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Protein

Erythroid membrane-associated protein

Gene

Ermap

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Possible role as a cell-adhesion or receptor molecule of erythroid cells.

Names & Taxonomyi

Protein namesi
Recommended name:
Erythroid membrane-associated protein
Gene namesi
Name:Ermap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1349816. Ermap.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 246217ExtracellularSequence AnalysisAdd
BLAST
Transmembranei247 – 26721HelicalSequence AnalysisAdd
BLAST
Topological domaini268 – 566299CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytoplasmic vesicle Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 566537Erythroid membrane-associated proteinPRO_0000226089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 ↔ 123PROSITE-ProRule annotation
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9JLN5.
PRIDEiQ9JLN5.

PTM databases

PhosphoSiteiQ9JLN5.

Expressioni

Tissue specificityi

Expressed in spleen and bone marrow.1 Publication

Developmental stagei

First detected at E.11. Expressed in fetal liver at E12.5 and E13.5.1 Publication

Gene expression databases

BgeeiQ9JLN5.
CleanExiMM_ERMAP.
ExpressionAtlasiQ9JLN5. baseline and differential.
GenevisibleiQ9JLN5. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000123426.

Structurei

3D structure databases

ProteinModelPortaliQ9JLN5.
SMRiQ9JLN5. Positions 24-236, 324-503.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 139110Ig-like V-typeAdd
BLAST
Domaini311 – 509199B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG320971.
HOGENOMiHOG000197761.
HOVERGENiHBG050747.
InParanoidiQ9JLN5.
KOiK06712.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
IPR006574. PRY.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00406. IGv. 1 hit.
SM00589. PRY. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JLN5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERPSPCGSW LVGCLFTIAV FQPPVQVLGD AGKVYIAPLR DTANLPCPLF
60 70 80 90 100
LWPNMVLSEM RWYRPGHLPR TQAVHVFRDG QDRDEDLMPE YKGRTALVRD
110 120 130 140 150
AHKESYILQI SNVRLEDRGL YQCQVWVGNS SREDNVTLQV AVLGSDPYIH
160 170 180 190 200
VKGYDAGWIE LLCQSVGWFP KPWTEWRDTT GRALLSLSEV HSLDENGLFR
210 220 230 240 250
TAVSSRIRDN ALGNVSCTIH NEALGQEKTT AMIIGAPERG SLSSPAVALS
260 270 280 290 300
VVLPVLGLLI LLGIWLICKQ KKSKEKLLYE QAMEVENLLE DHAKEKGRLH
310 320 330 340 350
KALKKLRSEL KLKRAAANAG WRRARLHFVA VTLDPDTAHP KLILSEDRRC
360 370 380 390 400
VRLGDRKRPV PDNPERFDFV VSVLGSEYFT TGCHYWEVYV GEKTKWILGV
410 420 430 440 450
CSESVSRKGK VTASPANGHW LVRQSRGNEY EALTSPQTSF RLKESPKCVG
460 470 480 490 500
IFLDYEAGII SFYNVTDKSH IFTFTHSFSS PLRPFFEPCL HDEGKNTAPL
510 520 530 540 550
IICTELQKSE ESIVPKQEGK DRANGDVSLK MNPSLLSPQG SELFLLNDTW
560
PSNLGPALKG LKVPSL
Length:566
Mass (Da):63,512
Last modified:March 7, 2006 - v2
Checksum:i0017069E16D5D112
GO
Isoform 2 (identifier: Q9JLN5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     125-147: VWVGNSSREDNVTLQVAVLGSDP → EFPYTGAQNLHRTKKPLLPLMTN
     148-566: Missing.

Note: No experimental confirmation available.
Show »
Length:147
Mass (Da):16,910
Checksum:iD94BAFF1D0ED3D94
GO
Isoform 3 (identifier: Q9JLN5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     142-143: Missing.

Note: No experimental confirmation available.
Show »
Length:564
Mass (Da):63,300
Checksum:i5A46DF790035C6C3
GO

Sequence cautioni

The sequence AAF31162.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH63257.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE23390.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911Y → S in AAF31162 (PubMed:10721728).Curated
Sequence conflicti180 – 1801T → A in AAF31162 (PubMed:10721728).Curated
Sequence conflicti221 – 2211N → I in AAF31162 (PubMed:10721728).Curated
Sequence conflicti287 – 2871N → S in AAF31162 (PubMed:10721728).Curated
Sequence conflicti374 – 3741L → P in AAF31162 (PubMed:10721728).Curated
Sequence conflicti462 – 4621F → L in BAC25788 (PubMed:16141072).Curated
Sequence conflicti541 – 5411S → C in AAF31162 (PubMed:10721728).Curated
Sequence conflicti554 – 5541L → F in AAF31162 (PubMed:10721728).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei125 – 14723VWVGN…LGSDP → EFPYTGAQNLHRTKKPLLPL MTN in isoform 2. 1 PublicationVSP_017425Add
BLAST
Alternative sequencei142 – 1432Missing in isoform 3. 1 PublicationVSP_017426
Alternative sequencei148 – 566419Missing in isoform 2. 1 PublicationVSP_017427Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF153906 mRNA. Translation: AAF31162.1. Different initiation.
AK028170 mRNA. Translation: BAC25788.1.
AK137510 mRNA. Translation: BAE23390.1. Different initiation.
BC063257 mRNA. Translation: AAH63257.1. Different initiation.
RefSeqiNP_038876.2. NM_013848.2.
UniGeneiMm.290753.

Genome annotation databases

GeneIDi27028.
KEGGimmu:27028.
UCSCiuc008ulh.2. mouse. [Q9JLN5-2]
uc012dke.1. mouse. [Q9JLN5-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF153906 mRNA. Translation: AAF31162.1. Different initiation.
AK028170 mRNA. Translation: BAC25788.1.
AK137510 mRNA. Translation: BAE23390.1. Different initiation.
BC063257 mRNA. Translation: AAH63257.1. Different initiation.
RefSeqiNP_038876.2. NM_013848.2.
UniGeneiMm.290753.

3D structure databases

ProteinModelPortaliQ9JLN5.
SMRiQ9JLN5. Positions 24-236, 324-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000123426.

PTM databases

PhosphoSiteiQ9JLN5.

Proteomic databases

MaxQBiQ9JLN5.
PRIDEiQ9JLN5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi27028.
KEGGimmu:27028.
UCSCiuc008ulh.2. mouse. [Q9JLN5-2]
uc012dke.1. mouse. [Q9JLN5-3]

Organism-specific databases

CTDi114625.
MGIiMGI:1349816. Ermap.

Phylogenomic databases

eggNOGiNOG320971.
HOGENOMiHOG000197761.
HOVERGENiHBG050747.
InParanoidiQ9JLN5.
KOiK06712.

Miscellaneous databases

NextBioi304957.
PROiQ9JLN5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JLN5.
CleanExiMM_ERMAP.
ExpressionAtlasiQ9JLN5. baseline and differential.
GenevisibleiQ9JLN5. MM.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
IPR006574. PRY.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00406. IGv. 1 hit.
SM00589. PRY. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ermap, a gene coding for a novel erythroid specific adhesion/receptor membrane protein."
    Ye T.-Z., Gordon C.T., Lai Y.-H., Fujiwara Y., Peters L.L., Perkins A.C., Chui D.H.K.
    Gene 242:337-345(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: C57BL/6J.
    Tissue: Erythroid cell.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-566 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Bone and Liver.
  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] (ISOFORM 3).
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiERMAP_MOUSE
AccessioniPrimary (citable) accession number: Q9JLN5
Secondary accession number(s): Q3UV82, Q6P4T5, Q8CEH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 7, 2006
Last modified: June 24, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.