSIPSGDTGFVKFNAEQIEQAKLSLQSWSDVANLTFTEVTGNKSANITFGNYTRDASGNLDYGTQAYAYYPGNYQGAGSSWYNYNQSNIRNPGSEEYGRQTFTHEIGHALGLAHPGEYNAGEGDPSYNDAVYAEDSYQFSIMSYWGENETGADYNGHYGGAPMIDDIAAIQRLYGANMTTRTGDSVYGFNSNTDRDFYTATDSSKALIFSVWDAGGNDTFDFSGYSNNQRINLNEGSFSDVGGLKGNVSIAHGVTIENAIGGSGNDILVGNSADNILQGGAGNDVLYGGAGADTLYGGAGRDTFVYGSGQDSTVAAYDWIADFQKGIDKIDLSAFRNEGQLSFVQDQFTGKGQEVMLQWDAANSITNLWLHEAGHSSVDFLVRIVGQAAQSDIIV
Protein: Gamma-aminobutyrate transaminase POP2, mitochondrial (AtGABA-T) (EC 2.6.1.96) (Gamma-aminobutyric acid aminotransferase 1) (Protein HEXENAL RESPONSE 1) (Protein POLLEN-PISTIL INCOMPATIBILITY 2) (AtPOP2) (Q94CE5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transaminase that degrades gamma-amino butyric acid (GABA) and uses pyruvate or glyoxylate as amino-group acceptor, but not 2-oxoglutarate. The pyruvate-dependent activity is reversible while the glyoxylate-dependent activity is irreversible. Cannot use beta-alanine, ornithine, acetylornithine, serine, glycine, asparagine, glutamine, glutamate, valine, leucine, isoleucine, methionine, phenylalanine, histidine, lysine, arginine, aspartate, threonine, tyrosine, tryptophan, proline, or cysteine as amino donors. Modulates steady-state GABA levels in diploid pistil cells and the haploid pollen tube. Involved in the formation of a gradient of GABA along the pollen tube path. Involved in the maintenance of the shoot apical meristem (SAM) structure and subsequent adaxial-abaxial axis-dependent development of cotyledons and leaves.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12859897, ECO:0000269|PubMed:19264755}.
Interaction partners:
- Glutamate decarboxylase 2
- Glutamate decarboxylase 1
- Succinate-semialdehyde dehydrogenase, mitochondrial
- Glutamate decarboxylase 3
- Glutamate decarboxylase 4
- Glutamate decarboxylase 5
- Glyoxylate/succinic semialdehyde reductase 1
- Glyoxylate/succinic semialdehyde reductase 2, chloroplastic
- Aldehyde dehydrogenase family 2 member B4, mitochondrial
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
Sequence:
MVVINSLRRLARTTQVHLHSKYATCMSGNSTSRRIFTTEAAPEKKNTVGSKGHDMLAPFTAGWQSADLDPLVIAKSEGSYVYDDTGKKYLDSLAGLWCTALGGNEPRLVSAAVEQLNTLPFYHSFWNRTTKPSLDLAKVLLEMFTANKMAKAFFTSGGSDANDTQVKLVWYYNNALGRPEKKKFIARKKSYHGSTLISASLSGLPPLHQNFDLPAPFVLHTDCPHYWRFHLPGETEEEFSTRLAKNLEDLIIKEGPETIGAFIAEPVMGAGGVIPPPATYFEKVQAVVKKYDILFIADEVICAFGRLGTMFGCDKYNIKPDLVTLAKALSSAYMPIGAILMSQEVADVINSHSSKLGVFSHGFTYSGHPVSCAVAIEALKIYKERNIPEYVAKVAPRFQDGVKAFASGSPIIGETRGTGLILGTEFVDNKSPNEPFPPEWGVGAFFGAECQKHGMLVRVAGDGILMSPPLIISPEEIDELISIYGKALKATEEKVKELKAQHKK
Protein: U6 snRNA-associated Sm-like protein LSm1 (Q20229)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU365047}. Cytoplasm, P-body {ECO:0000256|RuleBase:RU365047}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm7
- Protein PAT1 homolog 1
- U6 snRNA-associated Sm-like protein LSm6
- Probable U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm3
- ATP-dependent RNA helicase cgh-1
- 5'-3' exoribonuclease 1
- U6 snRNA-associated Sm-like protein LSm8
Sequence:
MDLPDPYLPGAISLFEQLDKKLLVVLRDGRKLIGFLRSIDQFANLILEDVVERTFVEKYFCETGQGFMLIRGENVELAGEIDDTIETGLTQVSPEEFRRLEDEYIAKNPPKFLKRQAEKTEEHDA
Protein: PRELI domain containing protein 3A (Protein slowmo homolog 1) (Q8VE85)
Organism: Mus musculus (Mouse)
Function: In vitro, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space. Phosphatidic acid import is required for cardiolipin (CL) synthesis in the mitochondrial inner membrane.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96N28}.
Interaction partners:
- TP53-regulated inhibitor of apoptosis 1
- PRELI domain-containing protein 1, mitochondrial
Sequence:
MKIWSSEHVFGHPWDTVIKAAMRKYPNPMNPCVVGVDVLERSVDGCGRLHSLRLLSTEWGLPGLVRAILGANRTLTYIKERSVVDPAARKMELCSTNITLTNLVSVNERLVYTPHPENPEKTVLTQEAIITVKGISLGSYLESLMATTISSNAKKGWAAIEWIIEHSESAIS
Protein: Evasin P1168 (A0A0K8RCU3)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2 and CXCL8.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MEVKISTFLQIAVLIVLGIHLIAAGQDTDGKEKSDEYELFTVEYCGTNCTQLENGSWTACTGKNGTCRCFHENDKKVGLCLSTEYTDFSEYPDPNSEEIKAASPLP
Protein: Acireductone dioxygenase (Acireductone dioxygenase (Fe(2+)-requiring)) (ARD') (Fe-ARD) (EC 1.13.11.54) (Acireductone dioxygenase (Ni(2+)-requiring)) (ARD) (Ni-ARD) (EC 1.13.11.53) (Q6AWN0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03154}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03154}.
Interaction partners:
- Probable methylthioribulose-1-phosphate dehydratase
- Enolase-phosphatase E1
- Tyrosine aminotransferase
- Phosphoglucomutase 1
- Protein hu-li tai shao
- Ribonuclease P protein subunit p29
- S-adenosylmethionine synthase
- GH04035p
- Methylthioribose-1-phosphate isomerase
- cystathionine gamma-lyase
Sequence:
MVQVWYMDTEETDQRLEHHRNPPAYLELDDLYQKTGVEYFKINADEYQSDNTLTELRAKRGYTYDDEITCSEKCLPDYANKLKAFFTEHLHTDEEIRLILEGSGYFDVRDNEDNWLRIKVVKGDLIIIPAGIYHRFTLDTNNFIRTRRYFVGEPVWAPHNRPADEMDCRKSYIKHQSENFVQFNKV
Protein: Leucine--tRNA ligase (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) (P9WFV1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
Interaction partners:
- Isoleucine--tRNA ligase
- Methionine--tRNA ligase
- Phenylalanine--tRNA ligase beta subunit
- Arginine--tRNA ligase
- Glutamate--tRNA ligase
- Valine--tRNA ligase
- Tyrosine--tRNA ligase
- Threonine--tRNA ligase
- Aspartate--tRNA
- Proline--tRNA ligase
Sequence:
MTESPTAGPGGVPRADDADSDVPRYRYTAELAARLERTWQENWARLGTFNVPNPVGSLAPPDGAAVPDDKLFVQDMFPYPSGEGLHVGHPLGYIATDVYARYFRMVGRNVLHALGFDAFGLPAEQYAVQTGTHPRTRTEANVVNFRRQLGRLGFGHDSRRSFSTTDVDFYRWTQWIFLQIYNAWFDTTANKARPISELVAEFESGARCLDGGRDWAKLTAGERADVIDEYRLVYRADSLVNWCPGLGTVLANEEVTADGRSDRGNFPVFRKRLRQWMMRITAYADRLLDDLDVLDWPEQVKTMQRNWIGRSTGAVALFSARAASDDGFEVDIEVFTTRPDTLFGATYLVLAPEHDLVDELVAASWPAGVNPLWTYGGGTPGEAIAAYRRAIAAKSDLERQESREKTGVFLGSYAINPANGEPVPIFIADYVLAGYGTGAIMAVPGHDQRDWDFARAFGLPIVEVIAGGNISESAYTGDGILVNSDYLNGMSVPAAKRAIVDRLESAGRGRARIEFKLRDWLFARQRYWGEPFPIVYDSDGRPHALDEAALPVELPDVPDYSPVLFDPDDADSEPSPPLAKATEWVHVDLDLGDGLKPYSRDTNVMPQWAGSSWYELRYTDPHNSERFCAKENEAYWMGPRPAEHGPDDPGGVDLYVGGAEHAVLHLLYSRFWHKVLYDLGHVSSREPYRRLVNQGYIQAYAYTDARGSYVPAEQVIERGDRFVYPGPDGEVEVFQEFGKIGKSLKNSVSPDEICDAYGADTLRVYEMSMGPLEASRPWATKDVVGAYRFLQRVWRLVVDEHTGETRVADGVELDIDTLRALHRTIVGVSEDFAALRNNTATAKLIEYTNHLTKKHRDAVPRAAVEPLVQMLAPLAPHIAEELWLRLGNTTSLAHGPFPKADAAYLVDETVEYPVQVNGKVRGRVVVAADTDEETLKAAVLTDEKVQAFLAGATPRKVIVVAGRLVNLVI
Protein: Putative acyl-[acyl-carrier-protein] desaturase DesA2 (Putative acyl-ACP desaturase DesA2) (EC 1.14.19.-) (P9WNZ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May be a desaturase involved in mycobacterial fatty acid biosynthesis.
Interaction partners:
- Putative acyl-[acyl-carrier-protein] desaturase DesA1
- NADPH-dependent stearoyl-CoA 9-desaturase
- Probable fatty acid synthase Fas
- NADPH oxidoreductase
- Ferredoxin
- Probable tRNA-dihydrouridine synthase
- Protein NrdI
- Ribonucleoside-diphosphate reductase subunit alpha
- Vitamin B12-dependent ribonucleoside-diphosphate reductase
- Protein PhoH2
Sequence:
MAQKPVADALTLELEPVVEANMTRHLDTEDIWFAHDYVPFDQGENFAFLGGRDWDPSQSTLPRTITDACEILLILKDNLAGHHRELVEHFILEDWWGRWLGRWTAEEHLHAIALREYLVVTREVDPVANEDVRVQHVMKGYRAEKYTQVETLVYMAFYERCGAVFCRNLAAQIEEPILAGLIDRIARDEVRHEEFFANLVTHCLDYTRDETIAAIAARAADLDVLGADIEAYRDKLQNVADAGIFGKPQLRQLISDRITAWGLAGEPSLKQFVTG
Protein: Mitochondrial fission 1 protein (FIS1 homolog) (hFis1) (Tetratricopeptide repeat protein 11) (TPR repeat protein 11) (Q9Y3D6)
Organism: Homo sapiens (Human)
Function: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission. May not be essential for the assembly of functional fission complexes and the subsequent membrane scission event. Also mediates peroxisomal fission. May act when the products of fission are directed toward mitochondrial homeostasis, mitophagy, or apoptosis. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:12783892, ECO:0000269|PubMed:14623186, ECO:0000269|PubMed:14996942, ECO:0000269|PubMed:16107562}; Single-pass membrane protein {ECO:0000269|PubMed:14996942}. Peroxisome membrane {ECO:0000269|PubMed:16107562}; Single-pass membrane protein {ECO:0000305|PubMed:16107562}.
Interaction partners:
- Dynamin-1-like protein
- TBC1 domain family member 15
- Dynamin-1
- B-cell receptor-associated protein 31
- TBC1 domain family member 17
- Density-regulated protein
- Mitochondrial fission factor
- Mitofusin-2
- Peroxisomal membrane protein 11A
- E3 ubiquitin-protein ligase MARCHF5
Sequence:
MEAVLNELVSVEDLLKFEKKFQSEKAAGSVSKSTQFEYAWCLVRSKYNDDIRKGIVLLEELLPKGSKEEQRDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS
Protein: Probable pectinesterase/pectinesterase inhibitor 17 [Includes: Pectinesterase inhibitor 17 (Pectin methylesterase inhibitor 17); Pectinesterase 17 (PE 17) (EC 3.1.1.11) (Pectin methylesterase 17) (AtPME17)] (O22149)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular location: Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Subtilisin-like protease SBT3.5
- Berberine bridge enzyme-like 8
- Berberine bridge enzyme-like 22
- Pectinesterase inhibitor 4
- Pectinesterase inhibitor 12
- Pectinesterase inhibitor 10
- Pectinesterase inhibitor 11
- Pectinesterase inhibitor 7
- At2g44240/F4I1.5
- Plant invertase/pectin methylesterase inhibitor superfamily protein
Sequence:
MMAFRAYIINFVILCILVASTVSGYNQKDVKAWCSQTPNPKPCEYFLTHNSNNEPIKSESEFLKISMKLVLDRAILAKTHAFTLGPKCRDTREKAAWEDCIKLYDLTVSKINETMDPNVKCSKLDAQTWLSTALTNLDTCRAGFLELGVTDIVLPLMSNNVSNLLCNTLAINKVPFNYTPPEKDGFPSWVKPGDRKLLQSSTPKDNAVVAKDGSGNFKTIKEAIDAASGSGRFVIYVKQGVYSENLEIRKKNVMLRGDGIGKTIITGSKSVGGGTTTFNSATVAAVGDGFIARGITFRNTAGASNEQAVALRSGSDLSVFYQCSFEAYQDTLYVHSNRQFYRDCDVYGTVDFIFGNAAAVLQNCNIFARRPRSKTNTITAQGRSDPNQNTGIIIHNSRVTAASDLRPVLGSTKTYLGRPWRQYSRTVFMKTSLDSLIDPRGWLEWDGNFALKTLFYAEFQNTGPGASTSGRVTWPGFRVLGSASEASKFTVGTFLAGGSWIPSSVPFTSGL
Protein: Small ribosomal subunit protein mS26 (28S ribosomal protein S26, mitochondrial) (H6UQ72)
Organism: Gallus gallus (Chicken)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAPGGCPLLALLLLAGTAQGQHWSHGWYPGGKRDLSAPQAIPAWSPWLVPSRGRKSRYDPPAKAKASRLKVPPPVDPAELYVVTERYRQHRLVLSALRSIFRSEVVQRKREAQRDAEDSAALSEEHRLLMAWNDAENARQRARR
Protein: Tubulin alpha-2 chain (EC 3.6.5.-) (P04689)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta chain
- Dynein heavy chain, cytoplasmic
- Kinesin-like protein cut7
- Microtubule integrity protein mal3
- Dynein intermediate chain 1
- Inner kinetochore subunit mis6
- Tubulin alpha-1 chain
- Actin
- Spindle pole body component alp14
- Nuclear envelope protein ndc1
Sequence:
MREIISIHVGQAGTQIGNACWELYCLEHGIQPNGYMNPETASQNSDGGFSTFFSETGQGKYVPRSIYVDLEPNVIDQVRTGPYRDLFHPEQLITGKEDASNNYARGHYTVGKELVDEVTDKIRRIADNCSGLQGFLVFHSFGGGTGSGFGALLLERLAMEYTKKSKLQFSVYPAPQVSTSVVEPYNSVLTTHATLDLADCTFMVDNESCYDICRRNLDIERPSYENLNRLIAQVVSSITASLRFEGSLNVDLAEFQTNLVPYPRIHFPLVTYAPIVSAAKAFHESNSVQEITNQCFEPYNQMVKCDPRAGRYMATCLLYRGDVIPRDVQAAVTTIKAKRTIQFVDWCPTGFKIGICDRPPQHIEGSEIAKVDRAVCMLSNTTSIAEAWSRLDHKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALERDYEEVGQDSMEVDYMEEEY
Protein: ALA-interacting subunit 3 (AtALIS3) (Q9SLK2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the lipid transport activity of the ALA/ALIS P4-ATPase complex.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein {ECO:0000269|PubMed:20053675}. Prevacuolar compartment membrane {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein {ECO:0000269|PubMed:20053675}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein {ECO:0000269|PubMed:20053675}. Note=In a heterologous system, the final intracellular localization after exit from the endoplasmic reticulum is the prevacuolar compartment in the presence of ALA2 and the Golgi in the presence of ALA3.
Interaction partners:
- Phospholipid-transporting ATPase 2
- Phospholipid-transporting ATPase 3
- Phospholipid-transporting ATPase 6
- Phospholipid-transporting ATPase 1
- Probable phospholipid-transporting ATPase 12
- Defensin-like protein 90
- Probable phospholipid-transporting ATPase 4
- Probable phospholipid-transporting ATPase 7
Sequence:
MSSNTASSSAGAAGSGDSSAARKNSKRPKYSKFTQQELPACKPILTPGWVISTFLIVSVIFIPLGVISLFASQDVVEIVDRYDTECIPAPARTNKVAYIQGDGDKVCNRDLKVTKRMKQPIYVYYQLENFYQNHRRYVKSRSDSQLRSTKYENQISACKPEDDVGGQPIVPCGLIAWSLFNDTYALSRNNVSLAVNKKGIAWKSDKEHKFGNKVFPKNFQKGNITGGATLDPRIPLSEQEDLIVWMRTAALPTFRKLYGKIESDLEMGDTIHVKLNNNYNTYSFNGKKKLVLSTTSWLGGKNDFLGIAYLTVGGICFILALAFTIMYLVKPRRLGDPSYLSWNRNPGGR
Protein: Deoxyhypusine synthase (DHS) (EC 2.5.1.46) (P38791)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Interaction partners:
- Eukaryotic translation initiation factor 5A-1
- Eukaryotic translation initiation factor 5A-2
- Deoxyhypusine hydroxylase
- Ornithine decarboxylase
- S-adenosylmethionine decarboxylase proenzyme
- Spermidine synthase SPE3
- Putative pterin-4-alpha-carbinolamine dehydratase
- Ribosome biogenesis protein BRX1
Sequence:
MSDINEKLPELLQDAVLKASVPIPDDFVKVQGIDYSKPEATNMRATDLIEAMKTMGFQASSVGTACEIIDSMRSWRGKHIDELDDHEKKGCFDEEGYQKTTIFMGYTSNLISSGVRETLRYLVQHKMVDAVVTSAGGVEEDLIKCLAPTYLGEFALKGKSLRDQGMNRIGNLLVPNDNYCKFEEWIVPILDKMLEEQDEYVKKHGADCLEANQDVDSPIWTPSKMIDRFGKEINDESSVLYWAHKNKIPIFCPSLTDGSIGDMLFFHTFKASPKQLRVDIVGDIRKINSMSMAAYRAGMIILGGGLIKHHIANACLMRNGADYAVYINTGQEYDGSDAGARPDEAVSWGKIKAEAKSVKLFADVTTVLPLIVAATFASGKPIKKVKN