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 A7MB75

Entry ID Method Resolution Chain Position Source
AF-A7MB75-F1 Predicted AlphaFoldDB

88 variants for A7MB75

Variant ID(s) Position Change Description Diseaes Association Provenance
rs447277876 6 L>I No EVA
rs477068677 31 T>P No EVA
rs443589738 32 A>G No EVA
rs458527660 32 A>S No EVA
rs482927222 34 T>A No EVA
rs461199654 40 L>M No EVA
rs472347499 46 H>D No EVA
rs478899967 48 F>L No EVA
rs460291002 50 L>V No EVA
rs438543357 51 K>E No EVA
rs470910033 58 Q>E No EVA
rs458847431 58 Q>H No EVA
rs476396621 60 T>P No EVA
rs476396621 60 T>S No EVA
rs455100255 61 V>G No EVA
rs472880141 62 R>P No EVA
rs436677741 62 R>S No EVA
rs454256521 63 F>S No EVA
rs432516277 64 Q>K No EVA
rs465085022 64 Q>P No EVA
rs449769557 65 H>D No EVA
rs437632372 65 H>P No EVA
rs467347142 67 V>G No EVA
rs477769174 72 L>F No EVA
rs445015306 72 L>V No EVA
rs458912392 73 L>R No EVA
rs442773532 76 E>A No EVA
rs461298872 76 E>K No EVA
rs454385196 77 P>R No EVA
rs472880005 77 P>T No EVA
rs456259594 80 F>C No EVA
rs437685867 81 L>H No EVA
rs448784161 83 W>* No EVA
rs467426704 83 W>G No EVA
rs433539543 84 S>G No EVA
rs466841367 85 T>P No EVA
rs445110865 85 T>R No EVA
rs477832616 86 F>C No EVA
rs469002872 86 F>L No EVA
rs450137915 87 P>H No EVA
rs482938673 88 A>G No EVA
rs461408382 89 F>L No EVA
rs442820261 90 N>I No EVA
rs479020702 91 R>L No EVA
rs439104219 92 L>P No EVA
rs439104219 92 L>R No EVA
rs456736632 93 Q>H No EVA
rs472035831 93 Q>P No EVA
rs444597138 94 E>A No EVA
rs444597138 94 E>G No EVA
rs473924506 95 G>C No EVA
rs455389428 95 G>D No EVA
rs466561124 96 H>Q No EVA
rs451546326 97 L>R No EVA
rs433036540 98 R>G No EVA
rs469070079 99 V>A No EVA
rs469070079 99 V>G No EVA
rs480195559 100 P>L No EVA
rs450605220 100 P>T No EVA
rs449352344 101 L>R No EVA
rs460553766 103 S>W No EVA
rs445540862 114 K>R No EVA
rs478441063 134 G>R No EVA
rs463170047 143 Y>D No EVA
rs465211305 152 V>M No EVA
rs435895667 155 S>I No EVA
rs468659277 156 M>I No EVA
rs447025258 158 F>V No EVA
rs479784323 162 S>P No EVA
rs445670785 163 F>S No EVA
rs448014569 180 Q>L No EVA
rs481396827 182 Q>R No EVA
rs449601814 224 T>P No EVA
rs479248595 225 I>F No EVA
rs460754191 225 I>T No EVA
rs471530213 233 W>R No EVA
rs462605510 235 V>L No EVA
rs444042625 236 G>E No EVA
rs136104308 239 A>S No EVA
rs136104308 239 A>T No EVA
rs440270975 241 A>S No EVA
rs451503533 244 V>G No EVA
rs465508634 245 V>F No EVA
rs456548427 248 V>F No EVA
rs438037667 251 Y>S No EVA
rs434486817 261 G>R No EVA
rs445609450 274 V>I No EVA
rs481844305 288 K>E No EVA

No associated diseases with A7MB75

4 regional properties for A7MB75

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 178 - 348 IPR000795
domain Small GTP-binding protein domain 181 - 304 IPR005225
domain Translation initiation factor IF- 2, domain 3 508 - 606 IPR023115
domain Translation initiation factor IF-2, domain II 354 - 448 IPR044145

Functions

Description
EC Number
Subcellular Localization
  • Cell projection, cilium membrane ; Multi-pass membrane protein
  • Localizes to the transition zone of primary cilia; SEPT2 is required for localization to the transition zone
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
ciliary membrane The portion of the plasma membrane surrounding a cilium.
ciliary transition zone A region of the cilium between the basal body and proximal segment that is characterized by Y-shaped assemblages that connect axonemal microtubules to the ciliary membrane. The ciliary transition zone appears to function as a gate that controls ciliary membrane composition and separates the cytosol from the ciliary plasm.
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.
MKS complex A protein complex that is located at the ciliary transition zone and consists of several proteins some of which are membrane bound. Acts as an organiser of transition zone inner structure, specifically the Y-shaped links, in conjunction with the NPHP complex. The MKS complex also acts as part of the selective barrier that prevents diffusion of proteins between the ciliary cytoplasm and cellular cytoplasm as well as between the ciliary membrane and plasma membrane.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

3 GO annotations of biological process

Name Definition
cilium assembly The assembly of a cilium, a specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface. Each cilium is bounded by an extrusion of the cytoplasmic membrane, and contains a regular longitudinal array of microtubules, anchored basally in a centriole.
regulation of protein localization Any process that modulates the frequency, rate or extent of any process in which a protein is transported to, or maintained in, a specific location.
smoothened signaling pathway The series of molecular signals generated as a consequence of activation of the transmembrane protein Smoothened.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3T0J3 MRPL16 39S ribosomal protein L16, mitochondrial Bos taurus (Bovine) PR
Q9H6L2 TMEM231 Transmembrane protein 231 Homo sapiens (Human) PR
Q5M818 Mrpl16 39S ribosomal protein L16, mitochondrial Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MALYELFAHP VERGYRAGLC SKAALFLLLA TALTYIPPLL VAFRSHGFWL KRSSYEEQPT
70 80 90 100 110 120
VRFQHQVLLV ALLGSEPGGF LAWSTFPAFN RLQEGHLRVP LVSAREEDRN QDGKMDMLHF
130 140 150 160 170 180
KLELPLQSTE QVLGVQLILT FSYQLHRMST FVMQSMAFLQ SSFALPGSQL YVNGDLRLQQ
190 200 210 220 230 240
KQPLGYGGLD VRYNVSVING TSPFASDYDL TRIVAAYQER NVTTILTDPS PIWLVGRAAE
250 260 270 280 290 300
APFVVNAVIR YPVEVISYLP GFWEMIKFAW IQYVSILLIF LWAFERIKRF VFQNQVVTTI
310
PVTAMPQGEL YKEHLS