wanglab/gogpt-training-data huggingface dataset:
Protein: Gem (nuclear organelle)-associated protein 5 (Gem-associated protein 5 isoform X1) (E9QH84)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Gem-associated protein 2
- Gem
- Probable ATP-dependent RNA helicase DDX20
- Gem
- Gem
- Survival motor neuron protein 1
- Gem
- Organic solute carrier partner 1a.
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D3
Sequence:
MHERHLPASPNWYCSRCSDINSKGVFGFGAKNTVYLLNVTAASPAVTGELAGHTERVSGFAFCPNEGQEHICCSTSDDKKVKIWDAEQKILLKEHNVHQNTITAVHWSPVQKLLLVTGDEKGIVVCYWFSSNDTQSFFPEPRTIFCLSCSPHDENLIAVGYKDGMIAVIDISKKGEVVHRLRGHDDEIHALAWCPRPREEPLYGRSEDNADGSSGVTEGAEAGCYLASGSRDQTMRIWSTARRKGVMTLKLPFLKRRGAGVDPTVKERLWLTVHWPKERPSQIVSSCFGGEIVVWDLMKSGKQKWSLLGSSSDGQNHSRIVFNMSSFRCGDRELLLSTSMDREIKCWDLESLECCWTLPTLGGFVYCLSFSPVGTGCLALGVGDSMIRVWNTLSIQNQYDIKTFWQGIKSKVTALAWHPLKEGSLAFGTDDGKVGIYEVYSNRPPQISSTYHRRTVYSLSWGPPLPPMSFGGAGDKPAYSLYSCAGEGVIFQHDPWKLSGEASNIDKLIRDTNNIKHKMPPHTDLSWKPDGSILAIGNEDGSIEVLKAPMLKLLCTVQQHHKIINSLRWHHQHSSQNELQYLLASGSSNATIYIHDLRSAVESPSESPVSVTEPFRTLSGHTNKITDLAWSPHHDGHLVTVCYDGTAQVWDVLKEEPVCNYRGHSGRLLCVQWSAVHPDLIWTGGDDFTLQEWAVSKQEHITPPKSKKRTEMEKKRVPQKKPKKKKKAPGKGGMKAEESEMPLGEEVKGAAGSGAEEGQSDNEEEEEEKEYTDAPSVTGRSRDSSVDTRASDRLHNGEKFSNAVKKEVKEEKKRDKIDLSLKKRKPRSILPLSTSMDHRPKDELQQDCLTLAAVRHSHGRSRTCVPGAGDHIQLGLFTDRDALYRMMQEEEESHVEAAHYDSVLYLRLWRGDLIGALNLAMEKGELTDHLLSLAPMAGYQVWLRTVEAYVKQLCHHEQFLKAASHLLSIHKLYEAISLLKSHQFYREAIALARARLQPEDPVLKDLYMSWAAVLEKDGHYATAAKCYLATDSSFDAAKVIGKKGDVTSLKTAAHLAHITGESELALSLSLRCAKDLIATQDWTAAQDVLRTQDSLLGHRLVFSVNEILTQRLADTDVVSWSSSSSHWWSSSREEVFFSAVLRVWQREFGVDPADHHKLKTLHQQLKAIENPPHTTTGPVKQLLSHISLDVTLCALSELLCDWPSVVEELLRALSRASAAGSFTLMAELSLLLFPHGLESVALYKQKLDPSDERSLAISQSIEAFICYPLMYEKWWTSTSTNNSISNGHRLTLTDGDEEKCNGEAQSDGFWKILLSEAHADLQANQRAIAEIQKRVSSLIQQHSRCKDPETALEGSAGGTGSESLSALTAQVAEHHKALAAVPEHIRKYPFPDVLECCIVLLYMEKHFNLIPQHICSEATALLRKYGTAESLSKAVRRLIH
Protein: FLR-1 (G5EGI5)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Glycoprotein Hormone
- Serine/threonine-protein kinase flr-4
Sequence:
METETESERIYLQLYDYETKEFSGLTTYHGLVRIYNSNTWPSRIFWVVVVLSCLSLFMIHSGYLLLGYHAKPTLFQTNTIVPMNGLLFPEVTICNLNPLNTTKLEELNISKSTWTYIFGYFDEITTSEHKSTKLGEEQFLEIMNNYQELTKQEFNVKNFLKSVSKSCEETFISCSFGREKLHNCCEHVTTEMTEVGVCFRLSNVNKKYRQWYSGNGFGWEFVLNGNNEIDDHADSLDFEPDRGFLIMVHESEKYPKINSYGVAVSPDSQLHAAISMKNISLLDKANWGSCSKGWNRNDTDVPYTATHCEIDCKLRKVRNLCGCSPLAYSARESGSNDTICTPYQIQQCFRKVRGLDNRWEDECDCPSECNMLEFDVTNSYSDLDGRSRGLSSSKVESDISHVSLYFSHVAYERIEQQKQLQTADLLSNIAGSMGLFLGMSTVTLLEIFIYLFKSVWGTVNSTRQQQFVDAVAEEEKERSESIVIIQNGRNDDMDDQKPSRFPGADRKLSGNSIHIHLDRRNSRMIRGGDLSAASRGSVSIPSQLLSPLSRHNRQSISYGQLGRKVSAIGIPLQPNHDTVESGTSLMPPKSPIRRCSTSTTPSMLTRKLSFASQQSDPAQPAHQSRKVSTSSIFKSQLI
Protein: UDP-glycosyltransferase 85A1 (EC 2.4.1.-) (Cytokinin-O-glucosyltransferase 2) (Zeatin O-glucosyltransferase 2) (AtZOG2) (Q9SK82)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the O-glucosylation of trans-zeatin and dihydrozeatin. Also active in vitro on cis-zeatin. Not active on N-glucosylated substrates.
Interaction partners:
Sequence:
MGSQIIHNSQKPHVVCVPYPAQGHINPMMRVAKLLHARGFYVTFVNTVYNHNRFLRSRGSNALDGLPSFRFESIADGLPETDMDATQDITALCESTMKNCLAPFRELLQRINAGDNVPPVSCIVSDGCMSFTLDVAEELGVPEVLFWTTSGCAFLAYLHFYLFIEKGLCPLKDESYLTKEYLEDTVIDFIPTMKNVKLKDIPSFIRTTNPDDVMISFALRETERAKRASAIILNTFDDLEHDVVHAMQSILPPVYSVGPLHLLANREIEEGSEIGMMSSNLWKEEMECLDWLDTKTQNSVIYINFGSITVLSVKQLVEFAWGLAGSGKEFLWVIRPDLVAGEEAMVPPDFLMETKDRSMLASWCPQEKVLSHPAIGGFLTHCGWNSILESLSCGVPMVCWPFFADQQMNCKFCCDEWDVGIEIGGDVKREEVEAVVRELMDGEKGKKMREKAVEWQRLAEKATEHKLGSSVMNFETVVSKFLLGQKSQD
Protein: Monoacylglycerol lipase ABHD2 (EC 3.1.1.23) (2-arachidonoylglycerol hydrolase) (Abhydrolase domain-containing protein 2) (Acetylesterase) (EC 3.1.1.6) (Lung alpha/beta hydrolase 2) (MmLABH2) (Triacylglycerol lipase) (EC 3.1.1.79) (Q9QXM0)
Organism: Mus musculus (Mouse)
Function: Progesterone-dependent acylglycerol lipase that catalyzes hydrolysis of endocannabinoid arachidonoylglycerol (AG) from cell membrane. Acts as a progesterone receptor: progesterone-binding activates the acylglycerol lipase activity, mediating degradation of 1-arachidonoylglycerol (1AG) and 2-arachidonoylglycerol (2AG) to glycerol and arachidonic acid (AA). Also displays an ester hydrolase activity against acetyl ester, butanoate ester and hexadecanoate ester. Plays a key role in sperm capacitation in response to progesterone by mediating degradation of 2AG, an inhibitor of the sperm calcium channel CatSper, leading to calcium influx via CatSper and sperm activation (By similarity). Involved in acrosomal reaction (Probable). May also play a role in smooth muscle cells migration.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P08910}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P08910}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:26989199}. Note=Absent from the sperm flagellum. {ECO:0000269|PubMed:26989199}.
Interaction partners:
Sequence:
MNAMLETPELPAVFDGVKLAAVAAVLYVIVRCLNLKSPTAPPDLYFQDSGLSRFLLKSCPLLTKEYIPPLIWGKSGHIQTALYGKMGRVRSPHPYGHRKFITMSDGATSTFDLFEPLAEHCVGDDITMVICPGIANHSEKQYIRTFVDYAQKNGYRCAVLNHLGALPNIELTSPRMFTYGCTWEFGAMVNYIKRTYPQTQLVVVGFSLGGNIVCKYLGETQANQEKVLCCVSVCQGYSALRAQETFMQWDQCRRFYNFLMADNMKKIILSHRQALFGDHVKKPQSLEDTDLSRLYTATSLMQIDDNVMRKFHGYNSLKEYYEEESCMRYLHRIYVPLMLVNAADDPLVHESLLTIPKSLSEKRENVMFVLPLHGGHLGFFEGSVLFPEPLTWMDKLVVEYANAICQWERNKSQCSDTEQMEAELE
Protein: Phospholipase A2 acanmyotoxin-3 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (P85061)
Organism: Acanthophis sp. (strain Seram) (Seram death adder)
Function: Snake venom phospholipase A2 (PLA2) that has myotoxic activity but no significant neurotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000269|PubMed:16242671}.
Interaction partners:
Sequence:
NLLQFAFMIRQANKRRRPVIPYEEYGLYYM
Protein: PRELI domain-containing protein 1, mitochondrial (Px19-like protein) (Q8R107)
Organism: Mus musculus (Mouse)
Function: Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane. Regulates the mitochondrial apoptotic pathway in primary Th cells. Regulates Th cell differentiation by down-regulating STAT6 thereby reducing IL-4-induced Th2 cell number. May be important for the development of vital and immunocompetent organs (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14640972}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q9Y255}.
Interaction partners:
- TP53-regulated inhibitor of apoptosis 1
- Phosphatidate cytidylyltransferase, mitochondrial
- PRELI domain containing protein 3A
Sequence:
MVKYFLGQSVLRSSWDQVFAAFWQRYPNPYSKHVLTEDIVHREVTPDQKLLSRRLLTKTNRMPRWAERLFPANVAHSVYILEDSIVDPQNQTMTTFTWNINHARLMVVEERCVYCVNSDNSGWTEIRREAWVSSSLFGVSRAVQEFGLARFKSNVTKTMKGFEYILAKLQGEAPSKTLVETAKEAKEKAKETALAATEKAKDLANKAATKQQQRQLV
Protein: Sodium-dependent proline transporter (Solute carrier family 6 member 7) (Q6PGE7)
Organism: Mus musculus (Mouse)
Function: Brain specific sodium (and chloride)-dependent proline transporter. Terminates the action of proline by its high affinity sodium-dependent reuptake into presynaptic terminals.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:Q99884}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Hairy and enhancer of split-related protein HELT
Sequence:
MKKLQEAHLRKPITPDLLMTPSDQGDVDLDVDFAADRGNWTGKLDFLLSCIGYCVGLGNVWRFPYRAYTNGGGAFLVPYFLMLAICGIPLFFLELSLGQFSSLGPLAVWKISPLFKGAGAAMLLIVGLVAIYYNMIIAYVLFYLFASLTSNLPWEHCGNWWNTELCLEHRGPKSGNGVLPLNLSSTVSPSEEYWSRYVLHIQGSQGIGRPGEIRWNLCLCLLLAWVIVFLCILKGVKSSGKVVYFTATFPYLILLMLLVRGVTLPGAWKGIQFYLTPQFHHLLSSKVWIEAALQIFYSLGVGFGGLLTFASYNTFHQNIYRDTFIVTLGNAITSILAGFAIFSVLGYMSQELGVPVDQVAKAGPGLAFVVYPQAMTMLPLSPFWSFLFFFMLLTLGLDSQFAFLETIVTAVTDEFPYYLRPKKAVFSGLICVAMYLMGLILTTDGGMYWLVLLDDYSASFGLMVVVITTCLAVTRVYGIQRFCRDIHMMLGFKPGLYFRACWLFLSPATLLALLVYSIVKYQPSEYGSYRFPAWAELLGILMGLLSCLMIPAGMLVAVLREEGSLWERLQQASRPAMDWGPSLEENRTGMYVATLAGSQSPKPLMVHMRKYGGITSFENTAIEVDREIAEEEEESMM
Protein: Calponin-homology (CH) domain-containing protein (C8V0A2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Actin, gamma
- Actin-related protein
- F-actin-capping protein subunit beta
- Calponin-homology domain protein
- Arp3 homolog
- Arp2 homolog
- Actin cytoskeleton-regulatory complex protein SLA1
- Twinfilin
Sequence:
MNVIKIQRKYPQFEQGEIFALQDAFRKLDVDDKGYLDEGTVIKATQQSERQPYDIVRQTLKEVELDSSRRVELEDYVDLIAKLRSGSTQSVPVRDPVSAAAPGAARHVSKGSVGGKIHVQGSSSNVTHTINEDERTEFTRHINAVLAGDPDIGHLLPFPTDTFEMFDKCKDGLVLAKLINDSVPDTIDERVLNKPGRKLKELNAFHMTENNNIVINSAKGIGCSVVNIGSGDIIEVREHLILGLIWQIIRRGLLGKIDIKLHPELYRLLEEDETLEQFLRLPPEQILLRWFNYHLKNAQWPRRVTNFSADVKDGENYTVLLSQLAPELCSRQPLQTRDLLQRAEEVLGNAEKLNCRKFLTPTSLVAGNPKLNLAFVANLFNTIPGLDPITEEEKLEVEDFDAEGEREARVFTLWLNSLDVQPAVNSLFDDLRDGTILMQAYDKVIPHSVNWRHVNKPPASGQEMMRFKAVENTNYAIELGKHHGFSLVGVQGADITDGQRTLTLGLVWQLMRRDITNTLSSLASRLGKHEITDSEMIKWANDMTRKGGRSSSIRSFKDQSIGSGVFLLDVLNGMKASYVDYDLVTPGQTDEQAYANAKLSISIARKLGATIWLVPEDICQVRSRLVTTFIGSLMATYEKM
Protein: Uncharacterized ABC transporter ATP-binding protein YadG (P36879)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Inner membrane transport permease YadH
- Probable multidrug ABC transporter permease YbhS
- Thiamine import ATP-binding protein ThiQ
Sequence:
MTIALELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKTSGRVSVFGYDLEKDVVNAKRQLGLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAYIRSEKYLKQLDLWGKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKALLAKLKSETFILDLAPKSPLPKLDGYQYRLVDTATLEVEVLREQGINSVFTQLSEQGIQVLSMRNKANRLEELFVSLVNEKQGDRA
Protein: RNA-binding protein RMD9, mitochondrial (Q5A2V2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Binds the 3'-UTR of mitochondrial mRNAs (By similarity). Involved in the processing or stability of mitochondrial mRNAs (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P53140}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53140}; Matrix side {ECO:0000250|UniProtKB:P53140}.
Interaction partners:
- Uncharacterized protein
Sequence:
MFRLIASGAQQGLRPSLISKVKPPTTTTTTSTTSKFTSTTQHFPFENNNLLGYQVRNNSSQAGVASEPKISLPETDVYQQKLLKYNIKKHEPYHLKFNPKTKNQRNNDSASSFSIDEFSQLLQDETFRNQLNEKHLFVYASNLYSGTINSRRARLNKSKNRDKDQRSAFREDMTLQSAVLNLTEIISTGELNSVLSARTLFKVFGTLLQFKLNDEIVNLWETGVNSDVGKLYLAHEVLSIVIQVGHETRRFNYDEIKQIYEMSVKEDKTVHPYLSDRMGQVAVMEGDYVTALDALESLMNLYEQNPNEKSVLGALAQIHLSFIGHSKDLAIAERFFEKGLQKEGLPYSVIMKAPYMTSFLSNCIAGGYSMEEVIDFWRRISKHYLEQDFDLISSQSTLHAGFFKSFFEKYPEPSKEAIDLLNLAIESAPKVNEVLLNTLISNLPWADKEIFNKLLNLYQEKNVTKSIVSHRIILKQSKQIEYTNEEILQLWNELLGKLDEAGYTYIANADWSALRASTMFSGKFSYQRTGLYLSVLGKYKDYMQNNFAAIQFLRNWVRDANAYRLISKITLEENPQFDGAIKVDIPEFDSLRPNINYREVTKQVTDADPRLLE
Protein: Uncharacterized protein ZK1320.2 (Q09364)
Organism: Caenorhabditis elegans
Interaction partners:
- NIM-2 protein
- VWFA domain-containing protein
- C-type LECtin
- VWFA domain-containing protein
- Pathogenesis-related protein 5-like
- C-type lectin domain-containing protein 87
- Uncharacterized protein ZK1320.3
Sequence:
MKLLLLACLAVPAIFAQQTSAPGGNLCNYTPVGDESTQDAVPIQDFRSSGLDFVRPNWCITHCADRKSVKVAARFQFANQSTAVPTYNVRRHYTRKSGVKVHAELISGTPTKRDDDDFNFCIDDTVSATIDTVVKTYNDIETMSEALNFYINKPGWAYVIYDMGVPPSVIGTDNVKQDMNYCEKFAQKQMPDGTWGLYQVFAGLIKAN
Protein: tRNA-splicing endonuclease subunit Sen15 (SEN15 homolog) (HsSEN15) (tRNA-intron endonuclease Sen15) (Q8WW01)
Organism: Homo sapiens (Human)
Function: Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events.
Subcellular location: Nucleus {ECO:0000305}. Nucleus, nucleolus {ECO:0000305}. Note=May be transiently localized in the nucleolus. {ECO:0000305}.
Interaction partners:
- tRNA-splicing endonuclease subunit Sen2
- tRNA-splicing endonuclease subunit Sen54
- tRNA-splicing endonuclease subunit Sen34
- Polyribonucleotide 5'-hydroxyl-kinase Clp1
- Cleavage stimulation factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 4
- Cleavage and polyadenylation specificity factor subunit 1
Sequence:
MEERGDSEPTPGCSGLGPGGVRGFGDGGGAPSWAPEDAWMGTHPKYLEMMELDIGDATQVYVAFLVYLDLMESKSWHEVNCVGLPELQLICLVGTEIEGEGLQTVVPTPITASLSHNRIREILKASRKLQGDPDLPMSFTLAIVESDSTIVYYKLTDGFMLPDPQNISLRR
Protein: Proto-oncogene Mas (P04201)
Organism: Homo sapiens (Human)
Function: Receptor for angiotensin 1-7 (By similarity). Acts specifically as a functional antagonist of AGTR1 (angiotensin-2 type 1 receptor), although it up-regulates AGTR1 receptor levels. Positive regulation of AGTR1 levels occurs through activation of the G-proteins GNA11 and GNAQ, and stimulation of the protein kinase C signaling cascade. The antagonist effect on AGTR1 function is probably due to AGTR1 being physically altered by MAS1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16611642}; Multi-pass membrane protein {ECO:0000269|PubMed:16611642}.
Interaction partners:
- Angiotensinogen
- Pro-FMRFamide-related neuropeptide FF
Sequence:
MDGSNVTSFVVEEPTNISTGRNASVGNAHRQIPIVHWVIMSISPVGFVENGILLWFLCFRMRRNPFTVYITHLSIADISLLFCIFILSIDYALDYELSSGHYYTIVTLSVTFLFGYNTGLYLLTAISVERCLSVLYPIWYRCHRPKYQSALVCALLWALSCLVTTMEYVMCIDREEESHSRNDCRAVIIFIAILSFLVFTPLMLVSSTILVVKIRKNTWASHSSKLYIVIMVTIIIFLIFAMPMRLLYLLYYEYWSTFGNLHHISLLFSTINSSANPFIYFFVGSSKKKRFKESLKVVLTRAFKDEMQPRRQKDNCNTVTVETVV
Protein: NADPH:adrenodoxin oxidoreductase, mitochondrial (EC 1.18.1.6) (A0A0A0MT64)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|PIRNR:PIRNR000362}.
Interaction partners:
Sequence:
MASRCWRWWGWSAWPRTRLPPAGSTPSFCHHFSTQEKTPQICVVGSGPAGFYTAQHLLKRVEALCSQPRVLNSPALSGEGEDLGASQPLSLGPTSCHPVPQQHPQAHVDIYEKQPVPFGLVRFGVAPDHPEVKNVINTFTQTAHSGRCAFWGNVEVGRDVTVPELQEAYHAVVLSYGAEDHRALEIPGEELPGVCSARAFVGWYNGLPENQELEPDLSCDTAVILGQGNVALDVARILLTPPEHLERTDITKAALGVLRQSRVKTVWLVGRRGPLQVAFTIKELREMIQLPGARPILDPVDFLGLQDKIKEVPRPRKRLTELLLRTATEKPGPAEAARQASASRAWGLRFFRSPQQVLPSPDGRRAAGVRLAVTRLEGVDEATRAVPTGDMEDLPCGLVLSSIGYKSRPVDPSVPFDSKLGVIPNVEGRVMDVPGLYCSGWVKRGPTGVIATTMTDSFLTGQMLLQDLKAGLLPSGPRPGYAAIQALLSSRGVRPVSFSDWEKLDAEEVARGQGTGKPREKLVDPQEMLRLLGH
Protein: Tetraspanin-7 (Tspan-7) (Cell surface glycoprotein A15) (Membrane component chromosome X surface marker 1) (T-cell acute lymphoblastic leukemia-associated antigen 1) (TALLA-1) (Transmembrane 4 superfamily member 2) (CD antigen CD231) (P41732)
Organism: Homo sapiens (Human)
Function: May be involved in cell proliferation and cell motility.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- PRKCA-binding protein
Sequence:
MASRRMETKPVITCLKTLLIIYSFVFWITGVILLAVGVWGKLTLGTYISLIAENSTNAPYVLIGTGTTIVVFGLFGCFATCRGSPWMLKLYAMFLSLVFLAELVAGISGFVFRHEIKDTFLRTYTDAMQTYNGNDERSRAVDHVQRSLSCCGVQNYTNWSTSPYFLEHGIPPSCCMNETDCNPQDLHNLTVAATKVNQKGCYDLVTSFMETNMGIIAGVAFGIAFSQLIGMLLACCLSRFITANQYEMV
Protein: Mitochondrial RNA binding complex 1 subunit (Q384B4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitochondrial RNA binding protein
- Mitochondrial RNA binding complex 1 subunit
- REH2-associated factor 2
- RNA editing associated helicase 2
Sequence:
MRSSRGILFLSGAFAIRGMSAYHSYQRLDTVSHTSKVYSLQMQRQTVHFTPITRLGVEATANPTTATNATGQTGDGDGATALDVAMRVNKLKRLHQTGGGPSGKKQVELDAWRDLNNLTEAQINSAEGKAVSLLLNSWAYFAKYWEKGAEGPSASLSEVTPSNDSSSAGEHGTQ
Protein: Cell division protein FtsL (Q07867)
Organism: Bacillus subtilis (strain 168)
Function: Essential cell division protein that may play a structural role. Probably involved in the regulation of the timing of cell division. Also required for sporulation.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00910, ECO:0000269|PubMed:10792716, ECO:0000269|PubMed:10844672, ECO:0000269|PubMed:11994149, ECO:0000269|PubMed:16936019}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_00910, ECO:0000269|PubMed:10792716, ECO:0000269|PubMed:10844672, ECO:0000269|PubMed:11994149, ECO:0000269|PubMed:16936019}. Note=Localizes to the division septum where it forms a ring structure. Remains localized at mid-cell during the whole septation process. Localization requires FtsZ, DivIB, DivIC and PBP-2B.
Interaction partners:
- Cell division protein DivIC
- Penicillin-binding protein 2B
- Cell division protein DivIB
- Ribosomal RNA small subunit methyltransferase H
- Cell division protein FtsA
- Probable peptidoglycan glycosyltransferase FtsW
- Septation ring formation regulator EzrA
- Cell division protein FtsZ
- Cell division protein SepF
- Cell division protein ZapA
Sequence:
MSNLAYQPEKQQRHAISPEKKVIVKKRASITLGEKVLLVLFAAAVLSVSLLIVSKAYAAYQTNIEVQKLEEQISSENKQIGDLEKSVADLSKPQRIMDIAKKNGLNLKDKKVKNIQE
Protein: Structural maintenance of chromosomes protein 2 (Cell untimely torn protein 14) (Chromosome segregation protein cut14) (P41003)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Subcellular location: Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.
Interaction partners:
- Condensin complex subunit 1
- Condensin complex subunit 2
- Structural maintenance of chromosomes protein 4
- Condensin complex subunit 3
- DNA topoisomerase 2
- Cohesin subunit rad21
- Kinesin-like protein cut7
- Kinetochore protein ndc80
- Aurora kinase
- N-acetyltransferase eso1
Sequence:
MKIEELIIDGFKSYAVRTVISNWDDQFNAITGLNGSGKSNILDAICFVLGITNMSTVRAQNLQDLIYKRGQAGITRASVTIVFNNRDPASSPIGFENHPQVSVTRQIIMGGTSKYLINGHRALQQNVQNLFQSVQLNINNPNFLIMQGRITKVLNMKATEILSMIEEASGTRMFEERKEKAFRTMQRKEAKVEEINTLLREEIEPRLTKLRTEKKTFLEYQHIYNDLERLSHLCTAYDYYKLSLKVEELTVQASQKHSHIAEMESSLQTSKQEVLILKEKIKKIEDERMRQMSVSSDRTLDSQLQTVNENITRISTSIELKNTALEEEHGDLQQIRGKAKELETLLRGKRKRLDEVLSVYEKRKDEHQSISKDFKSQEELISSLTTGLSTTEGHETGYSRKLHEARDTLNDFKAEKETNRLKLEGLNKQISLTKPKKAEATKRCDQLNREIDILQNHVEKLKMSLKNTNSDITGEDVLQQKLKQLAKDRGNLLNELDALKSKLAYMEFTYTDPTPNFDRSKVKGLVAQLLTLNEENYDKQTALEITAGGRLYNLIVETEKIGAQLLQKGNLKRRVTIIPLNKITSFVASAERVGAAKKISNNKAQLALELIGYDDELLPAMQYVFGSTLVCDTPESAKKVTFHPSVKLKSVTLDGDVYDPSGTLTGGSVNKSAGPLLQIQKLNSLQLKLQVVTSEYEKLETQLKDLKTQNANFHRLEQEIQLKQHELTLLIEQRETDSSFRLLSDYQQYKDDVKDLKQRLPELDRLILQSDQAIKKIERDMQEWKHNKGSKMAELEKEFNQYKHKLDEFTPILEKSENDYNGVKLECEQLEGELQNHQQSLVQGESTTSLIKTEIAELELSLVNEEHNRKKLTELIEIESAKFSGLNKEIDSLSTSMKTFESEINNGELTIQKLNHEFDRLEREKSVAITAINHLEKENDWIDGQKQHFGKQGTIFDFHSQNMRQCREQLHNLKPRFASMRKAINPKVMDMIDGVEKKEAKLRSMIKTIHRDKKKIQDTVKSIDRFKRSALEKTWREVNSSFGEIFDELLPGNSAELQPPENKEFTDGLEIHVKIGSIWKDSLAELSGGQRSLVALALIMSLLKYKPAPMYILDEIDAALDLSHTQNIGRLIKTKFKGSQFIIVSLKEGMFTNANRLFHVRFMDGSSVVQAR
Protein: NACHT, LRR and PYD domains-containing protein 11 (Nucleotide-binding oligomerization domain protein 17) (PAAD-and NACHT domain-containing protein 10) (PYRIN-containing APAF1-like protein 6) (P59045)
Organism: Homo sapiens (Human)
Function: Involved in inflammation.
Interaction partners:
- Pyrin
- E3 ubiquitin-protein ligase RNF19A
Sequence:
MAESDSTDFDLLWYLENLSDKEFQSFKKYLARKILDFKLPQFPLIQMTKEELANVLPISYEGQYIWNMLFSIFSMMRKEDLCRKIIGRRNRNQEACKAVMRRKFMLQWESHTFGKFHYKFFRDVSSDVFYILQLAYDSTSYYSANNLNVFLMGERASGKTIVINLAVLRWIKGEMWQNMISYVVHLTAHEINQMTNSSLAELIAKDWPDGQAPIADILSDPKKLLFILEDLDNIRFELNVNESALCSNSTQKVPIPVLLVSLLKRKMAPGCWFLISSRPTRGNNVKTFLKEVDCCTTLQLSNGKREIYFNSFFKDRQRASAALQLVHEDEILVGLCRVAILCWITCTVLKRQMDKGRDFQLCCQTPTDLHAHFLADALTSEAGLTANQYHLGLLKRLCLLAAGGLFLSTLNFSGEDLRCVGFTEADVSVLQAANILLPSNTHKDRYKFIHLNVQEFCTAIAFLMAVPNYLIPSGSREYKEKREQYSDFNQVFTFIFGLLNANRRKILETSFGYQLPMVDSFKWYSVGYMKHLDRDPEKLTHHMPLFYCLYENREEEFVKTIVDALMEVTVYLQSDKDMMVSLYCLDYCCHLRTLKLSVQRIFQNKEPLIRPTASQMKSLVYWREICSLFYTMESLRELHIFDNDLNGISERILSKALEHSSCKLRTLKLSYVSTASGFEDLLKALARNRSLTYLSINCTSISLNMFSLLHDILHEPTCQISHLSLMKCDLRASECEEIASLLISGGSLRKLTLSSNPLRSDGMNILCDALLHPNCTLISLVLVFCCLTENCCSALGRVLLFSPTLRQLDLCVNRLKNYGVLHVTFPLLFPTCQLEELHLSGCFFSSDICQYIAIVIATNEKLRSLEIGSNKIEDAGMQLLCGGLRHPNCMLVNIGLEECMLTSACCRSLASVLTTNKTLERLNLLQNHLGNDGVAKLLESLISPDCVLKVVGLPLTGLNTQTQQLLMTVKERKPSLIFLSETWSLKEGREIGVTPASQPGSIIPNSNLDYMFFKFPRMSAAMRTSNTASRQPL
Protein: Extracellular sulfatase (EC 3.1.6.-) (Q6EF98)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR036665}. Golgi apparatus, Golgi stack {ECO:0000256|ARBA:ARBA00004348, ECO:0000256|PIRNR:PIRNR036665}. Cell surface {ECO:0000256|PIRNR:PIRNR036665}.
Interaction partners:
Sequence:
MAAHGLAARLLPLLLLAMLAVAHASIFLSNQRLKPRFQRDRRNIRPNIILILTDDQDIELGSMQVMNKTRRIMEQGGTHFSNAFVTTPMCCPSRSSMLTGKYAHNHNTYTNNENCSSPSWQAQHEPRTFGVYLNNTGYRTAFFGKYLNEYNGTYIPPGWREWVAMVKNSRFYNYTLCRNGVREKHGFEYPKDYLTDLITNDSINYFRMSKKIYPHRPVLMVISHAAPHGPEDAAPQYTTAFPNASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLLSVDDSVEKVYNMLVDTGELDNTYVIYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYIRGPNVEAGGINPHIVLNIDLAPTILDIAGMDVPPDMDGKSILKLLDTDRMMNRFQLNKKGKVWRDSFLVERGKLLHKVLNDGKDMAEEENYLPKYQRVKDLCQRAEYQTPCEQIGQKWQCVEDATGKLRLSKCKGMSSLSAVQKPSVSSIKSQLYLQSISTPDVSLNSEPQECNCQPKSYRLSTYSKSKLFSKKKMKSLKSFSRNRFARALSMETGGDLYAVDLDNEHRNLSLRHSTADEDEEFSGAEPTTISQSNSLSVPSSIKVTHRCSILANETVKCDVGLYKSLQAWKDHKLHIDHEIETLQTKIKNLREVRGHLKKARPEECDCNKYYYKSKYKSKLRKYKTGNVHPFRKGQEKDKKAWMMLEQKRRKKLRKLLKRLRNNDTCSMPGLTCFTHDNQHWQTAPFWTLGPFCACTSANNNTYWCMRTINETHNFLFCEFATGFLEYFDINTDPYQLVNAVNTLDRYVLNQLHVQLMELRGCKGHKQCNPRTRSLDMGGKERSSYDEYRQFQRRKWPKVRKPVSKSLGQIWEGWEG
Protein: Uncharacterized protein (A0A1D8PHT4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Chromatin structure-remodeling complex subunit SFH1
- RSC chromatin remodeling complex ATPase subunit
- Snf5p
- Chromatin structure-remodeling complex protein RSC8
- Uncharacterized protein
- RFX-type winged-helix domain-containing protein
- Bromo domain-containing protein
- Npl6p
- Arp9p
- Uncharacterized protein
Sequence:
MQSISQQQVPHHPPPANKPRPNAAAVPTISYQPTDIIIPTQLYDKIGNLGEYKRLQEAEKKLDLLIARKSLDFQAIQQKSIHPHEYRPSTGVLRIFIYNTCENQPWQKQLLQQKGLPVPDPTLAESSWTLRIEGKFISDIPDEQQQIDETFKFSSFLSAISVDLLPNENYPNIQESQSHIIEWRDDGPNANKPPASVSFDGLDIKRNGIFNIKSKIALLVKNHSNSLKLSEEMSRFVGKQECSQQELLYIIWQYVLFKGLFKKSNAYTEVPAVETSTLPNPADDKDSSDDDLTLVEADDLLFELLKVKTFKFSDLYKLTQAHFVPREPIIVDYEVDTRKSTTLGNVVLDIPVELPLNLLKAQKELLDVNKTAFENLAKADSTISQLDQRISLAIIALQNANSREKFYRELSDDPVKFIENWLESQAETLKALKSDEGYDEEVVRRAKYFEENEHLIKEKIELLLGSNKF