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Q13796

- SHRM2_HUMAN

UniProt

Q13796 - SHRM2_HUMAN

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Protein

Protein Shroom2

Gene
SHROOM2, APXL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution By similarity.

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. actin filament binding Source: UniProtKB
  3. beta-catenin binding Source: UniProtKB
  4. ligand-gated sodium channel activity Source: ProtInc
  5. protein binding Source: IntAct

GO - Biological processi

  1. apical protein localization Source: HGNC
  2. brain development Source: HGNC
  3. camera-type eye development Source: HGNC
  4. camera-type eye morphogenesis Source: HGNC
  5. cell-cell junction maintenance Source: Ensembl
  6. cell migration Source: UniProtKB
  7. cellular pigment accumulation Source: HGNC
  8. ear development Source: HGNC
  9. establishment of melanosome localization Source: HGNC
  10. eye pigment granule organization Source: HGNC
  11. lens morphogenesis in camera-type eye Source: HGNC
  12. melanosome organization Source: HGNC
  13. negative regulation of actin filament depolymerization Source: Ensembl
  14. sodium ion transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Shroom2
Alternative name(s):
Apical-like protein
Protein APXL
Gene namesi
Name:SHROOM2
Synonyms:APXL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:630. SHROOM2.

Subcellular locationi

Apical cell membrane By similarity. Cell junctiontight junction By similarity. Cytoplasmcytoskeleton By similarity
Note: Associates with cortical F-actin By similarity.

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. cell-cell adherens junction Source: UniProtKB
  3. cell cortex Source: Ensembl
  4. cytoskeleton Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. filamentous actin Source: Ensembl
  7. microtubule Source: UniProtKB-KW
  8. neuronal cell body Source: Ensembl
  9. plasma membrane Source: UniProtKB
  10. tight junction Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Microtubule, Tight junction

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24916.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16161616Protein Shroom2PRO_0000064650Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei231 – 2311Phosphoserine By similarity
Modified residuei922 – 9221Phosphoserine By similarity
Modified residuei974 – 9741Phosphoserine1 Publication
Modified residuei1036 – 10361Phosphoserine1 Publication
Modified residuei1039 – 10391Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13796.
PaxDbiQ13796.
PRIDEiQ13796.

PTM databases

PhosphoSiteiQ13796.

Expressioni

Tissue specificityi

Abundant in retina and melanoma; also in brain, placenta, lung, kidney and pancreas.

Gene expression databases

ArrayExpressiQ13796.
BgeeiQ13796.
CleanExiHS_SHROOM2.
GenevestigatoriQ13796.

Organism-specific databases

HPAiHPA051646.

Interactioni

Subunit structurei

Interacts with F-actin By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-1644065,EBI-389883

Protein-protein interaction databases

BioGridi106853. 1 interaction.
IntActiQ13796. 5 interactions.
STRINGi9606.ENSP00000370299.

Structurei

3D structure databases

ProteinModelPortaliQ13796.
SMRiQ13796. Positions 27-108, 1436-1609.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 10883PDZAdd
BLAST
Domaini684 – 77390ASD1Add
BLAST
Domaini1317 – 1611295ASD2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi150 – 1534Poly-Ser
Compositional biasi314 – 3207Poly-Pro
Compositional biasi343 – 3464Poly-Ala
Compositional biasi1065 – 10684Poly-Pro

Domaini

The ASD1 domain mediates F-actin binding By similarity.

Sequence similaritiesi

Belongs to the shroom family.
Contains 1 ASD1 domain.
Contains 1 ASD2 domain.
Contains 1 PDZ (DHR) domain.

Phylogenomic databases

eggNOGiNOG72784.
HOGENOMiHOG000008235.
HOVERGENiHBG096290.
InParanoidiQ13796.
OMAiWKEQRKP.
OrthoDBiEOG73V6JC.
PhylomeDBiQ13796.
TreeFamiTF333370.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR014800. ASD1.
IPR014799. ASD2.
IPR001478. PDZ.
IPR027686. Shroom2.
IPR027685. Shroom_fam.
[Graphical view]
PANTHERiPTHR15012. PTHR15012. 1 hit.
PTHR15012:SF8. PTHR15012:SF8. 1 hit.
PfamiPF08688. ASD1. 1 hit.
PF08687. ASD2. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS51306. ASD1. 1 hit.
PS51307. ASD2. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13796-1 [UniParc]FASTAAdd to Basket

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MEGAEPRARP ERLAEAETRA ADGGRLVEVQ LSGGAPWGFT LKGGREHGEP     50
LVITKIEEGS KAAAVDKLLA GDEIVGINDI GLSGFRQEAI CLVKGSHKTL 100
KLVVKRRSEL GWRPHSWHAT KFSDSHPELA ASPFTSTSGC PSWSGRHHAS 150
SSSHDLSSSW EQTNLQRTLD HFSSLGSVDS LDHPSSRLSV AKSNSSIDHL 200
GSHSKRDSAY GSFSTSSSTP DHTLSKADTS SAENILYTVG LWEAPRQGGR 250
QAQAAGDPQG SEEKLSCFPP RVPGDSGKGP RPEYNAEPKL AAPGRSNFGP 300
VWYVPDKKKA PSSPPPPPPP LRSDSFAATK SHEKAQGPVF SEAAAAQHFT 350
ALAQAQPRGD RRPELTDRPW RSAHPGSLGK GSGGPGCPQE AHADGSWPPS 400
KDGASSRLQA SLSSSDVRFP QSPHSGRHPP LYSDHSPLCA DSLGQEPGAA 450
SFQNDSPPQV RGLSSCDQKL GSGWQGPRPC VQGDLQAAQL WAGCWPSDTA 500
LGALESLPPP TVGQSPRHHL PQPEGPPDAR ETGRCYPLDK GAEGCSAGAQ 550
EPPRASRAEK ASQRLAASIT WADGESSRIC PQETPLLHSL TQEGKRRPES 600
SPEDSATRPP PFDAHVGKPT RRSDRFATTL RNEIQMHRAK LQKSRSTVAL 650
TAAGEAEDGT GRWRAGLGGG TQEGPLAGTY KDHLKEAQAR VLRATSFKRR 700
DLDPNPGDLY PESLEHRMGD PDTVPHFWEA GLAQPPSSTS GGPHPPRIGG 750
RRRFTAEQKL KSYSEPEKMN EVGLTRGYSP HQHPRTSEDT VGTFADRWKF 800
FEETSKPVPQ RPAQKQALHG IPRDKPERPR TAGRTCEGTE PWSRTTSLGD 850
SLNAHSAAEK AGTSDLPRRL GTFAEYQASW KEQRKPLEAR SSGRCHSADD 900
ILDVSLDPQE RPQHVHGRSR SSPSTDHYKQ EASVELRRQA GDPGEPREEL 950
PSAVRAEEGQ STPRQADAQC REGSPGSQQH PPSQKAPNPP TFSELSHCRG 1000
APELPREGRG RAGTLPRDYR YSEESTPADL GPRAQSPGSP LHARGQDSWP 1050
VSSALLSKRP APQRPPPPKR EPRRYRATDG APADAPVGVL GRPFPTPSPA 1100
SLDVYVARLS LSHSPSVFSS AQPQDTPKAT VCERGSQHVS GDASRPLPEA 1150
LLPPKQQHLR LQTATMETSR SPSPQFAPQK LTDKPPLLIQ DEDSTRIERV 1200
MDNNTTVKMV PIKIVHSESQ PEKESRQSLA CPAEPPALPH GLEKDQIKTL 1250
STSEQFYSRF CLYTRQGAEP EAPHRAQPAE PQPLGTQVPP EKDRCTSPPG 1300
LSYMKAKEKT VEDLKSEELA REIVGKDKSL ADILDPSVKI KTTMDLMEGI 1350
FPKDEHLLEE AQQRRKLLPK IPSPRSTEER KEEPSVPAAV SLATNSTYYS 1400
TSAPKAELLI KMKDLQEQQE HEEDSGSDLD HDLSVKKQEL IESISRKLQV 1450
LREARESLLE DVQANTVLGA EVEAIVKGVC KPSEFDKFRM FIGDLDKVVN 1500
LLLSLSGRLA RVENALNNLD DGASPGDRQS LLEKQRVLIQ QHEDAKELKE 1550
NLDRRERIVF DILANYLSEE SLADYEHFVK MKSALIIEQR ELEDKIHLGE 1600
EQLKCLLDSL QPERGK 1616
Length:1,616
Mass (Da):176,410
Last modified:November 1, 1996 - v1
Checksum:i752406B5BC0B60A2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti942 – 9421D → E.
Corresponds to variant rs16985780 [ dbSNP | Ensembl ].
VAR_053896
Natural varianti1245 – 12451D → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_036577
Natural varianti1475 – 14751I → V.
Corresponds to variant rs12012202 [ dbSNP | Ensembl ].
VAR_053897
Natural varianti1607 – 16071L → F.
Corresponds to variant rs2073942 [ dbSNP | Ensembl ].
VAR_024250

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83543 mRNA. Translation: CAA58534.1.
AC002365 Genomic DNA. Translation: AAC32592.1.
AC090481 Genomic DNA. No translation available.
BC140866 mRNA. Translation: AAI40867.1.
CCDSiCCDS14135.1.
PIRiI37183.
RefSeqiNP_001640.1. NM_001649.2.
UniGeneiHs.567236.

Genome annotation databases

EnsembliENST00000380913; ENSP00000370299; ENSG00000146950.
GeneIDi357.
KEGGihsa:357.
UCSCiuc004csu.1. human.

Polymorphism databases

DMDMi2498147.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83543 mRNA. Translation: CAA58534.1 .
AC002365 Genomic DNA. Translation: AAC32592.1 .
AC090481 Genomic DNA. No translation available.
BC140866 mRNA. Translation: AAI40867.1 .
CCDSi CCDS14135.1.
PIRi I37183.
RefSeqi NP_001640.1. NM_001649.2.
UniGenei Hs.567236.

3D structure databases

ProteinModelPortali Q13796.
SMRi Q13796. Positions 27-108, 1436-1609.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106853. 1 interaction.
IntActi Q13796. 5 interactions.
STRINGi 9606.ENSP00000370299.

PTM databases

PhosphoSitei Q13796.

Polymorphism databases

DMDMi 2498147.

Proteomic databases

MaxQBi Q13796.
PaxDbi Q13796.
PRIDEi Q13796.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380913 ; ENSP00000370299 ; ENSG00000146950 .
GeneIDi 357.
KEGGi hsa:357.
UCSCi uc004csu.1. human.

Organism-specific databases

CTDi 357.
GeneCardsi GC0XP009714.
HGNCi HGNC:630. SHROOM2.
HPAi HPA051646.
MIMi 300103. gene.
neXtProti NX_Q13796.
PharmGKBi PA24916.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG72784.
HOGENOMi HOG000008235.
HOVERGENi HBG096290.
InParanoidi Q13796.
OMAi WKEQRKP.
OrthoDBi EOG73V6JC.
PhylomeDBi Q13796.
TreeFami TF333370.

Miscellaneous databases

ChiTaRSi SHROOM2. human.
GenomeRNAii 357.
NextBioi 1493.
PROi Q13796.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13796.
Bgeei Q13796.
CleanExi HS_SHROOM2.
Genevestigatori Q13796.

Family and domain databases

Gene3Di 2.30.42.10. 1 hit.
InterProi IPR014800. ASD1.
IPR014799. ASD2.
IPR001478. PDZ.
IPR027686. Shroom2.
IPR027685. Shroom_fam.
[Graphical view ]
PANTHERi PTHR15012. PTHR15012. 1 hit.
PTHR15012:SF8. PTHR15012:SF8. 1 hit.
Pfami PF08688. ASD1. 1 hit.
PF08687. ASD2. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view ]
SMARTi SM00228. PDZ. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 1 hit.
PROSITEi PS51306. ASD1. 1 hit.
PS51307. ASD2. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a human homologue of the Xenopus laevis APX gene from the ocular albinism type 1 critical region."
    Schiaffino V.M., Bassi M.T., Rugarli E.I., Renieri A., Galli L., Ballabio A.
    Hum. Mol. Genet. 4:373-382(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NOMENCLATURE.
  5. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974; SER-1036 AND SER-1039, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-1245.

Entry informationi

Entry nameiSHRM2_HUMAN
AccessioniPrimary (citable) accession number: Q13796
Secondary accession number(s): B9EIQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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