wanglab/gogpt-training-data huggingface dataset:
Protein: Pancreatic lipase-related protein 2 (PL-RP2) (Cytotoxic T lymphocyte lipase) (Galactolipase) (EC 3.1.1.26) (Triacylglycerol lipase) (EC 3.1.1.3) (P54317)
Organism: Homo sapiens (Human)
Function: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides. In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides. Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity. Can completely deacylate triacylglycerols. When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids. Hydrolyzes medium- and long-chain fatty acyls in galactolipids. May act together with LIPF to hydrolyze partially digested triglycerides. Hydrolyzes long-chain monoglycerides with high efficiency. In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity. In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:18702514, ECO:0000269|PubMed:19824014}. Zymogen granule membrane {ECO:0000250|UniProtKB:P54318}; Peripheral membrane protein {ECO:0000250|UniProtKB:P54318}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P54318}. Note=Localizes to neurite tips in neuronal cells. {ECO:0000250|UniProtKB:P54318}.
Interaction partners:
Sequence:
MLPPWTLGLLLLATVRGKEVCYGQLGCFSDEKPWAGTLQRPVKLLPWSPEDIDTRFLLYTNENPNNFQLITGTEPDTIEASNFQLDRKTRFIIHGFLDKAEDSWPSDMCKKMFEVEKVNCICVDWRHGSRAMYTQAVQNIRVVGAETAFLIQALSTQLGYSLEDVHVIGHSLGAHTAAEAGRRLGGRVGRITGLDPAGPCFQDEPEEVRLDPSDAVFVDVIHTDSSPIVPSLGFGMSQKVGHLDFFPNGGKEMPGCKKNVLSTITDIDGIWEGIGGFVSCNHLRSFEYYSSSVLNPDGFLGYPCASYDEFQESKCFPCPAEGCPKMGHYADQFKGKTSAVEQTFFLNTGESGNFTSWRYKISVTLSGKEKVNGYIRIALYGSNENSKQYEIFKGSLKPDASHTCAIDVDFNVGKIQKVKFLWNKRGINLSEPKLGASQITVQSGEDGTEYNFCSSDTVEENVLQSLYPC
Protein: Bax inhibitor 1 (BH3 domain-containing protein BXI1) (P48558)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Links the unfolded protein response and programmed cell death and mediates mitochondrial-dependent apoptosis. Induces cell death and disruption of the mitochondrial transmembrane potential via the mitochondrial phosphate carrier MIR1. Dispensible for starvation-induced autophagy.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21673967}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21673659, ECO:0000269|PubMed:21673967}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:21673659}; Multi-pass membrane protein {ECO:0000255}. Note=Translocated from predominantly vacuolar sites in healthy cells to mitochondria upon apoptosis induction. {ECO:0000269|PubMed:21673659}.
Interaction partners:
- Metacaspase-1
- Pro-apoptotic serine protease NMA111
- Cytochrome c isoform 2
- Mitochondrial nuclease
- Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial
- Apoptosis-inducing factor 1
- Cytochrome c isoform 1
- Dynamin-related protein DNM1
Sequence:
MSGPPPPYEEQSSHLYGQPASSQDGNAFIPEDFKYSTVVISCEPIIRQRFMHKVYSLLSCQLLASLSFCYWASVSTSLQNFIMSHIALFYICMVVSLVSCIWLAVSPRPEDYEASVPEPLLTGSSEEPAQEQRRLPWYVLSSYKQKLTLLSIFTLSEAYCLSLVTLAYDKDTVLSALLITTIVVVGVSLTALSERFENVLNSATSIYYWLNWGLWIMIGMGLTALLFGWNTHSSKFNLLYGWLGAILFTAYLFIDTQLIFRKVYPDEEVRCAMMLYLDIVNLFLSILRILANSNDDN
Protein: Verthandi, isoform B (A0A021WW32)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFYEHIILAKKGPLARIWLAAHWDKKITKAHVFETNIEKSVEGILQPKVKLALRTSGHLLLGVVRIYSRKAKYLLADCNEAFVKIKMAFRPGMVDLPEGHREANVNAITLPEVFHDFDTALPELNDIDIEAQFSINQSRADEITMREDYGSLSLSLQDDGFGDIGFEAETPEIIRCSIPSNINDKIFDNDVLENIESLDPHSLDAHADMPGSRLDGDGFGDSFGQPALFEDDLFGDPSQPVEQITKESTTVLNADDSDEDAIDNIHNVPSPATSLVNSIEDEKEENNLNGHASVSENVPMNEITLVQNEDEGFALAPLDVSMYKGVTKAKRKRKLIIDEIKNISGEEMKAQLADTSDILTTLDLAPPTKRLMYWKETGGVEKLFSLPSRSIPARALFGNYNRQLFSHSTFFEDFSSVVPMEILALEFYTKENENALIIFNKKGRKRKNDNMSNLFLDHVPDSVVQSLEAPEVLRANHKSLGVSTVSVEIVSKEQESISCQNELTFFDNMRSPDLLSLNEMEQFSSINELPLTPRNMNHEMGDDFNQGDSTPAGLDHGHATPQHGNIGEMDHDSVIPTKKTAVILNESVGTSVLSDNGVSKRTNNILKGWDNYEIPSFVGQGIRHAGHCYQQYH
Protein: Nestin (P86839)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells (By similarity). Required for brain and eye development.
Interaction partners:
Sequence:
MELLGVRQPFGPQFQEEKYQMLELNHRLESYLGRVKLLEEENKLLREEIHTLKSSRDPAGQRKAQEEALSQARRMMEEAWRKKDCVELEVENLMEDMEKVSFQRKKVKTAQAEAQRKLTESRKELEEERRAQIWLREKVGQLEKDLMLQMQVHQENMETMQASLKQTKQVLMAPQRVQATSIPDLGQEYGYKAAQAWQEAANNYQKQVGRLEESLNQTKANMTKIYQEKRESQRQVQHLAKELESTRIKRQMLEKHAMQQREEQKEELQHLQAQVNTLELEKDCLGQQIDSLMLDRQHLLQVKMSLGLEVATYRALLDSEGLRIDRPTPNKTSSTVFLDALSKPTGIQSTSQTTAASCLLSSSVSTSHRSIASSRSLLTSAAPSWTLTRGTPQRPPSSTSMTEKTEDHISEETKRSAEESVDQLQQEKVQQDWTLESTLPKTSAEPKPELQPEEIKVEDEANEPQQAHMVESKTDESELTSVPAEQQGSMSQTPETKSWAGHFNDPAEVSEDGKDEDTEVSVEMARISHAPKVAWEEIKSAVEDEKDDASEMDVRSEIISESHTFAYGDAENDSNTLTSSHISQNTNALASSFLEQGTLDSASYFGYEATNENLMKEEELDNVSNISEEVTEQLNSETEAAIDSINEWDRQEESEPENETKVMTSYFEVEEGEMSINTDTKDKTEDDIEREELEVTEREILVQSAGGMLGVDLPNDTDHQDEHNLPQIELNEDQSEAEEENQKEKQCDEDDSPNISASLKTDPGEGDSYSQEHTLADTRPLIRYKSDEETSHHIGETSDSEDEKERIDQGHLNEKRFNTMEDLTEEPDMEVTGKMRLEDLVSNEEAAADDVASVMFQKVSGDHESLDVVVQESERKGNLEKEDSGDADNMRDNKEEDVSVFEQNENQQLTEHQHVHTEQVEDKPVHSHETQEHVNTEFSSTFSERSQQEQLEESSLTMFEDEAATKEAEDSDVSMHTNIDLIDSRSLESEINGQPDIMTSDMANSECNSSEDESPNASQCFQNTSLLAAATPNEQPLTFTNEVSKADYVSDNNDVPEEVLSEEKSTDEPKASQIDDLENFNIWGESTSISDAAQTTHASMDEHSSISPVNENLESSNKIPSVAENIFGHFEEHLERSVESFPEKEVTVMDFENNDLGEEFQSKQMKSEIHSFFSTSLKQDFWSEGKMEMAATYDPAKTEDLNQAMVFGEEWREIGVQSANGDTKEEMEILKIRDDKQKDGQPAQSKIVQSDDSADEGDSWSSGDE
Protein: Paired box protein Pax-3-A (xPax3-A) (Paired-domain transcription factor Pax3-A) (Q645N4)
Organism: Xenopus laevis (African clawed frog)
Function: Probable transcription factor. Promotes both hatching gland and neural crest cell fates, two of the cell populations that arise from the neural plate border. Acts downstream of msx1 to induce the neural crest, cooperating with zic1 and mediating signals from both the wnt and fgf8 signaling pathways. Induction of hatching gland cell fate is independent of zic1.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P23760, ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00381}.
Interaction partners:
Sequence:
MTSLAGAVPRMMRPCPGQNYPRTGFPLEVSTPLGQGRVNQLGGVFINGRPLPNHIRHKIVEMAHHGVRPCVISRQLRVSHGCVSKILCRYQETGSIRPGAIGGSKPKQVTTPEVEKKMEEFKRDNPGMFSWEIRDKLLKDGVCDRNTVPSVSSISRILRSKFGKGDEEDMELDRKEQEESEKRAKHSIDGILRERAPVSPESEEGSDIDSEPDLPLKRKQRRSRTTFTAEQLEELERAFERTHYPDIYTREELAQRAKLTEARVQVWFSNRRARWRKQAGANQLMAFNHLIPGAFPPAAMPALPTYQLSETSYQPTSIPQAVSDPSNTVHRPQPLPPSSVHQSSLPSNPESSSAYCLPSGRHGFSSYTDSFVPPSGPSNPMNPAIGNGLSPQVMGLLTNHGGVPHQPQTDYALSPLTGGLEPSTAVSASCSQRLEHMKSLDSLSTSQSYCPTYSTSGYSMEPVTGYQYPQYGQSAFHYLKPDIA
Protein: Large ribosomal subunit protein uL4 (60S ribosomal protein L4) (Q54Z69)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein uL22
- Large ribosomal subunit protein eL15
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL27
- Small ribosomal subunit protein eS4
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL30
Sequence:
MTTRPFVQVFDAQNKVVGKVKLPNVLTTPIRPDLVNFVHTNLNKNARQAYGAAPYAGEQTSAESWGTGRAVARIPRVPGSGTHRSGQGAFGNMCRGGRMYGPNKTWRRWNRKVNVNQKRYAVVSALAASAVPALVMARGHRINGINEVPLVIANESVDTLQKTKAAVELLKKINAYADVTKVIDSKHIRAGAGKARNRRYKVRKGPLVVVSGKTTVSQALRNIPGVEVANVSRLNLLKLAPGGHLGRFIIWTKSAFEQLDSTFGTFAKSSAQKKGYTLPRPMIANADIVRLVNSDEIQAAVRASKVVVKRPTAPVRRSNPLKNLRAMIKLNPAAVSTRRTQVKSLKSKGIKVSKKNQLRAKLVAATFNQ
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A060Y6Z6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- 5'-AMP-activated protein kinase subunit beta-1
- AMP-activated protein kinase glycogen-binding domain-containing protein
- CBS domain-containing protein
- CBS domain-containing protein
- Protein kinase, AMP-activated, beta 1 non-catalytic subunit, b
- Association with the SNF1 complex
- Association with the SNF1 complex
- 5'-AMP-activated protein kinase subunit gamma-1
- 5'-AMP-activated protein kinase subunit gamma-1
- calcium/calmodulin-dependent protein kinase
Sequence:
MVTFVIVTVCSIIRIESSSNLLLFTSYCVEDKEARRLFQQIISGVDYCHRHMVVHRDLKPENVLLDHSKNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSCGVILYALLCGTLPFDDEHVPTLFKKIRGGVFYMPEYLTRPVASLLLLMLQVDPLKRATIKDIREHEWFKQDLPGYLFPEDLSYDSTVLDEEAVREVCDKFESTESEVMSSLYSGDPQDQLAVAYHLIIDNRRIMTQASEFYLASSPPQGSFMEDGMPLPPGVKPHPERMPPLLIDSPKASSCTLPAGCPQHHQSQTPGSEESQVAPGHQESEQTL
Protein: S-arrestin (48 kDa protein) (Retinal S-antigen) (S-AG) (Rod photoreceptor arrestin) (P15887)
Organism: Rattus norvegicus (Rat)
Function: Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO. May play a role in preventing light-dependent degeneration of retinal photoreceptor cells.
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P20443}. Membrane {ECO:0000250|UniProtKB:P20443}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20443}. Note=Highly expressed in photoreceptor outer segments in light-exposed retina. Evenly distributed throughout rod photoreceptor cells in dark-adapted retina (By similarity). Predominantly dectected at the proximal region of photoreceptor outer segments, near disk membranes. {ECO:0000250|UniProtKB:P08168, ECO:0000250|UniProtKB:P10523}.
Interaction partners:
- Rhodopsin
- G protein subunit alpha transducin 1
- Rhodopsin kinase GRK1
- Beta-2 adrenergic receptor
- G protein-coupled receptor kinase 4
- Retinol-binding protein 3
- Clathrin heavy chain 1
- Recoverin
Sequence:
MAACVKTNKSHVIFKKVSRDKSVTIYLGKRDYIDHVSQVEPVDGVVLVDPELVKGKKVYVTLTCAFRYGQEDIDVIGLTFRRDLYFSRVQVYPPVGAMSAPTQLQLSLLKKLGDNTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVDFEVKAFATDITDAEEDKIPKKSSVRLLIRKVQHAPPEMGPQPCAEASWQFFMSDKPLHLSVSLSKEIYFHGEPIPVTVTVTNNTEKVVKKIKVSVEQIANVVLYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGILVSYHIKVKLTVSGFLGELTSSEVATEVPFRLMHPQPEDPAKESVQDENLVFEEFARQNLKDTGENTEGKKDEDAGQDE
Protein: Chromodomain helicase DNA binding protein 8 (H0YJA4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XASEWPKDRVLINRIDLVCQAVLSGKWPSSRRSQEMVTGGILGPGNHLLDSPSLTPGEYGDSPVPTPRSSSAASMAEEEASAVSTAAAQFTKLRRGMDEKEFTVQIKDEEGLKLTFQKHKLMANGVMGDGHPLFHKKKGNRKKLVEYMEDRRKQKWQRCKKNNKAELNCLGMEPVQTANSRNGKKGHHTETVFNRVLPGPIAPESSKKRARRMRPDLSKMMALMQGGSTGSLSLHNTFQHSSSGLQSVSSLGHSSATSASLPFMPFVMGGAPSSPHVDSSTMLHHHHHHPHPHHHHHHHPGLRAPGYPSSPVTTASGTTLRLPPLQPEEDDDEDEEDDDDLSQGYDSSERDFSLIDDPMMPANSDSSEDADD
Protein: Inner membrane protein YdcZ (P76111)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- L-amino acid N-acyltransferase MnaT
- Uncharacterized protein YfdY
- UPF0410 protein YeaQ
Sequence:
MNQSLTLAFLIAAGIGLVVQNTLMVRITQTSSTILIAMLLNSLVGIVLFVSILWFKQGMAGFGELVSSVRWWTLIPGLLGSFFVFASISGYQNVGAATTIAVLVASQLIGGLMLDIFRSHGVPLRALFGPICGAILLVVGAWLVARRSF
Protein: Type III pantothenate kinase (EC 2.7.1.33) (PanK-III) (Pantothenic acid kinase) (P9WPA1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01274}.
Interaction partners:
- Pantothenate synthetase
- Aspartate 1-decarboxylase
- Conserved hypothetical alanine and leucine rich protein
- Lysine--tRNA ligase 1
- Phosphopantetheine adenylyltransferase
- Pantothenate kinase
- Coenzyme A biosynthesis bifunctional protein CoaBC
- Conserved transmembrane protein
- 
- Uncharacterized protein Rv2003c
Sequence:
MLLAIDVRNTHTVVGLLSGMKEHAKVVQQWRIRTESEVTADELALTIDGLIGEDSERLTGTAALSTVPSVLHEVRIMLDQYWPSVPHVLIEPGVRTGIPLLVDNPKEVGADRIVNCLAAYDRFRKAAIVVDFGSSICVDVVSAKGEFLGGAIAPGVQVSSDAAAARSAALRRVELARPRSVVGKNTVECMQAGAVFGFAGLVDGLVGRIREDVSGFSVDHDVAIVATGHTAPLLLPELHTVDHYDQHLTLQGLRLVFERNLEVQRGRLKTAR
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (A0A140VJZ4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAVLLLFPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFLEESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHLYELDGRKPFPINHGETSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA
Protein: GPI-anchored adhesin-like protein (Q9M2F2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pre-mRNA-splicing factor 38
- Protein STABILIZED1
- Pre-mRNA-processing protein 40C
- Microfibril-associated protein-like
- Microfibrillar-associated protein-like protein
- Sm-like protein LSM2
- Sm-like protein LSM8
- Sm-like protein LSM4
- tRNA
- At2g32600/T26B15.16
Sequence:
MDVVERKRPRGAFLNLFDWHGKSRKKLFSSNLSQLSEESKQAKENVQNPSITPHSVFEVDQSVKNPTYNPRSDSSCCASSVTSDDGNVVRASVVARLMGLEGLPLPNVLEPRVNPDLDPYFLRSSRQANTWDANVDRQSDFDGVSWDHLDSRTSKGPRKRMIERFQTETLPPRSAKPISVTHNKLLSPIRNPGFVPSRNPAYVMEAASRMIEQSPRMIARTRMVSSSDSSSPVPLRIRDLKEKLEAAQKASTSVPQISNDTRNSRYLRGDQNEKKTTVLGKNSYDALKGGEVKPPSFAAQAKVSSNQKQDSLSMSSSGNKRMSSGQKEKVEAKNRAVKSQNSSKGSSLSTGKNVLRQNNQKQNCRDNQQSRRVMNKVVNKVLVESGSISKSSGFTMSSAEKPTSLPLSRKKSLPRSKKPRNGVQESGIYEDKRIKRGEKSIKCNISIDGDSSTSKDDQKRDMDVISFTFSSSIKGLSSPHSQGTKQDADSAIRFNVIGGDSLNALLEQKLRELTTKIESSSSSLIQEEPLSSISKDRANAMISSPSKYSGLTQSSLDRVLTESESVSDCTSFFNSQKVQKQKVIQGEEQEVSSITTLTEADDFALSCSKSISDCRHDREYGMKQSSSDQELTWGSSNESQHTLDETESATLDWELEYITEILNSGQLMFQDFASGTTTNESLLPSSLFDEMERSRGAATSMKTERKALFDCVNQCLAVKFERMLIGSCKGMMMSGGILLEHRDLLAEEVNREVKGLKKMREMMIDELVDHDMSCFEGRWIGYEREMFEEGIDMEGEIVSALVDDLVSDILSTSVLKRSLL
Protein: ORM1-like protein 1 (Adoplin-1) (Q9P0S3)
Organism: Homo sapiens (Human)
Function: Negative regulator of sphingolipid synthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12093374}; Multi-pass membrane protein {ECO:0000269|PubMed:12093374}.
Interaction partners:
- Serine palmitoyltransferase 1
- Serine palmitoyltransferase 3
- Serine palmitoyltransferase 2
- Alpha-1-acid glycoprotein 1
- Alpha-1-acid glycoprotein 2
- Serine palmitoyltransferase small subunit A
- Serine palmitoyltransferase small subunit B
Sequence:
MNVGVAHSEVNPNTRVMNSRGMWLTYALGVGLLHIVLLSIPFFSVPVAWTLTNIIHNLGMYVFLHAVKGTPFETPDQGKARLLTHWEQLDYGVQFTSSRKFFTISPIILYFLASFYTKYDPTHFILNTASLLSVLIPKMPQLHGVRIFGINKY
Protein: Trihydrophobin (CFTH1) (Q9UVI4)
Organism: Claviceps fusiformis (Ergot fungus)
Function: Self-assembles at hydrophilic-hydrophobic interfaces on hyphal surface. Reduces water surface tension dramatically upon assembly at the water-air interface. Probable role in growth of aerial hyphae.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:10336622}.
Interaction partners:
Sequence:
MKFLAAASLLVASTLAVPTSSGGSCRPRPPPGGGNGGNGGNGGNGGNGYQPCPAGLYSNPQCCATDVLGVADLDCKNPSSAPMSGDNFKSICNAVGQQAKCCVLPVAGQAVLCQDSINGGGNGGNNGGNGGNNGGNGGNNGGNTDYPGGNGGNNGGNNGGNNGGNNGGNNGGNNGGNNGGNNGGNNGGNNGGNGGNGGNGYQACPAGLLYSNPQCCSTGVLGVADLDCKNPSSAPTSGDDFQKICANGGQQAQCCSIPVAGQAVLCQPAIGGGNPGGNGGNNGGNGGNGGNNGGNNGGNGDYPGGNGGNNGGSNGGGNGGNGGNGGSFKCPSGLYSVPQCCATDVLGVADLDCGNPSRQPTDSSDFASVCAAKGQRARCCVLPLLGQAVLCTGA
Protein: GH06023p (RNaseP protein p30, isoform A) (RNaseP protein p30, isoform B) (Q9VPM0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ribonuclease P/MRP subunit p21, isoform A
- FI18256p1
- Ribonuclease P/MRP protein subunit POP5
- Ribonuclease P protein subunit p29
- FI09323p
- Ribonuclease P protein subunit p20
- H/ACA ribonucleoprotein complex subunit 2
- NHP2-like protein 1 homolog
- Ribonuclease P/MRP subunit p14 a
- GEO10372p1
Sequence:
MEQTRPFYDFSIPYNKDDSVLRALLNELVETGYKTVAIDQSFDHSKKDPGKRGSEMFPEPHKIEHLRKEFQDKLRILQRITILYVDVNVAHAMSVSHNLRKFNLIAGQPKTDAALTHCCTAFNGDLITFDPVAGSRLLVNRKAYQVAVRRGMFFEIKYAPSICDSNNRKDMIKIAQNYCTKGKSKNVIFSSGAAHEFQLRGPYDVANLAFIFGLSEDQGKNAVDGHCRELFLKAEARRLGKTIMFLKGNGPIIYSDSSEDEKSTEDEMKGLKPQIGKADAFEVKDGTEHAIKRLKVA
Protein: Adhesion G protein-coupled receptor V1 (A0A8I6A7V4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
TSVAGMVSSLLLVYLSALVVSFVCGEAEIRFTGQTEFFVNETSTTVIRFVIERIGEPANVTAIVSLDGEDTGDFFDTYAAAFIPAGGTNRTVYIAVCDDDLPEPDETFTFQLTLQKPSANVKLGWPRAAAVTILSNDNAFGVISFSTPSSITVTEPRSRNASVSLTLIREKGTYGMVTVTFDVSGGSNPPEEDLSPVRGNITFPPGRATIIHNLTVLDDEVPENDEMFLIQLRSVGGGAEINASRSSVEIIVKKNDSPVKFLQSVYVVPEDDHVLTIPVVRGKDNNGHPIGSDESQVSVRYKVVTGDSTAHAQQNVDFIDLQPDTTLVFPPFVHESHLKFQIIDDLIPEIAESFHIMLLKNTLQGDAVLMDPSTVQVTIKANDKPHGVLSFNSILFERPVVIDEDTASRFEEITVVRNGGTHGNVSVNWVLTRNSSDPSPVTADLSPASGTLQFAQGQMLALIPLAIIDDELPEEAEAYLLTILPHTIQGGAEVSEPAQLLFYVQDSDDVYGEIALFPVESQRIESSPSERSLSLSFTRLGGSKGDLKVIYSALYIPAGAVDPLRAKDGILNTSRRNTLLFPEQNYQVTAKLPIRNDAFLQNGAHFLVQLEAVELVNIVPLIPPVSPRFGEIRNTSLLVTPAIANGEIGFLSNLPIILHEPNDSAAEVVSIPLHRDGTDGQATVYWSLRPSGFNSKAVTVDDTGPFNGSVVFLSGQSDTSINITVKGDDTPELNETVTLSLDRVSVDSDVLKSGYTSRDLIILENDDPGGIFEFSYDSRGPYVIKEGDAVELRIARSRGALVKQFLRFHVEPRDSNEFYGNTGVLEFSPGEREVVITLLTRLDGMPEVPGSGLLPCPFERLTVSGF
Protein: Calmodulin-regulated spectrin-associated protein 1 (D3Z8E6)
Organism: Rattus norvegicus (Rat)
Function: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization. Specifically recognizes growing microtubule minus-ends and stabilizes microtubules (By similarity). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (By similarity). In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of minus-end microtubules without significantly affecting the polymerization rate: binds at the very tip of the microtubules minus-end and acts as a minus-end tracking protein (-TIP) that dissociates from microtubules after allowing tubulin incorporation (By similarity). Through interaction with spectrin may regulate neurite outgrowth.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5T5Y3}. Note=Associates with the minus-end of microtubules. In contrast to CAMSAP2 and CAMSAP3, does not form stretches of decorated microtubule minus-ends. {ECO:0000250|UniProtKB:Q5T5Y3}.
Interaction partners:
Sequence:
MVDAGGRSAAEGWRRMEAPPEGADLVPLDRYDAARAKIAANLQWICAKAYGLDNIPEDLRDPFYIDQYEQEHIKPPVIKLLLSSELYCRVCSLILKGDQAATLQGHQSVIQALSRKGIYVMESDDTPVTDADLSQAPIKMSGHMAMVDALMMAYTVEMISIEKVVASVKRFSTFSASKELPYDLEDAMVFWINKVNLKMREITEKEVKLKQQPLESPAHQKPGLEHAVMHCMLEPVDFARVVRYRREHLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHLNKCFYLTLEDMLYAPLVLKPNVMVFIAELFWWFENVKPDFVQPRDIQELKDAKTVLQQKSSRPPVPISNATKRSFLGSPAAMSPADLPPSTQPLTEGSHRYHLHSEEPECLGKGASTFSPSHPLLPLRQKQQKVSQAEEIPDQRHRSNSLTRADGQPRGAAIAWPDKKNRPVSQPTSFALHHAASCDVDPSSGDSISLARSISKDSLASNIIHLTPQNQPHPSAGKTNGKSLLSNVNIEDDEEEELVAIIRTDVSPHSPEIPRTSPQAPGLVASIRSPQRQADTLESKPDSFYLEPLMPAVLRPAKEKQIITKEDERGEGRPRTIMAKRPSEGSQPLVRKKVTGSHGSRDLNRTFTPIPCSEFAASIDPTEVGPQSTEATGEGQPLALGRFDPVPQGQVADGFFLHVGRAEEDEGRWYVGSQSPSSHDSEPWTILRQDSDSDVVDVEDAEQDFIGEDHPVVIPRYAGEEESAKLQEDMKVKEHEDKDDASGRSSPCLSTTSQLSSMSMASGSVKMTSFAERKLQRLNSCETKSSTSSSQKTTPDASESCPAPLTTWRQKREQSPSRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKKGKADGAPQPLRPEHFTKEFTQHNGEDLDDGTCKTEGFLVKEEQRDLSDSQDVAFVQLHKPRDPATLHDGEKHRVISAALLEDSVGEVDVNECDLSIEKLNETISTLQQAILKISQQQEQLLMKSPTVPTSGTKNNCQDQKVKAPVHFVEPLSPTGVPGHRKPPRLGQGRNSRSGRPAELKVPKDRQQGCSRSKTPTPSVETLPHSRSLPPSTHPRSPLDPGGELPEKCLFDSYRLHDESNHRTFGLSSCKDANIVSEQMNFKEGLDTSVQEAELSSSAITGKEHTPMEEPLRSKASLIEVDLSDLKAPDEDGEVVGHESSLELGGESDQKPGVGFFFKDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEEQGLGKPKSKPKKPRPKSVHREESCSDSGTKCSSTPDNLSQTHSGSSLSLASAATTEPESVHSGGTPSHRVESLEALPILSRNPSRSTDRDWETASAASSLASVAEYTGPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGTGPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKRPTVPKKTQTRK
Protein: Myelodysplastic syndrome 2 translocation-associated protein (Q8NDY4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLQAADFIERTETAGELSRGLIGVLSSQISWCLLNVNLSKLPTRLQRLSCSVLNSSPAMRGGARGRPQLTLERPLRPGCRLHSCSEAEKGGFVRRKEIILFPPCEDPARGWLSANPGREPSPGICWHLNLGLPSLHNCEE
Protein: Fumarate hydratase, mitochondrial (Fumarase) (EC 4.2.1.2) (EF-3) (P97807)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. Experiments in different species have demonstrated that specific isoforms of this protein act in defined pathways and favor one direction over the other (Probable).
Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:P07954}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P07954}. Nucleus {ECO:0000250|UniProtKB:P07954}. Chromosome {ECO:0000250|UniProtKB:P07954}. Note=Translocates to the nucleus in response to DNA damage: localizes to DNA double-strand breaks (DSBs) following phosphorylation by PRKDC. {ECO:0000250|UniProtKB:P07954}.
Interaction partners:
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Malate dehydrogenase, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Malate dehydrogenase, cytoplasmic
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Citrate synthase, mitochondrial
- Citrate synthase
- NAD-dependent malic enzyme, mitochondrial
- NADP-dependent malic enzyme
Sequence:
MYRALRLLARSRRLLRVPSAGAAVSGEATTLPRCAPNVARMASQNSFRVEFDTFGELKVPTDKYYGAQTVRSTMNFKIGGATERMPIPVIQAFGILKRAAAEVNQEYGLDPKIASAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAAVEVHKVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMVRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTAACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTDNCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK
Protein: Semenogelin-2 (Semenogelin II) (SGII) (Q02383)
Organism: Homo sapiens (Human)
Function: Participates in the formation of a gel matrix (sperm coagulum) entrapping the accessory gland secretions and ejaculated spermatozoa.
Subcellular location: Secreted.
Interaction partners:
- WAP four-disulfide core domain protein 12
- Semenogelin-1
- Prostate-specific antigen
- Elafin
Sequence:
MKSIILFVLSLLLILEKQAAVMGQKGGSKGQLPSGSSQFPHGQKGQHYFGQKDQQHTKSKGSFSIQHTYHVDINDHDWTRKSQQYDLNALHKATKSKQHLGGSQQLLNYKQEGRDHDKSKGHFHMIVIHHKGGQAHHGTQNPSQDQGNSPSGKGLSSQCSNTEKRLWVHGLSKEQASASGAQKGRTQGGSQSSYVLQTEELVVNKQQRETKNSHQNKGHYQNVVDVREEHSSKLQTSLHPAHQDRLQHGPKDIFTTQDELLVYNKNQHQTKNLSQDQEHGRKAHKISYPSSRTEERQLHHGEKSVQKDVSKGSISIQTEEKIHGKSQNQVTIHSQDQEHGHKENKISYQSSSTEERHLNCGEKGIQKGVSKGSISIQTEEQIHGKSQNQVRIPSQAQEYGHKENKISYQSSSTEERRLNSGEKDVQKGVSKGSISIQTEEKIHGKSQNQVTIPSQDQEHGHKENKMSYQSSSTEERRLNYGGKSTQKDVSQSSISFQIEKLVEGKSQIQTPNPNQDQWSGQNAKGKSGQSADSKQDLLSHEQKGRYKQESSESHNIVITEHEVAQDDHLTQQYNEDRNPIST