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Protein

Amyloid beta A4 precursor protein-binding family B member 1-interacting protein

Gene

Apbb1ip

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

Functioni

Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-MMU-372708. p130Cas linkage to MAPK signaling for integrins.

Names & Taxonomyi

Protein namesi
Recommended name:
Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
Alternative name(s):
APBB1-interacting protein 1
Proline-rich EVH1 ligand 1
Short name:
PREL-1
Proline-rich protein 48
Gene namesi
Name:Apbb1ip
Synonyms:Prel1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1861354. Apbb1ip.

Subcellular locationi

GO - Cellular componenti

  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: MGI
  • focal adhesion Source: UniProtKB-SubCell
  • lamellipodium Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
  • T cell receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 670670Amyloid beta A4 precursor protein-binding family B member 1-interacting proteinPRO_0000181348Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551PhosphoserineCombined sources
Modified residuei532 – 5321PhosphoserineCombined sources
Modified residuei534 – 5341PhosphothreonineCombined sources
Modified residuei537 – 5371PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8R5A3.
MaxQBiQ8R5A3.
PaxDbiQ8R5A3.
PRIDEiQ8R5A3.

PTM databases

iPTMnetiQ8R5A3.
PhosphoSiteiQ8R5A3.

Miscellaneous databases

PMAP-CutDBQ8R5A3.

Expressioni

Tissue specificityi

Ubiquitously expressed with high expression in the hematopoietic system.2 Publications

Gene expression databases

BgeeiQ8R5A3.
ExpressionAtlasiQ8R5A3. baseline and differential.
GenevisibleiQ8R5A3. MM.

Interactioni

Subunit structurei

Interacts, through the N-terminal Pro-rich region, with the WW domain of APBB1. Interacts with RAP1A, PFN1, VASP and ENAH.2 Publications

Protein-protein interaction databases

DIPiDIP-29358N.
MINTiMINT-1215604.
STRINGi10090.ENSMUSP00000014290.

Structurei

Secondary structure

1
670
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 116Combined sources
Helixi13 – 2210Combined sources
Beta strandi180 – 1878Combined sources
Beta strandi192 – 1987Combined sources
Helixi203 – 21412Combined sources
Beta strandi222 – 2287Combined sources
Turni229 – 2324Combined sources
Beta strandi233 – 2364Combined sources
Helixi243 – 2475Combined sources
Beta strandi257 – 2626Combined sources
Turni264 – 2674Combined sources
Helixi268 – 2714Combined sources
Helixi273 – 2753Combined sources
Helixi295 – 30612Combined sources
Beta strandi307 – 3104Combined sources
Beta strandi317 – 3237Combined sources
Beta strandi330 – 3378Combined sources
Beta strandi339 – 3446Combined sources
Turni353 – 3553Combined sources
Beta strandi357 – 3615Combined sources
Helixi362 – 3643Combined sources
Beta strandi366 – 3705Combined sources
Helixi373 – 3775Combined sources
Beta strandi380 – 3823Combined sources
Beta strandi384 – 3885Combined sources
Beta strandi400 – 4034Combined sources
Helixi407 – 42216Combined sources
Helixi424 – 43411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TCAX-ray2.35A/B150-437[»]
4KVGX-ray1.65B/D179-437[»]
4W8PX-ray1.50B5-25[»]
ProteinModelPortaliQ8R5A3.
SMRiQ8R5A3. Positions 178-437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini179 – 26688Ras-associatingPROSITE-ProRule annotationAdd
BLAST
Domaini313 – 422110PHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi129 – 14921Pro-richAdd
BLAST
Compositional biasi155 – 1584Poly-Glu
Compositional biasi517 – 635119Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the MRL family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 Ras-associating domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3751. Eukaryota.
ENOG410XXC8. LUCA.
GeneTreeiENSGT00550000074537.
HOGENOMiHOG000033749.
HOVERGENiHBG080806.
InParanoidiQ8R5A3.
KOiK17704.
OMAiKVKYKAP.
OrthoDBiEOG715Q3B.
PhylomeDBiQ8R5A3.
TreeFamiTF317511.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000159. RA_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF00788. RA. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R5A3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGESNEDIDQ MFSTLLGEMD LLTQSLGVDT LPPPDPNPPR EEFNYTVGFK
60 70 80 90 100
DLNESLNALE DQDLDALMAD LVADISEAEQ RTIQAQKESS QNQDRFALLR
110 120 130 140 150
ASDGQGTASG GYGASAAAID VSHHEEALPP PPVEPMLDLL PPPPPPPPPE
160 170 180 190 200
LLSKEEEEAK AKADKIKLAL EKLKEAKVKK LVVKVHMDDS STKSLMVDER
210 220 230 240 250
QLARDVLDNL FEKTHCDCNV DWCLYEIYPE LQIERVFEDH ENVVEVLSDW
260 270 280 290 300
TRDTENKVLF LEKEERYAVF KNPQNFYLDN KGKKENKETN EKMNAKNKEY
310 320 330 340 350
LLEESFCGTS IIVPELEGAL YLKEDGKKSW KRRYFLLRAS GIYYVPKGKT
360 370 380 390 400
KTSRDLACFI QFENVNIYYG IQCKMKYKAP TDHCFVLKHP QIQKESQYIK
410 420 430 440 450
YLCCDDARTL SQWVMGIRIA KYGKTLYDNY QRAVARAGLA SRWTNLGTVG
460 470 480 490 500
TPMPAQPSTV SSGLKTGTSQ PNGQMPQAIP SAGPPLQEAQ TQIETTKDEK
510 520 530 540 550
QGLGNHSPGA TRENHRPKSS LPPPPPPVRR SSDTCGSPAL PSKVKGPGTC
560 570 580 590 600
TFPHPPENFL PPPPPPPPEE DNSGLLPPPP PPPYLEEPPD FVPPPPPPAA
610 620 630 640 650
VEDSALPPPP PPPPCLSQEI TKSSPLPPKK PLVPPKRQEN QGLPGAPGNS
660 670
EQDFMSDLMK ALQKKRGNIP
Length:670
Mass (Da):74,319
Last modified:November 22, 2005 - v2
Checksum:i39EB28E468C479C8
GO

Sequence cautioni

The sequence AAB94880.1 differs from that shown. Reason: Frameshift at positions 348 and 477. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 694ALMA → EFKP in AAB94880 (PubMed:9407065).Curated
Sequence conflicti127 – 1271A → D in AAH03991 (PubMed:15489334).Curated
Sequence conflicti141 – 1411Missing (PubMed:15642358).Curated
Sequence conflicti141 – 1411Missing (PubMed:15489334).Curated
Sequence conflicti141 – 1411Missing (PubMed:9407065).Curated
Sequence conflicti142 – 1421Missing (PubMed:15642358).Curated
Sequence conflicti142 – 1421Missing in AAH23110 (PubMed:15489334).Curated
Sequence conflicti142 – 1421Missing (PubMed:9407065).Curated
Sequence conflicti461 – 4611S → P in AAH03991 (PubMed:15489334).Curated
Sequence conflicti549 – 5491T → S in AAH03991 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC003991 mRNA. Translation: AAH03991.1.
BC023110 mRNA. Translation: AAH23110.1.
AK041552 mRNA. Translation: BAC30983.1.
AF020313 mRNA. Translation: AAB94880.1. Frameshift.
CCDSiCCDS38056.1.
RefSeqiNP_062329.2. NM_019456.2.
XP_006498249.1. XM_006498186.2.
XP_011237441.1. XM_011239139.1.
UniGeneiMm.14255.

Genome annotation databases

EnsembliENSMUST00000014290; ENSMUSP00000014290; ENSMUSG00000026786.
GeneIDi54519.
KEGGimmu:54519.
UCSCiuc008inn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC003991 mRNA. Translation: AAH03991.1.
BC023110 mRNA. Translation: AAH23110.1.
AK041552 mRNA. Translation: BAC30983.1.
AF020313 mRNA. Translation: AAB94880.1. Frameshift.
CCDSiCCDS38056.1.
RefSeqiNP_062329.2. NM_019456.2.
XP_006498249.1. XM_006498186.2.
XP_011237441.1. XM_011239139.1.
UniGeneiMm.14255.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TCAX-ray2.35A/B150-437[»]
4KVGX-ray1.65B/D179-437[»]
4W8PX-ray1.50B5-25[»]
ProteinModelPortaliQ8R5A3.
SMRiQ8R5A3. Positions 178-437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29358N.
MINTiMINT-1215604.
STRINGi10090.ENSMUSP00000014290.

PTM databases

iPTMnetiQ8R5A3.
PhosphoSiteiQ8R5A3.

Proteomic databases

EPDiQ8R5A3.
MaxQBiQ8R5A3.
PaxDbiQ8R5A3.
PRIDEiQ8R5A3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000014290; ENSMUSP00000014290; ENSMUSG00000026786.
GeneIDi54519.
KEGGimmu:54519.
UCSCiuc008inn.2. mouse.

Organism-specific databases

CTDi54518.
MGIiMGI:1861354. Apbb1ip.

Phylogenomic databases

eggNOGiKOG3751. Eukaryota.
ENOG410XXC8. LUCA.
GeneTreeiENSGT00550000074537.
HOGENOMiHOG000033749.
HOVERGENiHBG080806.
InParanoidiQ8R5A3.
KOiK17704.
OMAiKVKYKAP.
OrthoDBiEOG715Q3B.
PhylomeDBiQ8R5A3.
TreeFamiTF317511.

Enzyme and pathway databases

ReactomeiR-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-MMU-372708. p130Cas linkage to MAPK signaling for integrins.

Miscellaneous databases

ChiTaRSiApbb1ip. mouse.
PMAP-CutDBQ8R5A3.
PROiQ8R5A3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R5A3.
ExpressionAtlasiQ8R5A3. baseline and differential.
GenevisibleiQ8R5A3. MM.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000159. RA_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF00788. RA. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PREL1 provides a link from Ras signalling to the actin cytoskeleton via Ena/VASP proteins."
    Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.
    FEBS Lett. 579:455-463(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ENAH; VASP AND RAP1A.
    Tissue: Cervix carcinoma.
  2. "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].
    Strain: Czech II and FVB/N.
    Tissue: Mammary tumor.
  3. "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] OF 1-282.
    Strain: C57BL/6J.
    Tissue: Thymus.
  4. "The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled."
    Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F., Russo T., Sudol M.
    J. Biol. Chem. 272:32869-32877(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-670, TISSUE SPECIFICITY, INTERACTION WITH APBB1.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532; THR-534 AND SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Lung and Spleen.

Entry informationi

Entry nameiAB1IP_MOUSE
AccessioniPrimary (citable) accession number: Q8R5A3
Secondary accession number(s): O35329, Q8BRU0, Q99KV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: June 8, 2016
This is version 117 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

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.