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Protein

Ras-associated and pleckstrin homology domains-containing protein 1

Gene

RAPH1

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

Functioni

Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion.

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-associated and pleckstrin homology domains-containing protein 1
Short name:
RAPH1
Alternative name(s):
Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 18 protein
Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 9 protein
Lamellipodin
Proline-rich EVH1 ligand 2
Short name:
PREL-2
Protein RMO1
Gene namesi
Name:RAPH1
Synonyms:ALS2CR18, ALS2CR9, KIAA1681, LPD, PREL2, RMO1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:14436. RAPH1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24749.

Polymorphism and mutation databases

BioMutaiRAPH1.
DMDMi215274220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12501250Ras-associated and pleckstrin homology domains-containing protein 1PRO_0000181352Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei5 – 51PhosphoserineCombined sources
Modified residuei17 – 171PhosphoserineCombined sources
Modified residuei54 – 541PhosphoserineCombined sources
Modified residuei150 – 1501PhosphoserineCombined sources
Modified residuei192 – 1921PhosphoserineCombined sources
Modified residuei203 – 2031PhosphoserineCombined sources
Modified residuei205 – 2051PhosphoserineCombined sources
Modified residuei426 – 4261Phosphotyrosine; by ABL11 Publication
Modified residuei456 – 4561Phosphotyrosine; by ABL11 Publication
Modified residuei610 – 6101PhosphoserineCombined sources
Modified residuei827 – 8271PhosphoserineCombined sources
Modified residuei830 – 8301PhosphothreonineCombined sources
Modified residuei845 – 8451PhosphoserineCombined sources
Modified residuei853 – 8531PhosphoserineCombined sources
Modified residuei894 – 8941PhosphoserineCombined sources
Modified residuei965 – 9651PhosphoserineCombined sources
Modified residuei974 – 9741PhosphothreonineCombined sources
Modified residuei996 – 9961PhosphoserineCombined sources
Modified residuei1183 – 11831PhosphoserineCombined sources
Modified residuei1226 – 12261Phosphotyrosine; by ABL11 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ70E73.
MaxQBiQ70E73.
PaxDbiQ70E73.
PRIDEiQ70E73.

PTM databases

iPTMnetiQ70E73.
PhosphoSiteiQ70E73.

Expressioni

Tissue specificityi

Isoform RMO1-RAPH1 is ubiquitously expressed with highest levels in brain, heart, ovary and developing embryo. Isoform RMO1 is widely expressed with highest levels in liver. Low expression in B-cells.2 Publications

Inductioni

Reduced expression in metastatic osteosarcomas compared to primary osteosarcoma tumors. Down-regulated in both breast (43% of tissue samples) and ovarian (25% of tissue samples) cancers.

Gene expression databases

BgeeiQ70E73.
CleanExiHS_RAPH1.
ExpressionAtlasiQ70E73. baseline and differential.
GenevisibleiQ70E73. HS.

Organism-specific databases

HPAiHPA016744.
HPA020027.

Interactioni

Subunit structurei

Interacts with EVL and VASP and targets them to the leading edge (PubMed:15469845). Interacts (via Ras associating and PH domains) with RAC1 (PubMed:18499456).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005332EBI-3940924,EBI-297353
Sh3gl1O3596413EBI-3940924,EBI-1149235From a different organism.
SH3GL2Q999624EBI-3940924,EBI-77938
SH3GL3Q999634EBI-3940924,EBI-473910

Protein-protein interaction databases

BioGridi122380. 14 interactions.
DIPiDIP-61336N.
IntActiQ70E73. 8 interactions.
STRINGi9606.ENSP00000316543.

Structurei

Secondary structure

1
1250
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi255 – 26410Combined sources
Beta strandi270 – 2767Combined sources
Beta strandi282 – 2887Combined sources
Helixi293 – 30412Combined sources
Beta strandi312 – 3187Combined sources
Helixi319 – 3213Combined sources
Beta strandi323 – 3264Combined sources
Helixi333 – 3375Combined sources
Beta strandi348 – 3525Combined sources
Helixi354 – 3563Combined sources
Helixi358 – 3614Combined sources
Helixi363 – 3653Combined sources
Helixi378 – 38912Combined sources
Beta strandi390 – 3934Combined sources
Beta strandi400 – 4067Combined sources
Beta strandi413 – 4219Combined sources
Beta strandi424 – 4274Combined sources
Beta strandi429 – 4335Combined sources
Helixi436 – 4383Combined sources
Beta strandi440 – 4434Combined sources
Helixi445 – 4473Combined sources
Beta strandi449 – 4557Combined sources
Helixi456 – 4594Combined sources
Beta strandi463 – 4653Combined sources
Beta strandi467 – 4715Combined sources
Beta strandi483 – 4864Combined sources
Helixi490 – 50516Combined sources
Helixi507 – 51610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GMVX-ray2.40A/B240-520[»]
4GN1X-ray2.40A/B/C/D266-520[»]
ProteinModelPortaliQ70E73.
SMRiQ70E73. Positions 268-518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini269 – 35587Ras-associatingPROSITE-ProRule annotationAdd
BLAST
Domaini396 – 505110PHPROSITE-ProRule annotationAdd
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.
HOGENOMiHOG000154072.
HOVERGENiHBG089219.
InParanoidiQ70E73.
PhylomeDBiQ70E73.
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]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform RMO1-RAPH1 (identifier: Q70E73-10) [UniParc]FASTAAdd to basket

Also known as: Lamellipodin, RAPH1

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
MEQLSDEEID HGAEEDSDKE DQDLDKMFGA WLGELDKLTQ SLDSDKPMEP
60 70 80 90 100
VKRSPLRQET NMANFSYRFS IYNLNEALNQ GETVDLDALM ADLCSIEQEL
110 120 130 140 150
SSIGSGNSKR QITETKATQK LPVSRHTLKH GTLKGLSSSS NRIAKPSHAS
160 170 180 190 200
YSLDDVTAQL EQASLSMDEA AQQSVLEDTK PLVTNQHRRT ASAGTVSDAE
210 220 230 240 250
VHSISNSSHS SITSAASSMD SLDIDKVTRP QELDLTHQGQ PITEEEQAAK
260 270 280 290 300
LKAEKIRVAL EKIKEAQVKK LVIRVHMSDD SSKTMMVDER QTVRQVLDNL
310 320 330 340 350
MDKSHCGYSL DWSLVETVSE LQMERIFEDH ENLVENLLNW TRDSQNKLIF
360 370 380 390 400
MERIEKYALF KNPQNYLLGK KETAEMADRN KEVLLEECFC GSSVTVPEIE
410 420 430 440 450
GVLWLKDDGK KSWKKRYFLL RASGIYYVPK GKAKVSRDLV CFLQLDHVNV
460 470 480 490 500
YYGQDYRNKY KAPTDYCLVL KHPQIQKKSQ YIKYLCCDDV RTLHQWVNGI
510 520 530 540 550
RIAKYGKQLY MNYQEALKRT ESAYDWTSLS SSSIKSGSSS SSIPESQSNH
560 570 580 590 600
SNQSDSGVSD TQPAGHVRSQ SIVSSVFSEA WKRGTQLEES SKARMESMNR
610 620 630 640 650
PYTSLVPPLS PQPKIVTPYT ASQPSPPLPP PPPPPPPPPP PPPPPPPPLP
660 670 680 690 700
SQSAPSAGSA APMFVKYSTI TRLQNASQHS GALFKPPTPP VMQSQSVKPQ
710 720 730 740 750
ILVPPNGVVP PPPPPPPPPT PGSAMAQLKP APCAPSLPQF SAPPPPLKIH
760 770 780 790 800
QVQHITQVAP PTPPPPPPIP APLPPQAPPK PLVTIPAPTS TKTVAPVVTQ
810 820 830 840 850
AAPPTPTPPV PPAKKQPAFP ASYIPPSPPT PPVPVPPPTL PKQQSFCAKP
860 870 880 890 900
PPSPLSPVPS VVKQIASQFP PPPTPPAMES QPLKPVPANV APQSPPAVKA
910 920 930 940 950
KPKWQPSSIP VPSPDFPPPP PESSLVFPPP PPSPVPAPPP PPPPTASPTP
960 970 980 990 1000
DKSGSPGKKT SKTSSPGGKK PPPTPQRNSS IKSSSGAEHP EPKRPSVDSL
1010 1020 1030 1040 1050
VSKFTPPAES GSPSKETLPP PAAPPKPGKL NLSGVNLPGV LQQGCVSAKA
1060 1070 1080 1090 1100
PVLSGRGKDS VVEFPSPPSD SDFPPPPPET ELPLPPIEIP AVFSGNTSPK
1110 1120 1130 1140 1150
VAVVNPQPQQ WSKMSVKKAP PPTRPKRNDS TRLTQAEISE QPTMATVVPQ
1160 1170 1180 1190 1200
VPTSPKSSLS VQPGFLADLN RTLQRKSITR HGSLSSRMSR AEPTATMDDM
1210 1220 1230 1240 1250
ALPPPPPELL SDQQKAGYGG SHISGYATLR RGPPPAPPKR DQNTKLSRDW
Length:1,250
Mass (Da):135,256
Last modified:November 25, 2008 - v3
Checksum:i1DFB651F945DA3DC
GO
Isoform RMO1 (identifier: Q70E73-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     593-597: ARMES → VTASF
     598-1250: Missing.

Show »
Length:597
Mass (Da):67,456
Checksum:i75BDB66A42373617
GO
Isoform RMO1a (identifier: Q70E73-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     244-244: E → EHAISLRCSSKQAKRHIDFTEEQAELTP
     593-597: ARMES → VTASF
     598-1250: Missing.

Show »
Length:624
Mass (Da):70,534
Checksum:i64CEFFB3F5491DBE
GO
Isoform RMO1b (identifier: Q70E73-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     244-244: E → EHSYLDRETSLLLRNIAGKPSHLLTK
     593-597: ARMES → VTASF
     598-1250: Missing.

Show »
Length:622
Mass (Da):70,301
Checksum:iD4492E1C4D82C239
GO
Isoform RMO1c (identifier: Q70E73-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     593-1250: Missing.

Show »
Length:592
Mass (Da):66,950
Checksum:i07361715124582FF
GO
Isoform RMO1ab (identifier: Q70E73-6) [UniParc]FASTAAdd to basket

Also known as: Lamellipodin-S, Lpd-S

The sequence of this isoform differs from the canonical sequence as follows:
     244-244: E → EHAISLRCSSKQAKRHIDFTEEQAELTPHSYLDRETSLLLRNIAGKPSHLLTK
     593-597: ARMES → VTASF
     598-1250: Missing.

Show »
Length:649
Mass (Da):73,379
Checksum:i3B54297D886F095B
GO
Isoform RMO1ac (identifier: Q70E73-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     244-244: E → EHAISLRCSSKQAKRHIDFTEEQAELTP
     593-1250: Missing.

Show »
Length:619
Mass (Da):70,028
Checksum:i691DBE08F3FC2768
GO
Isoform RMO1bc (identifier: Q70E73-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     244-244: E → EHSYLDRETSLLLRNIAGKPSHLLTK
     593-1250: Missing.

Show »
Length:617
Mass (Da):69,795
Checksum:iE2C239CF09D9A2F4
GO
Isoform RMO1abc (identifier: Q70E73-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     244-244: E → EHAISLRCSSKQAKRHIDFTEEQAELTPHSYLDRETSLLLRNIAGKPSHLLTK
     593-1250: Missing.

Show »
Length:644
Mass (Da):72,874
Checksum:iBF095B6EDA528735
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1081 – 10811E → D in AAS82582 (PubMed:15469845).Curated
Sequence conflicti1081 – 10811E → D in CAE48361 (PubMed:15586368).Curated
Sequence conflicti1081 – 10811E → D in BAB21772 (PubMed:11214970).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti891 – 8911A → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_036009
Natural varianti1228 – 12281T → A in a breast cancer sample; somatic mutation. 1 Publication
VAR_036010

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei244 – 2441E → EHAISLRCSSKQAKRHIDFT EEQAELTP in isoform RMO1a and isoform RMO1ac. CuratedVSP_035784
Alternative sequencei244 – 2441E → EHAISLRCSSKQAKRHIDFT EEQAELTPHSYLDRETSLLL RNIAGKPSHLLTK in isoform RMO1ab and isoform RMO1abc. 2 PublicationsVSP_035785
Alternative sequencei244 – 2441E → EHSYLDRETSLLLRNIAGKP SHLLTK in isoform RMO1b and isoform RMO1bc. CuratedVSP_035786
Alternative sequencei593 – 1250658Missing in isoform RMO1c, isoform RMO1ac, isoform RMO1bc and isoform RMO1abc. 1 PublicationVSP_035787Add
BLAST
Alternative sequencei593 – 5975ARMES → VTASF in isoform RMO1, isoform RMO1a, isoform RMO1b and isoform RMO1ab. 2 PublicationsVSP_035788
Alternative sequencei598 – 1250653Missing in isoform RMO1, isoform RMO1a, isoform RMO1b and isoform RMO1ab. 2 PublicationsVSP_035789Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB053311 mRNA. Translation: BAB69020.1.
AY494951 mRNA. Translation: AAS82582.1.
AY523977 mRNA. Translation: AAS16935.1.
AY523978 mRNA. Translation: AAS16936.1.
AJ584699 mRNA. Translation: CAE48361.1.
AC018891 Genomic DNA. Translation: AAY14676.1.
AB051468 mRNA. Translation: BAB21772.1.
CCDSiCCDS2359.1. [Q70E73-10]
CCDS2360.1. [Q70E73-9]
RefSeqiNP_976241.1. NM_203365.3. [Q70E73-9]
NP_998754.1. NM_213589.2. [Q70E73-10]
UniGeneiHs.471162.

Genome annotation databases

EnsembliENST00000308091; ENSP00000311293; ENSG00000173166. [Q70E73-9]
ENST00000319170; ENSP00000316543; ENSG00000173166. [Q70E73-10]
ENST00000418114; ENSP00000396711; ENSG00000173166. [Q70E73-2]
ENST00000419464; ENSP00000390578; ENSG00000173166. [Q70E73-5]
ENST00000423104; ENSP00000397751; ENSG00000173166. [Q70E73-7]
ENST00000439222; ENSP00000411138; ENSG00000173166. [Q70E73-8]
ENST00000453034; ENSP00000406662; ENSG00000173166. [Q70E73-6]
GeneIDi65059.
KEGGihsa:65059.
UCSCiuc002vad.5. human. [Q70E73-10]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB053311 mRNA. Translation: BAB69020.1.
AY494951 mRNA. Translation: AAS82582.1.
AY523977 mRNA. Translation: AAS16935.1.
AY523978 mRNA. Translation: AAS16936.1.
AJ584699 mRNA. Translation: CAE48361.1.
AC018891 Genomic DNA. Translation: AAY14676.1.
AB051468 mRNA. Translation: BAB21772.1.
CCDSiCCDS2359.1. [Q70E73-10]
CCDS2360.1. [Q70E73-9]
RefSeqiNP_976241.1. NM_203365.3. [Q70E73-9]
NP_998754.1. NM_213589.2. [Q70E73-10]
UniGeneiHs.471162.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GMVX-ray2.40A/B240-520[»]
4GN1X-ray2.40A/B/C/D266-520[»]
ProteinModelPortaliQ70E73.
SMRiQ70E73. Positions 268-518.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122380. 14 interactions.
DIPiDIP-61336N.
IntActiQ70E73. 8 interactions.
STRINGi9606.ENSP00000316543.

PTM databases

iPTMnetiQ70E73.
PhosphoSiteiQ70E73.

Polymorphism and mutation databases

BioMutaiRAPH1.
DMDMi215274220.

Proteomic databases

EPDiQ70E73.
MaxQBiQ70E73.
PaxDbiQ70E73.
PRIDEiQ70E73.

Protocols and materials databases

DNASUi65059.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308091; ENSP00000311293; ENSG00000173166. [Q70E73-9]
ENST00000319170; ENSP00000316543; ENSG00000173166. [Q70E73-10]
ENST00000418114; ENSP00000396711; ENSG00000173166. [Q70E73-2]
ENST00000419464; ENSP00000390578; ENSG00000173166. [Q70E73-5]
ENST00000423104; ENSP00000397751; ENSG00000173166. [Q70E73-7]
ENST00000439222; ENSP00000411138; ENSG00000173166. [Q70E73-8]
ENST00000453034; ENSP00000406662; ENSG00000173166. [Q70E73-6]
GeneIDi65059.
KEGGihsa:65059.
UCSCiuc002vad.5. human. [Q70E73-10]

Organism-specific databases

CTDi65059.
GeneCardsiRAPH1.
HGNCiHGNC:14436. RAPH1.
HPAiHPA016744.
HPA020027.
MIMi609035. gene.
neXtProtiNX_Q70E73.
PharmGKBiPA24749.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3751. Eukaryota.
ENOG410XXC8. LUCA.
GeneTreeiENSGT00550000074537.
HOGENOMiHOG000154072.
HOVERGENiHBG089219.
InParanoidiQ70E73.
PhylomeDBiQ70E73.
TreeFamiTF317511.

Miscellaneous databases

ChiTaRSiRAPH1. human.
GeneWikiiRAPH1.
GenomeRNAii65059.
PROiQ70E73.
SOURCEiSearch...

Gene expression databases

BgeeiQ70E73.
CleanExiHS_RAPH1.
ExpressionAtlasiQ70E73. baseline and differential.
GenevisibleiQ70E73. HS.

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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RMO1AB).
    Tissue: Lymphocyte.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RMO1-RAPH1), INTERACTION WITH EVL AND VASP, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RMO1AB AND RMO1ABC), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Tissue: Osteosarcoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RMO1-RAPH1).
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-1250 (ISOFORM RMO1-RAPH1).
    Tissue: Brain.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-610; SER-827; THR-830; SER-853; SER-894; SER-965 AND THR-974, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "c-Abl, Lamellipodin, and Ena/VASP proteins cooperate in dorsal ruffling of fibroblasts and axonal morphogenesis."
    Michael M., Vehlow A., Navarro C., Krause M.
    Curr. Biol. 20:783-791(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-426; TYR-456 AND TYR-1226.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-17; SER-827; THR-830 AND SER-894, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-150; SER-192; SER-203; SER-205; SER-845; SER-894; SER-996 AND SER-1183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-891 AND ALA-1228.
  14. "CED-10/Rac1 mediates axon guidance by regulating the asymmetric distribution of MIG-10/lamellipodin."
    Quinn C.C., Pfeil D.S., Wadsworth W.G.
    Curr. Biol. 18:808-813(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAC1.

Entry informationi

Entry nameiRAPH1_HUMAN
AccessioniPrimary (citable) accession number: Q70E73
Secondary accession number(s): Q96Q37, Q9C0I2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 25, 2008
Last modified: June 8, 2016
This is version 112 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.