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Q13796

- SHRM2_HUMAN

UniProt

Q13796 - SHRM2_HUMAN

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Protein

Protein Shroom2

Gene

SHROOM2

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).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

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 – 2311PhosphoserineBy similarity
Modified residuei922 – 9221PhosphoserineBy 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

BgeeiQ13796.
CleanExiHS_SHROOM2.
ExpressionAtlasiQ13796. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 10883PDZPROSITE-ProRule annotationAdd
BLAST
Domaini684 – 77390ASD1PROSITE-ProRule annotationAdd
BLAST
Domaini1317 – 1611295ASD2PROSITE-ProRule annotationAdd
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.Curated
Contains 1 ASD1 domain.PROSITE-ProRule annotation
Contains 1 ASD2 domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG72784.
GeneTreeiENSGT00530000063061.
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

« Hide

        10         20         30         40         50
MEGAEPRARP ERLAEAETRA ADGGRLVEVQ LSGGAPWGFT LKGGREHGEP
60 70 80 90 100
LVITKIEEGS KAAAVDKLLA GDEIVGINDI GLSGFRQEAI CLVKGSHKTL
110 120 130 140 150
KLVVKRRSEL GWRPHSWHAT KFSDSHPELA ASPFTSTSGC PSWSGRHHAS
160 170 180 190 200
SSSHDLSSSW EQTNLQRTLD HFSSLGSVDS LDHPSSRLSV AKSNSSIDHL
210 220 230 240 250
GSHSKRDSAY GSFSTSSSTP DHTLSKADTS SAENILYTVG LWEAPRQGGR
260 270 280 290 300
QAQAAGDPQG SEEKLSCFPP RVPGDSGKGP RPEYNAEPKL AAPGRSNFGP
310 320 330 340 350
VWYVPDKKKA PSSPPPPPPP LRSDSFAATK SHEKAQGPVF SEAAAAQHFT
360 370 380 390 400
ALAQAQPRGD RRPELTDRPW RSAHPGSLGK GSGGPGCPQE AHADGSWPPS
410 420 430 440 450
KDGASSRLQA SLSSSDVRFP QSPHSGRHPP LYSDHSPLCA DSLGQEPGAA
460 470 480 490 500
SFQNDSPPQV RGLSSCDQKL GSGWQGPRPC VQGDLQAAQL WAGCWPSDTA
510 520 530 540 550
LGALESLPPP TVGQSPRHHL PQPEGPPDAR ETGRCYPLDK GAEGCSAGAQ
560 570 580 590 600
EPPRASRAEK ASQRLAASIT WADGESSRIC PQETPLLHSL TQEGKRRPES
610 620 630 640 650
SPEDSATRPP PFDAHVGKPT RRSDRFATTL RNEIQMHRAK LQKSRSTVAL
660 670 680 690 700
TAAGEAEDGT GRWRAGLGGG TQEGPLAGTY KDHLKEAQAR VLRATSFKRR
710 720 730 740 750
DLDPNPGDLY PESLEHRMGD PDTVPHFWEA GLAQPPSSTS GGPHPPRIGG
760 770 780 790 800
RRRFTAEQKL KSYSEPEKMN EVGLTRGYSP HQHPRTSEDT VGTFADRWKF
810 820 830 840 850
FEETSKPVPQ RPAQKQALHG IPRDKPERPR TAGRTCEGTE PWSRTTSLGD
860 870 880 890 900
SLNAHSAAEK AGTSDLPRRL GTFAEYQASW KEQRKPLEAR SSGRCHSADD
910 920 930 940 950
ILDVSLDPQE RPQHVHGRSR SSPSTDHYKQ EASVELRRQA GDPGEPREEL
960 970 980 990 1000
PSAVRAEEGQ STPRQADAQC REGSPGSQQH PPSQKAPNPP TFSELSHCRG
1010 1020 1030 1040 1050
APELPREGRG RAGTLPRDYR YSEESTPADL GPRAQSPGSP LHARGQDSWP
1060 1070 1080 1090 1100
VSSALLSKRP APQRPPPPKR EPRRYRATDG APADAPVGVL GRPFPTPSPA
1110 1120 1130 1140 1150
SLDVYVARLS LSHSPSVFSS AQPQDTPKAT VCERGSQHVS GDASRPLPEA
1160 1170 1180 1190 1200
LLPPKQQHLR LQTATMETSR SPSPQFAPQK LTDKPPLLIQ DEDSTRIERV
1210 1220 1230 1240 1250
MDNNTTVKMV PIKIVHSESQ PEKESRQSLA CPAEPPALPH GLEKDQIKTL
1260 1270 1280 1290 1300
STSEQFYSRF CLYTRQGAEP EAPHRAQPAE PQPLGTQVPP EKDRCTSPPG
1310 1320 1330 1340 1350
LSYMKAKEKT VEDLKSEELA REIVGKDKSL ADILDPSVKI KTTMDLMEGI
1360 1370 1380 1390 1400
FPKDEHLLEE AQQRRKLLPK IPSPRSTEER KEEPSVPAAV SLATNSTYYS
1410 1420 1430 1440 1450
TSAPKAELLI KMKDLQEQQE HEEDSGSDLD HDLSVKKQEL IESISRKLQV
1460 1470 1480 1490 1500
LREARESLLE DVQANTVLGA EVEAIVKGVC KPSEFDKFRM FIGDLDKVVN
1510 1520 1530 1540 1550
LLLSLSGRLA RVENALNNLD DGASPGDRQS LLEKQRVLIQ QHEDAKELKE
1560 1570 1580 1590 1600
NLDRRERIVF DILANYLSEE SLADYEHFVK MKSALIIEQR ELEDKIHLGE
1610
EQLKCLLDSL QPERGK
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.
GeneTreei ENSGT00530000063061.
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

Bgeei Q13796.
CleanExi HS_SHROOM2.
ExpressionAtlasi Q13796. baseline and differential.
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: October 29, 2014
This is version 120 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