Q13796 (SHRM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein Shroom2

Alternative name(s):
Apical-like protein
Protein APXL

Gene names

Name:	SHROOM2
Synonyms:	APXL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1616 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Interacts with F-actin By similarity.
Subcellular location	Apical cell membrane By similarity. Cell junction › tight junction By similarity. Cytoplasm › cytoskeleton By similarity. Note: Associates with cortical F-actin By similarity.
Tissue specificity	Abundant in retina and melanoma; also in brain, placenta, lung, kidney and pancreas.
Domain	The ASD1 domain mediates F-actin binding By similarity.
Sequence similarities	Belongs to the shroom family. Contains 1 ASD1 domain. Contains 1 ASD2 domain. Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Microtubule Tight junction
Coding sequence diversity	Polymorphism
Ligand	Actin-binding
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apical protein localization Inferred from sequence or structural similarity. Source: HGNC brain development Inferred from sequence or structural similarity. Source: HGNC cell migration Inferred from sequence or structural similarity. Source: UniProtKB cell-cell junction maintenance Inferred from electronic annotation. Source: Compara cellular pigment accumulation Inferred from sequence or structural similarity. Source: HGNC ear development Inferred from sequence or structural similarity. Source: HGNC establishment of melanosome localization Inferred from sequence or structural similarity. Source: HGNC eye pigment granule organization Inferred from sequence or structural similarity. Source: HGNC lens morphogenesis in camera-type eye Inferred from sequence or structural similarity. Source: HGNC melanosome organization Inferred from sequence or structural similarity. Source: HGNC negative regulation of actin filament depolymerization Inferred from electronic annotation. Source: Compara
Cellular_component	apical plasma membrane Inferred from sequence or structural similarity PubMed 16684770. Source: UniProtKB cell cortex Inferred from electronic annotation. Source: Compara cell-cell adherens junction Inferred from sequence or structural similarity PubMed 16684770. Source: UniProtKB cytoskeleton Inferred from sequence or structural similarity. Source: UniProtKB filamentous actin Inferred from electronic annotation. Source: Compara microtubule Inferred from electronic annotation. Source: UniProtKB-KW neuronal cell body Inferred from electronic annotation. Source: Compara tight junction Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	actin filament binding Inferred from sequence or structural similarity PubMed 16684770. Source: UniProtKB beta-catenin binding Inferred from sequence or structural similarity PubMed 16684770. Source: UniProtKB ligand-gated sodium channel activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	2	EBI-1644065,EBI-389883

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1616	1616	Protein Shroom2		PRO_0000064650
Regions
	Domain	26 – 108	83	PDZ
	Domain	684 – 773	90	ASD1
	Domain	1317 – 1611	295	ASD2
	Compositional bias	150 – 153	4	Poly-Ser
	Compositional bias	314 – 320	7	Poly-Pro
	Compositional bias	343 – 346	4	Poly-Ala
	Compositional bias	1065 – 1068	4	Poly-Pro
Amino acid modifications
	Modified residue	922	1	Phosphoserine By similarity
	Modified residue	974	1	Phosphoserine Ref.5
	Modified residue	1036	1	Phosphoserine Ref.5
	Modified residue	1039	1	Phosphoserine Ref.5
	Modified residue	1297	1	Phosphoserine By similarity
Natural variations
	Natural variant	942	1	D → E. Corresponds to variant rs16985780 [ dbSNP | Ensembl ].		VAR_053896
	Natural variant	1245	1	D → H in a breast cancer sample; somatic mutation. Ref.6		VAR_036577
	Natural variant	1475	1	I → V. Corresponds to variant rs12012202 [ dbSNP | Ensembl ].		VAR_053897
	Natural variant	1607	1	L → F. Corresponds to variant rs2073942 [ dbSNP | Ensembl ].		VAR_024250

Sequences

	Sequence		Length	Mass (Da)
	Q13796 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 752406B5BC0B60A2	FASTA	1,616	176,410
	10 20 30 40 50 60 MEGAEPRARP ERLAEAETRA ADGGRLVEVQ LSGGAPWGFT LKGGREHGEP LVITKIEEGS 70 80 90 100 110 120 KAAAVDKLLA GDEIVGINDI GLSGFRQEAI CLVKGSHKTL KLVVKRRSEL GWRPHSWHAT 130 140 150 160 170 180 KFSDSHPELA ASPFTSTSGC PSWSGRHHAS SSSHDLSSSW EQTNLQRTLD HFSSLGSVDS 190 200 210 220 230 240 LDHPSSRLSV AKSNSSIDHL GSHSKRDSAY GSFSTSSSTP DHTLSKADTS SAENILYTVG 250 260 270 280 290 300 LWEAPRQGGR QAQAAGDPQG SEEKLSCFPP RVPGDSGKGP RPEYNAEPKL AAPGRSNFGP 310 320 330 340 350 360 VWYVPDKKKA PSSPPPPPPP LRSDSFAATK SHEKAQGPVF SEAAAAQHFT ALAQAQPRGD 370 380 390 400 410 420 RRPELTDRPW RSAHPGSLGK GSGGPGCPQE AHADGSWPPS KDGASSRLQA SLSSSDVRFP 430 440 450 460 470 480 QSPHSGRHPP LYSDHSPLCA DSLGQEPGAA SFQNDSPPQV RGLSSCDQKL GSGWQGPRPC 490 500 510 520 530 540 VQGDLQAAQL WAGCWPSDTA LGALESLPPP TVGQSPRHHL PQPEGPPDAR ETGRCYPLDK 550 560 570 580 590 600 GAEGCSAGAQ EPPRASRAEK ASQRLAASIT WADGESSRIC PQETPLLHSL TQEGKRRPES 610 620 630 640 650 660 SPEDSATRPP PFDAHVGKPT RRSDRFATTL RNEIQMHRAK LQKSRSTVAL TAAGEAEDGT 670 680 690 700 710 720 GRWRAGLGGG TQEGPLAGTY KDHLKEAQAR VLRATSFKRR DLDPNPGDLY PESLEHRMGD 730 740 750 760 770 780 PDTVPHFWEA GLAQPPSSTS GGPHPPRIGG RRRFTAEQKL KSYSEPEKMN EVGLTRGYSP 790 800 810 820 830 840 HQHPRTSEDT VGTFADRWKF FEETSKPVPQ RPAQKQALHG IPRDKPERPR TAGRTCEGTE 850 860 870 880 890 900 PWSRTTSLGD SLNAHSAAEK AGTSDLPRRL GTFAEYQASW KEQRKPLEAR SSGRCHSADD 910 920 930 940 950 960 ILDVSLDPQE RPQHVHGRSR SSPSTDHYKQ EASVELRRQA GDPGEPREEL PSAVRAEEGQ 970 980 990 1000 1010 1020 STPRQADAQC REGSPGSQQH PPSQKAPNPP TFSELSHCRG APELPREGRG RAGTLPRDYR 1030 1040 1050 1060 1070 1080 YSEESTPADL GPRAQSPGSP LHARGQDSWP VSSALLSKRP APQRPPPPKR EPRRYRATDG 1090 1100 1110 1120 1130 1140 APADAPVGVL GRPFPTPSPA SLDVYVARLS LSHSPSVFSS AQPQDTPKAT VCERGSQHVS 1150 1160 1170 1180 1190 1200 GDASRPLPEA LLPPKQQHLR LQTATMETSR SPSPQFAPQK LTDKPPLLIQ DEDSTRIERV 1210 1220 1230 1240 1250 1260 MDNNTTVKMV PIKIVHSESQ PEKESRQSLA CPAEPPALPH GLEKDQIKTL STSEQFYSRF 1270 1280 1290 1300 1310 1320 CLYTRQGAEP EAPHRAQPAE PQPLGTQVPP EKDRCTSPPG LSYMKAKEKT VEDLKSEELA 1330 1340 1350 1360 1370 1380 REIVGKDKSL ADILDPSVKI KTTMDLMEGI FPKDEHLLEE AQQRRKLLPK IPSPRSTEER 1390 1400 1410 1420 1430 1440 KEEPSVPAAV SLATNSTYYS TSAPKAELLI KMKDLQEQQE HEEDSGSDLD HDLSVKKQEL 1450 1460 1470 1480 1490 1500 IESISRKLQV LREARESLLE DVQANTVLGA EVEAIVKGVC KPSEFDKFRM FIGDLDKVVN 1510 1520 1530 1540 1550 1560 LLLSLSGRLA RVENALNNLD DGASPGDRQS LLEKQRVLIQ QHEDAKELKE NLDRRERIVF 1570 1580 1590 1600 1610 DILANYLSEE SLADYEHFVK MKSALIIEQR ELEDKIHLGE EQLKCLLDSL QPERGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A new standard nomenclature for proteins related to Apx and Shroom." Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P., Schiaffino M.V., Smith P., Staub O., Hildebrand J.D., Wallingford J.B. BMC Cell Biol. 7:18-18(2006) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
[6]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-1245.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X83543 mRNA. Translation: CAA58534.1. AC002365 Genomic DNA. Translation: AAC32592.1. AC090481 Genomic DNA. No translation available. BC140866 mRNA. Translation: AAI40867.1.
IPI	IPI00015180.
PIR	I37183.
RefSeq	NP_001640.1. NM_001649.2.
UniGene	Hs.567236.
3D structure databases
ProteinModelPortal	Q13796.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13796. 5 interactions.
MINT	MINT-6774089.
STRING	9606.ENSP00000370299.
PTM databases
PhosphoSite	Q13796.
Polymorphism databases
DMDM	2498147.
Proteomic databases
PaxDb	Q13796.
PRIDE	Q13796.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380913; ENSP00000370299; ENSG00000146950.
GeneID	357.
KEGG	hsa:357.
UCSC	uc004csu.1. human.
Organism-specific databases
CTD	357.
GeneCards	GC0XP009714.
HGNC	HGNC:630. SHROOM2.
HPA	HPA051646.
MIM	300103. gene.
neXtProt	NX_Q13796.
PharmGKB	PA24916.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG72784.
HOGENOM	HOG000008235.
HOVERGEN	HBG096290.
InParanoid	Q13796.
OMA	NSSIDHL.
OrthoDB	EOG4FBHS5.
PhylomeDB	Q13796.
Gene expression databases
ArrayExpress	Q13796.
Bgee	Q13796.
CleanEx	HS_SHROOM2.
Genevestigator	Q13796.
GermOnline	ENSG00000146950. Homo sapiens.
Family and domain databases
InterPro	IPR014800. ASD1. IPR014799. ASD2. IPR001478. PDZ. [Graphical view]
Pfam	PF08688. ASD1. 1 hit. PF08687. ASD2. 1 hit. PF00595. PDZ. 1 hit. [Graphical view]
SMART	SM00228. PDZ. 1 hit. [Graphical view]
SUPFAM	SSF50156. PDZ. 1 hit.
PROSITE	PS51306. ASD1. 1 hit. PS51307. ASD2. 1 hit. PS50106. PDZ. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SHROOM2. human.
GenomeRNAi	357.
NextBio	1493.
SOURCE	Search...

Entry information

Entry name

SHRM2_HUMAN

Accession

Primary (citable) accession number: Q13796
Secondary accession number(s): B9EIQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.