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Protein

Rab11 family-interacting protein 1

Gene

RAB11FIP1

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

Functioni

A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis.4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Rab11 family-interacting protein 1
Short name:
Rab11-FIP1
Alternative name(s):
Rab-coupling protein
Gene namesi
Name:RAB11FIP1
Synonyms:RCP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:30265. RAB11FIP1.

Subcellular locationi

Isoform 2 :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1254 – 12541Y → F: Does not abolish the interaction with RAB11A, homooligomerization and subcellular location. Reduces the interaction with RAB4A. 1 Publication
Mutagenesisi1255 – 12551I → E: Abolishes the interaction with RAB11A and RAB4A, homooligomerization and subcellular location. 1 Publication
Mutagenesisi1256 – 12561D → N: Does not abolish the interaction with RAB11A, homooligomerization and subcellular location. Reduces the interaction with RAB4A. 1 Publication

Organism-specific databases

PharmGKBiPA134937501.

Polymorphism and mutation databases

BioMutaiRAB11FIP1.
DMDMi519668675.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12831283Rab11 family-interacting protein 1PRO_0000097304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei184 – 1841PhosphoserineBy similarity
Modified residuei202 – 2021PhosphoserineCombined sources
Modified residuei234 – 2341PhosphoserineBy similarity
Modified residuei300 – 3001PhosphoserineCombined sources
Modified residuei339 – 3391PhosphoserineCombined sources
Modified residuei341 – 3411PhosphoserineBy similarity
Modified residuei343 – 3431PhosphoserineCombined sources
Modified residuei345 – 3451PhosphoserineCombined sources
Modified residuei357 – 3571PhosphoserineCombined sources
Modified residuei382 – 3821PhosphoserineBy similarity
Modified residuei435 – 4351PhosphoserineCombined sources
Modified residuei477 – 4771PhosphoserineCombined sources
Modified residuei545 – 5451PhosphoserineCombined sources
Modified residuei758 – 7581PhosphoserineCombined sources
Modified residuei1135 – 11351PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6WKZ4.
MaxQBiQ6WKZ4.
PaxDbiQ6WKZ4.
PRIDEiQ6WKZ4.

PTM databases

iPTMnetiQ6WKZ4.
PhosphoSiteiQ6WKZ4.

Expressioni

Tissue specificityi

Isoform 2 is expressed in brain, heart, testis, lung, spleen, ovary and small intestine.1 Publication

Gene expression databases

BgeeiQ6WKZ4.
CleanExiHS_RAB11FIP1.
ExpressionAtlasiQ6WKZ4. baseline and differential.
GenevisibleiQ6WKZ4. HS.

Organism-specific databases

HPAiCAB017037.
HPA023904.
HPA024010.
HPA025960.

Interactioni

Subunit structurei

Homooligomer (isoform 2). Isoform 2 interacts with RAB4A, RAB11A, RAB11B and RAB25. According to PubMed:15280022, RAB4A binding to RAB11FIP1 is of very low affinity in vitro and in vivo.5 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi123189. 27 interactions.
IntActiQ6WKZ4. 16 interactions.
STRINGi9606.ENSP00000331342.

Structurei

Secondary structure

1
1283
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1233 – 126533Combined sources
Helixi1267 – 12704Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D0GX-ray2.50C1216-1283[»]
ProteinModelPortaliQ6WKZ4.
SMRiQ6WKZ4. Positions 19-130, 1229-1274.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 108104C2PROSITE-ProRule annotationAdd
BLAST
Domaini1211 – 127363FIP-RBDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1219 – 128365Necessary for interaction with RAB4A and RAB11A, subcellular location and endosomal recyclingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi209 – 21810Poly-Lys
Compositional biasi556 – 60954Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 FIP-RBD domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IGQZ. Eukaryota.
ENOG410Z6B0. LUCA.
GeneTreeiENSGT00530000063203.
HOGENOMiHOG000234700.
InParanoidiQ6WKZ4.
KOiK12484.
OMAiYQSKASD.
OrthoDBiEOG7WQ7SB.
PhylomeDBiQ6WKZ4.
TreeFamiTF326172.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR019018. Rab-bd_FIP-RBD.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF09457. RBD-FIP. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6WKZ4-4) [UniParc]FASTAAdd to basket

Also known as: Rab11-FIP 1B

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
MSLMVSAGRG LGAVWSPTHV QVTVLQARGL RAKGPGGTSD AYAVIQVGKE
60 70 80 90 100
KYATSVSERS LGAPVWREEA TFELPSLLSS GPAAAATLQL TVLHRALLGL
110 120 130 140 150
DKFLGRAEVD LRDLHRDQGR RKTQWYKLKS KPGKKDKERG EIEVDIQFMR
160 170 180 190 200
NNMTASMFDL SMKDKSRNPF GKLKDKIKGK NKDSGSDTAS AIIPSTTPSV
210 220 230 240 250
DSDDESVVKD KKKKSKIKTL LSKSNLQKTP LSQSMSVLPT SKPEKVLLRP
260 270 280 290 300
GDFQSQWDED DNEDESSSAS DVMSHKRTAS TDLKQLNQVN FTLPKKEGLS
310 320 330 340 350
FLGGLRSKND VLSRSNVCIN GNHVYLEQPE AKGEIKDSSP SSSPSPKGFR
360 370 380 390 400
KKHLFSSTEN LAAGSWKEPA EGGGLSSDRQ LSESSTKDSL KSMTLPSYRP
410 420 430 440 450
APLVSGDLRE NMAPANSEAT KEAKESKKPE SRRSSLLSLM TGKKDVAKGS
460 470 480 490 500
EGENPLTVPG REKEGMLMGV KPGEDASGPA EDLVRRSEKD TAAVVSRQGS
510 520 530 540 550
SLNLFEDVQI TEPEAEPESK SEPRPPISSP RAPQTRAVKP RLEVSPEAQP
560 570 580 590 600
TARLPSPTDS PSSLPPLPSS SGQASVPSEL GHGADTQSSE SPSVFSSLSS
610 620 630 640 650
PIAAPISTST PIESWPLVDR GQAKSEGPPL LPKAELQTES LTPVPNSGSS
660 670 680 690 700
ALGSLFKQPS FPANKGTEDS LMGRTRETGT EKNTSSLELE ESLPEQPETG
710 720 730 740 750
RQEEELPRFP CKKQDYSPSS GEAQEVPFAL SLSSDGAVSP VGELAAGGDR
760 770 780 790 800
DLESQAGSLV ESKARDAAEE VAPPLPMGAS VPSIDSMMRK LEEMGLNLRK
810 820 830 840 850
DQKKTKKRVS FSEQLFTEEA VAGAALLVEG HSSCPQELNP AWSVAGNASD
860 870 880 890 900
GEPPESPHAE DSERESVTTP GPATCGAPAS PADHLLLPSQ EESFSEVPMS
910 920 930 940 950
EASSAKDTPL FRMEGEDALV TQYQSKASDH EGLLSDPLSD LQLVSDFKSP
960 970 980 990 1000
IMADLNLSLP SIPEVASDDE RIDQVEDDGD QVEDDGETAK SSTLDIGALS
1010 1020 1030 1040 1050
LGLVVPCPER GKGPSGEADR LVLGEGLCDF RLQAPQASVT APSEQTTEFG
1060 1070 1080 1090 1100
IHKPHLGKSS SLDKQLPGPS GGEEEKPMGN GSPSPPPGTS LDNPVPSPSP
1110 1120 1130 1140 1150
SEIFPVTHSF PSSAHSDTHH TSTAESQKKA TAEGSAGRVE NFGKRKPLLQ
1160 1170 1180 1190 1200
AWVSPSETHP VSAQPGAGTG SAKHRLHPVK PMNAMATKVA NCSLGTATII
1210 1220 1230 1240 1250
SENLNNEVMM KKYSPSDPAF AYAQLTHDEL IQLVLKQKET ISKKEFQVRE
1260 1270 1280
LEDYIDNLLV RVMEETPNIL RIPTQVGKKA GKM
Length:1,283
Mass (Da):137,167
Last modified:June 26, 2013 - v3
Checksum:i19DF0C848435780B
GO
Isoform 2 (identifier: Q6WKZ4-3) [UniParc]FASTAAdd to basket

Also known as: Rab11-FIP 1C

The sequence of this isoform differs from the canonical sequence as follows:
     541-1174: Missing.

Show »
Length:649
Mass (Da):70,983
Checksum:iC291028B31112E01
GO
Isoform 3 (identifier: Q6WKZ4-1) [UniParc]FASTAAdd to basket

Also known as: Rab11-FIP 1A

The sequence of this isoform differs from the canonical sequence as follows:
     1-671: Missing.

Show »
Length:612
Mass (Da):65,217
Checksum:i310263344F395FD4
GO
Isoform 4 (identifier: Q6WKZ4-2) [UniParc]FASTAAdd to basket

Also known as: Rab11-FIP 1H, No Rab11-binding protein 2

The sequence of this isoform differs from the canonical sequence as follows:
     1-148: Missing.
     541-1174: Missing.
     1212-1221: KYSPSDPAFA → VCPLRSWCVR
     1222-1283: Missing.

Show »
Length:439
Mass (Da):47,704
Checksum:i9A54EC6C78C3C3F3
GO
Isoform 5 (identifier: Q6WKZ4-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     116-142: RDQGRRKTQWYKLKSKPGKKDKERGEI → SSLGKSFFKTLKKRAWAIFLRLCLKKN
     143-1283: Missing.

Show »
Length:142
Mass (Da):15,304
Checksum:i6C070166F8160FDF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti330 – 3323EAK → QPT in AAM09571 (PubMed:11786538).Curated
Sequence conflicti353 – 3531H → T in AAM09571 (PubMed:11786538).Curated
Sequence conflicti377 – 3771S → T in AAM09571 (PubMed:11786538).Curated
Sequence conflicti380 – 3812QL → DV in AAM09571 (PubMed:11786538).Curated
Sequence conflicti397 – 3971S → T in AAM09571 (PubMed:11786538).Curated
Sequence conflicti404 – 4041V → I in AAM09571 (PubMed:11786538).Curated
Sequence conflicti411 – 4111N → K in AAM09571 (PubMed:11786538).Curated
Sequence conflicti455 – 4551P → L in AAM09571 (PubMed:11786538).Curated
Sequence conflicti482 – 4821D → G in AAQ18788 (PubMed:16920206).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti622 – 6221Q → K.2 Publications
Corresponds to variant rs7341564 [ dbSNP | Ensembl ].
VAR_069365
Natural varianti651 – 6511A → V.1 Publication
Corresponds to variant rs12541651 [ dbSNP | Ensembl ].
VAR_059714
Natural varianti768 – 7681A → V.
Corresponds to variant rs16887092 [ dbSNP | Ensembl ].
VAR_056977
Natural varianti1185 – 11851M → T.3 Publications
Corresponds to variant rs7817179 [ dbSNP | Ensembl ].
VAR_022447

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 671671Missing in isoform 3. 2 PublicationsVSP_013726Add
BLAST
Alternative sequencei1 – 148148Missing in isoform 4. 1 PublicationVSP_013727Add
BLAST
Alternative sequencei116 – 14227RDQGR…ERGEI → SSLGKSFFKTLKKRAWAIFL RLCLKKN in isoform 5. 1 PublicationVSP_013728Add
BLAST
Alternative sequencei143 – 12831141Missing in isoform 5. 1 PublicationVSP_013729Add
BLAST
Alternative sequencei541 – 1174634Missing in isoform 2 and isoform 4. 3 PublicationsVSP_013730Add
BLAST
Alternative sequencei1212 – 122110KYSPSDPAFA → VCPLRSWCVR in isoform 4. 1 PublicationVSP_013731
Alternative sequencei1222 – 128362Missing in isoform 4. 1 PublicationVSP_013732Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF368294 mRNA. Translation: AAM09571.1.
DQ236342 mRNA. Translation: ABB43161.1.
AY280966 mRNA. Translation: AAQ18784.1.
AY280968 mRNA. Translation: AAQ18786.1.
AY280970 mRNA. Translation: AAQ18788.1.
AK026275 mRNA. Translation: BAB15424.1.
AK122583 mRNA. Translation: BAC56924.1.
AK291781 mRNA. Translation: BAF84470.1.
AC130304 Genomic DNA. No translation available.
BC077720 mRNA. Translation: AAH77720.1.
CCDSiCCDS34881.1. [Q6WKZ4-3]
CCDS34882.1. [Q6WKZ4-4]
RefSeqiNP_001002814.2. NM_001002814.2. [Q6WKZ4-4]
NP_079427.4. NM_025151.4. [Q6WKZ4-3]
UniGeneiHs.191179.

Genome annotation databases

EnsembliENST00000287263; ENSP00000287263; ENSG00000156675. [Q6WKZ4-3]
ENST00000330843; ENSP00000331342; ENSG00000156675. [Q6WKZ4-4]
ENST00000524118; ENSP00000430680; ENSG00000156675. [Q6WKZ4-2]
GeneIDi80223.
KEGGihsa:80223.
UCSCiuc003xkm.3. human. [Q6WKZ4-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF368294 mRNA. Translation: AAM09571.1.
DQ236342 mRNA. Translation: ABB43161.1.
AY280966 mRNA. Translation: AAQ18784.1.
AY280968 mRNA. Translation: AAQ18786.1.
AY280970 mRNA. Translation: AAQ18788.1.
AK026275 mRNA. Translation: BAB15424.1.
AK122583 mRNA. Translation: BAC56924.1.
AK291781 mRNA. Translation: BAF84470.1.
AC130304 Genomic DNA. No translation available.
BC077720 mRNA. Translation: AAH77720.1.
CCDSiCCDS34881.1. [Q6WKZ4-3]
CCDS34882.1. [Q6WKZ4-4]
RefSeqiNP_001002814.2. NM_001002814.2. [Q6WKZ4-4]
NP_079427.4. NM_025151.4. [Q6WKZ4-3]
UniGeneiHs.191179.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D0GX-ray2.50C1216-1283[»]
ProteinModelPortaliQ6WKZ4.
SMRiQ6WKZ4. Positions 19-130, 1229-1274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123189. 27 interactions.
IntActiQ6WKZ4. 16 interactions.
STRINGi9606.ENSP00000331342.

PTM databases

iPTMnetiQ6WKZ4.
PhosphoSiteiQ6WKZ4.

Polymorphism and mutation databases

BioMutaiRAB11FIP1.
DMDMi519668675.

Proteomic databases

EPDiQ6WKZ4.
MaxQBiQ6WKZ4.
PaxDbiQ6WKZ4.
PRIDEiQ6WKZ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000287263; ENSP00000287263; ENSG00000156675. [Q6WKZ4-3]
ENST00000330843; ENSP00000331342; ENSG00000156675. [Q6WKZ4-4]
ENST00000524118; ENSP00000430680; ENSG00000156675. [Q6WKZ4-2]
GeneIDi80223.
KEGGihsa:80223.
UCSCiuc003xkm.3. human. [Q6WKZ4-4]

Organism-specific databases

CTDi80223.
GeneCardsiRAB11FIP1.
HGNCiHGNC:30265. RAB11FIP1.
HPAiCAB017037.
HPA023904.
HPA024010.
HPA025960.
MIMi608737. gene.
neXtProtiNX_Q6WKZ4.
PharmGKBiPA134937501.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGQZ. Eukaryota.
ENOG410Z6B0. LUCA.
GeneTreeiENSGT00530000063203.
HOGENOMiHOG000234700.
InParanoidiQ6WKZ4.
KOiK12484.
OMAiYQSKASD.
OrthoDBiEOG7WQ7SB.
PhylomeDBiQ6WKZ4.
TreeFamiTF326172.

Miscellaneous databases

ChiTaRSiRAB11FIP1. human.
GeneWikiiRAB11FIP1.
GenomeRNAii80223.
PROiQ6WKZ4.
SOURCEiSearch...

Gene expression databases

BgeeiQ6WKZ4.
CleanExiHS_RAB11FIP1.
ExpressionAtlasiQ6WKZ4. baseline and differential.
GenevisibleiQ6WKZ4. HS.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR019018. Rab-bd_FIP-RBD.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF09457. RBD-FIP. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN ENDOSOMAL RECYCLING PROCESS, VARIANT THR-1185, INTERACTION WITH RAB4A AND RAB11A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  2. "The Rab11-FIP1/RCP gene codes for multiple protein transcripts related to the plasma membrane recycling system."
    Jin M., Goldenring J.R.
    Biochim. Biophys. Acta 1759:281-295(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, VARIANTS LYS-622; VAL-651 AND THR-1185.
    Tissue: Gastric antrum.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 603-1283, VARIANTS LYS-622 AND THR-1185.
    Tissue: Placenta and Small intestine.
  4. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2).
    Tissue: Lung and Spleen.
  6. Cited for: INTERACTION WITH RAB11A; RAB11B AND RAB25.
  7. "The novel Rab11-FIP/Rip/RCP family of proteins displays extensive homo- and hetero-interacting abilities."
    Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.
    Biochem. Biophys. Res. Commun. 292:909-915(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "Characterisation of the Rab binding properties of Rab coupling protein (RCP) by site-directed mutagenesis."
    Lindsay A.J., McCaffrey M.W.
    FEBS Lett. 571:86-92(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB4A AND RAB11A, MUTAGENESIS OF TYR-1254; ILE-1255 AND ASP-1256, SUBCELLULAR LOCATION.
  9. Cited for: FUNCTION IN ENDOSOMAL RECYCLING PROCESS, INTERACTION WITH RAB11A, SUBCELLULAR LOCATION.
  10. "Rab coupling protein associates with phagosomes and regulates recycling from the phagosomal compartment."
    Damiani M.T., Pavarotti M., Leiva N., Lindsay A.J., McCaffrey M.W., Colombo M.I.
    Traffic 5:785-797(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHAGOSOME TRAFFICKING AND PHAGOCYTOSIS, SUBCELLULAR LOCATION.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-477; SER-545; SER-758 AND SER-1135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-339; SER-343; SER-345; SER-435 AND SER-545, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRFIP1_HUMAN
AccessioniPrimary (citable) accession number: Q6WKZ4
Secondary accession number(s): J3KNP0
, Q307T1, Q6AZK4, Q6WKZ2, Q6WKZ6, Q86YV4, Q8TDL1, Q9H642
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 26, 2013
Last modified: June 8, 2016
This is version 123 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 8
    Human chromosome 8: 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.