Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q2TBM9

Entry ID Method Resolution Chain Position Source
AF-Q2TBM9-F1 Predicted AlphaFoldDB

84 variants for Q2TBM9

Variant ID(s) Position Change Description Diseaes Association Provenance
rs439825321 64 Q>K No EVA
rs452277159 94 A>T No EVA
rs443493036 118 A>D No EVA
rs457768935 119 D>A No EVA
rs476540614 119 D>H No EVA
rs478976137 121 F>L No EVA
rs460337196 134 W>R No EVA
rs441765729 135 L>V No EVA
rs474828994 137 L>V No EVA
rs444540617 140 S>I No EVA
rs456435139 140 S>R No EVA
rs470805600 140 S>R No EVA
rs452420633 142 S>A No EVA
rs467207451 143 D>V No EVA
rs436534165 146 A>E No EVA
rs455244383 146 A>S No EVA
rs449791751 148 R>P No EVA
rs445696214 151 A>P No EVA
rs478669421 152 V>A No EVA
rs478669421 152 V>D No EVA
rs460356440 154 E>D No EVA
rs441918146 155 M>L No EVA
rs481268411 155 M>R No EVA
rs441918146 155 M>V No EVA
rs462630890 156 S>P No EVA
rs444481284 158 A>P No EVA
rs444481284 158 A>T No EVA
rs452507553 162 H>Q No EVA
rs460005604 183 R>* No EVA
rs453896491 190 R>L No EVA
rs478450638 247 G>C No EVA
rs472877008 249 L>F No EVA
rs460905015 251 C>G No EVA
rs442327988 251 C>W No EVA
rs475212763 252 F>C No EVA
rs432317808 254 G>R No EVA
rs471583897 254 G>V No EVA
rs434581368 256 G>E No EVA
rs449409268 259 Y>F No EVA
rs458032955 261 E>* No EVA
rs437185858 261 E>G No EVA
rs470219074 262 S>R No EVA
rs445505405 264 G>* No EVA
rs445505405 264 G>R No EVA
rs478583017 265 E>K No EVA
rs460069197 267 P>H No EVA
rs447763231 268 S>* No EVA
rs480621179 269 A>D No EVA
rs460837486 271 V>A No EVA
rs460837486 271 V>E No EVA
rs463342707 275 C>F No EVA
rs475202262 275 C>R No EVA
rs438669230 276 L>F No EVA
rs471639350 280 V>G No EVA
rs441033956 325 M>L No EVA
rs382552957 353 I>V No EVA
rs446836942 357 S>Y No EVA
rs479814503 370 T>N No EVA
rs435520705 389 S>R No EVA
rs386018489 423 V>I No EVA
rs474031559 452 E>D No EVA
rs462216263 454 D>A No EVA
rs443744509 455 T>P No EVA
rs476604171 460 W>* No EVA
rs451644425 468 R>M No EVA
rs518293856 475 S>G No EVA
rs435167461 481 K>T No EVA
rs468195045 483 R>G No EVA
rs209114168 514 R>K No EVA
rs479429936 572 D>G No EVA
rs460986436 597 S>R No EVA
rs448800394 598 M>L No EVA
rs463658143 601 L>P No EVA
rs482144071 601 L>V No EVA
rs438577002 602 H>P No EVA
rs471634018 603 V>G No EVA
rs459834654 604 V>G No EVA
rs474323647 606 L>R No EVA
rs455691832 607 D>G No EVA
rs437183251 608 S>A No EVA
rs437183251 608 S>P No EVA
rs476665027 608 S>W No EVA
rs451928965 609 A>G No EVA
rs442200520 620 D>G No EVA

No associated diseases with Q2TBM9

No regional properties for Q2TBM9

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q2TBM9

Functions

Description
EC Number
Subcellular Localization
  • Membrane ; Single-pass membrane protein
  • Endoplasmic reticulum
  • Mitochondrion
  • Localizes at the endoplasmic reticulum and at the endoplasmic reticulum-mitochondria interface
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
extracellular matrix A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
mitochondria-associated endoplasmic reticulum membrane A zone of apposition between endoplasmic-reticulum and mitochondrial membranes, structured by bridging complexes. These contact sites are thought to facilitate inter-organelle calcium and phospholipid exchange.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

4 GO annotations of biological process

Name Definition
extracellular matrix organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix.
intracellular cholesterol transport The directed movement of cholesterol, cholest-5-en-3-beta-ol, within cells.
phosphatidylglycerol acyl-chain remodeling Remodeling the acyl chains of phosphatidylglycerol, through sequential deacylation and re-acylation reactions, to generate phosphatidylglycerol containing different types of fatty acid acyl chains.
phospholipid biosynthetic process The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q96JX3 SERAC1 Protein SERAC1 Homo sapiens (Human) PR
Q5SNQ7 serac1 Protein SERAC1 Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MSLAAYCVIC CRRMGTSTPP PKSSTYWRDI RNIIKFTGSL ILGGSLFITY EVLALKKSLT
70 80 90 100 110 120
LDTQVIEREK MKSYIYVHTV SLDKTENHGI TYQARKELHK AVRKVLATSA RIFRGPFADT
130 140 150 160 170 180
FSTVDIEDHD CAVWLLLRKS RSDDRAARLQ AVQEMSEARH WHDYQYRIIA QACDMRTLTG
190 200 210 220 230 240
LARSKDSDLR FFLRPPPLPS LKEDSSTEEE LRHLLASLPQ TDLDECIQCF TALALSESSQ
250 260 270 280 290 300
SLAAQKGGLW CFGGNGLPYA ESFGEVPSAT VEMFCLEALV KHSEIPTHCD KIEANGGLQL
310 320 330 340 350 360
LQRLYQLHKD CPKVQRNIMR ILGNMALNEH LHSTIVRSGW VSILAEAIKS QHIMEASHAA
370 380 390 400 410 420
RTLANLDRET VPDKYHDGVY VLHPQYRTSQ PIKADVLFIH GLMGAAFKTW RQQDNDQDLT
430 440 450 460 470 480
EKVSEDETKY TTCWPKSWLA RDCPALRIIS VEYDTSLSDW RARCPTERKS IAFRSNELLR
490 500 510 520 530 540
KLRAAGVGDR PVVWVSHSMG GLLVKKMLLE ASKRPEMNTI INNTRGIIFY SVPHHGSHLA
550 560 570 580 590 600
EYSVNIRYLL FPSLEVKELS KDSPALKTLQ DDFLEFAKDK NFQVLSFVET LPTYIGSMIK
610 620 630 640 650
LHVVPLDSAD LGLGDLIPVD VNHLNICKPK KKDAFLYQRT LQFIRDALAK DLEN