Q6WKZ4 (RFIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rab11 family-interacting protein 1
Short name=Rab11-FIP1

Alternative name(s):
Rab-coupling protein

Gene names

Name:	RAB11FIP1
Synonyms:	RCP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1283 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis. Ref.1 Ref.8 Ref.9
Subunit structure	Homooligomer (isoform 2). Isoform 2 interacts with RAB4A, RAB11A, RAB11B and RAB25. According to Ref.7, RAB4A binding to RAB11FIP1 is of very low affinity in vitro and in vivo. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8
Subcellular location	Recycling endosome. Note: Rab11A rather than Rab4A mediates localization in the endocytic recycling compartment (ERC). Ref.1 Ref.7 Ref.8 Ref.9 Isoform 2: Cytoplasmic vesicle › phagosome membrane. Note: Membrane-bound (isoform 2). Colocalizes with Rab11A at phagosomes (isoform 2). Ref.1 Ref.7 Ref.8 Ref.9
Tissue specificity	Isoform 2 is expressed in brain, heart, testis, lung, spleen, ovary and small intestine. Ref.1
Sequence similarities	Contains 1 C2 domain. Contains 1 FIP-RBD domain.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasmic vesicle Endosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	centrosome Inferred from direct assay. Source: HPA phagocytic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell recycling endosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6WKZ4-4)

Also known as: Rab11-family-interacting protein 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.

Isoform 2 (identifier: Q6WKZ4-3)

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

Isoform 3 (identifier: Q6WKZ4-1)

Also known as: Rab11-family-interacting protein 1A;

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

Isoform 4 (identifier: Q6WKZ4-2)

Also known as: 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.

Isoform 5 (identifier: Q6WKZ4-5)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1283	1283	Rab11 family-interacting protein 1		PRO_0000097304
Regions
	Domain	5 – 108	104	C2
	Domain	1211 – 1273	63	FIP-RBD
	Region	1219 – 1283	65	Necessary for interaction with RAB4A and RAB11A, subcellular location and endosomal recycling
	Compositional bias	209 – 218	10	Poly-Lys
	Compositional bias	556 – 609	54	Ser-rich
Amino acid modifications
	Modified residue	156	1	Phosphoserine Ref.16
	Modified residue	199	1	Phosphoserine Ref.15
	Modified residue	202	1	Phosphoserine Ref.14 Ref.15
	Modified residue	236	1	Phosphoserine Ref.12
	Modified residue	300	1	Phosphoserine Ref.13
	Modified residue	338	1	Phosphoserine Ref.14 Ref.15
	Modified residue	339	1	Phosphoserine Ref.14
	Modified residue	341	1	Phosphoserine Ref.14
	Modified residue	342	1	Phosphoserine Ref.14
	Modified residue	343	1	Phosphoserine Ref.14 Ref.15
	Modified residue	345	1	Phosphoserine Ref.14 Ref.15
	Modified residue	356	1	Phosphoserine By similarity
	Modified residue	357	1	Phosphoserine Ref.10 Ref.16
	Modified residue	382	1	Phosphoserine By similarity
	Modified residue	435	1	Phosphoserine Ref.13 Ref.14
	Modified residue	477	1	Phosphoserine Ref.13 Ref.14
	Modified residue	496	1	Phosphoserine Ref.11
	Modified residue	500	1	Phosphoserine Ref.13
	Modified residue	501	1	Phosphoserine Ref.13
	Modified residue	545	1	Phosphoserine Ref.13 Ref.14 Ref.15 Ref.16
	Modified residue	684	1	Phosphothreonine Ref.13
	Modified residue	685	1	Phosphoserine Ref.13
	Modified residue	686	1	Phosphoserine Ref.13
	Modified residue	692	1	Phosphoserine Ref.13
	Modified residue	754	1	Phosphoserine Ref.13
	Modified residue	758	1	Phosphoserine Ref.13
	Modified residue	1135	1	Phosphoserine Ref.13
Natural variations
	Alternative sequence	1 – 671	671	Missing in isoform 3.		VSP_013726
	Alternative sequence	1 – 148	148	Missing in isoform 4.		VSP_013727
	Alternative sequence	116 – 142	27	RDQGR…ERGEI → SSLGKSFFKTLKKRAWAIFL RLCLKKN in isoform 5.		VSP_013728
	Alternative sequence	143 – 1283	1141	Missing in isoform 5.		VSP_013729
	Alternative sequence	541 – 1174	634	Missing in isoform 2 and isoform 4.		VSP_013730
	Alternative sequence	1212 – 1221	10	KYSPSDPAFA → VCPLRSWCVR in isoform 4.		VSP_013731
	Alternative sequence	1222 – 1283	62	Missing in isoform 4.		VSP_013732
	Natural variant	651	1	V → A. Corresponds to variant rs12541651 [ dbSNP | Ensembl ].		VAR_059714
	Natural variant	768	1	A → V. Corresponds to variant rs16887092 [ dbSNP | Ensembl ].		VAR_056977
	Natural variant	1185	1	M → T. Ref.1 Ref.2 Corresponds to variant rs7817179 [ dbSNP | Ensembl ].		VAR_022447
Experimental info
	Mutagenesis	1254	1	Y → F: Does not abolish the interaction with RAB11A, homooligomerization and subcellular location. Reduces the interaction with RAB4A. Ref.7
	Mutagenesis	1255	1	I → E: Abolishes the interaction with RAB11A and RAB4A, homooligomerization and subcellular location. Ref.7
	Mutagenesis	1256	1	D → N: Does not abolish the interaction with RAB11A, homooligomerization and subcellular location. Reduces the interaction with RAB4A. Ref.7
	Sequence conflict	330 – 332	3	EAK → QPT in AAM09571. Ref.1
	Sequence conflict	353	1	H → T in AAM09571. Ref.1
	Sequence conflict	377	1	S → T in AAM09571. Ref.1
	Sequence conflict	380 – 381	2	QL → DV in AAM09571. Ref.1
	Sequence conflict	397	1	S → T in AAM09571. Ref.1
	Sequence conflict	404	1	V → I in AAM09571. Ref.1
	Sequence conflict	411	1	N → K in AAM09571. Ref.1
	Sequence conflict	455	1	P → L in AAM09571. Ref.1
	Sequence conflict	482	1	D → G in AAQ18788. Ref.2
	Sequence conflict	622	1	K → Q in BAC56924. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Rab11-family-interacting protein 1B) [UniParc]. Last modified May 10, 2005. Version 2. Checksum: CAACD23C611CBB78	FASTA	1,283	137,195
	10 20 30 40 50 60 MSLMVSAGRG LGAVWSPTHV QVTVLQARGL RAKGPGGTSD AYAVIQVGKE KYATSVSERS 70 80 90 100 110 120 LGAPVWREEA TFELPSLLSS GPAAAATLQL TVLHRALLGL DKFLGRAEVD LRDLHRDQGR 130 140 150 160 170 180 RKTQWYKLKS KPGKKDKERG EIEVDIQFMR NNMTASMFDL SMKDKSRNPF GKLKDKIKGK 190 200 210 220 230 240 NKDSGSDTAS AIIPSTTPSV DSDDESVVKD KKKKSKIKTL LSKSNLQKTP LSQSMSVLPT 250 260 270 280 290 300 SKPEKVLLRP GDFQSQWDED DNEDESSSAS DVMSHKRTAS TDLKQLNQVN FTLPKKEGLS 310 320 330 340 350 360 FLGGLRSKND VLSRSNVCIN GNHVYLEQPE AKGEIKDSSP SSSPSPKGFR KKHLFSSTEN 370 380 390 400 410 420 LAAGSWKEPA EGGGLSSDRQ LSESSTKDSL KSMTLPSYRP APLVSGDLRE NMAPANSEAT 430 440 450 460 470 480 KEAKESKKPE SRRSSLLSLM TGKKDVAKGS EGENPLTVPG REKEGMLMGV KPGEDASGPA 490 500 510 520 530 540 EDLVRRSEKD TAAVVSRQGS SLNLFEDVQI TEPEAEPESK SEPRPPISSP RAPQTRAVKP 550 560 570 580 590 600 RLEVSPEAQP TARLPSPTDS PSSLPPLPSS SGQASVPSEL GHGADTQSSE SPSVFSSLSS 610 620 630 640 650 660 PIAAPISTST PIESWPLVDR GKAKSEGPPL LPKAELQTES LTPVPNSGSS VLGSLFKQPS 670 680 690 700 710 720 FPANKGTEDS LMGRTRETGT EKNTSSLELE ESLPEQPETG RQEEELPRFP CKKQDYSPSS 730 740 750 760 770 780 GEAQEVPFAL SLSSDGAVSP VGELAAGGDR DLESQAGSLV ESKARDAAEE VAPPLPMGAS 790 800 810 820 830 840 VPSIDSMMRK LEEMGLNLRK DQKKTKKRVS FSEQLFTEEA VAGAALLVEG HSSCPQELNP 850 860 870 880 890 900 AWSVAGNASD GEPPESPHAE DSERESVTTP GPATCGAPAS PADHLLLPSQ EESFSEVPMS 910 920 930 940 950 960 EASSAKDTPL FRMEGEDALV TQYQSKASDH EGLLSDPLSD LQLVSDFKSP IMADLNLSLP 970 980 990 1000 1010 1020 SIPEVASDDE RIDQVEDDGD QVEDDGETAK SSTLDIGALS LGLVVPCPER GKGPSGEADR 1030 1040 1050 1060 1070 1080 LVLGEGLCDF RLQAPQASVT APSEQTTEFG IHKPHLGKSS SLDKQLPGPS GGEEEKPMGN 1090 1100 1110 1120 1130 1140 GSPSPPPGTS LDNPVPSPSP SEIFPVTHSF PSSAHSDTHH TSTAESQKKA TAEGSAGRVE 1150 1160 1170 1180 1190 1200 NFGKRKPLLQ AWVSPSETHP VSAQPGAGTG SAKHRLHPVK PMNAMATKVA NCSLGTATII 1210 1220 1230 1240 1250 1260 SENLNNEVMM KKYSPSDPAF AYAQLTHDEL IQLVLKQKET ISKKEFQVRE LEDYIDNLLV 1270 1280 RVMEETPNIL RIPTQVGKKA GKM
	Isoform 2 [UniParc]. Checksum: C291028B31112E01	FASTA	649	70,983
	10 20 30 40 50 60 MSLMVSAGRG LGAVWSPTHV QVTVLQARGL RAKGPGGTSD AYAVIQVGKE KYATSVSERS 70 80 90 100 110 120 LGAPVWREEA TFELPSLLSS GPAAAATLQL TVLHRALLGL DKFLGRAEVD LRDLHRDQGR 130 140 150 160 170 180 RKTQWYKLKS KPGKKDKERG EIEVDIQFMR NNMTASMFDL SMKDKSRNPF GKLKDKIKGK 190 200 210 220 230 240 NKDSGSDTAS AIIPSTTPSV DSDDESVVKD KKKKSKIKTL LSKSNLQKTP LSQSMSVLPT 250 260 270 280 290 300 SKPEKVLLRP GDFQSQWDED DNEDESSSAS DVMSHKRTAS TDLKQLNQVN FTLPKKEGLS 310 320 330 340 350 360 FLGGLRSKND VLSRSNVCIN GNHVYLEQPE AKGEIKDSSP SSSPSPKGFR KKHLFSSTEN 370 380 390 400 410 420 LAAGSWKEPA EGGGLSSDRQ LSESSTKDSL KSMTLPSYRP APLVSGDLRE NMAPANSEAT 430 440 450 460 470 480 KEAKESKKPE SRRSSLLSLM TGKKDVAKGS EGENPLTVPG REKEGMLMGV KPGEDASGPA 490 500 510 520 530 540 EDLVRRSEKD TAAVVSRQGS SLNLFEDVQI TEPEAEPESK SEPRPPISSP RAPQTRAVKP 550 560 570 580 590 600 RLHPVKPMNA MATKVANCSL GTATIISENL NNEVMMKKYS PSDPAFAYAQ LTHDELIQLV 610 620 630 640 LKQKETISKK EFQVRELEDY IDNLLVRVME ETPNILRIPT QVGKKAGKM
	Isoform 3 (Rab11-family-interacting protein 1A) [UniParc]. Checksum: 310263344F395FD4	FASTA	612	65,217
	10 20 30 40 50 60 MGRTRETGTE KNTSSLELEE SLPEQPETGR QEEELPRFPC KKQDYSPSSG EAQEVPFALS 70 80 90 100 110 120 LSSDGAVSPV GELAAGGDRD LESQAGSLVE SKARDAAEEV APPLPMGASV PSIDSMMRKL 130 140 150 160 170 180 EEMGLNLRKD QKKTKKRVSF SEQLFTEEAV AGAALLVEGH SSCPQELNPA WSVAGNASDG 190 200 210 220 230 240 EPPESPHAED SERESVTTPG PATCGAPASP ADHLLLPSQE ESFSEVPMSE ASSAKDTPLF 250 260 270 280 290 300 RMEGEDALVT QYQSKASDHE GLLSDPLSDL QLVSDFKSPI MADLNLSLPS IPEVASDDER 310 320 330 340 350 360 IDQVEDDGDQ VEDDGETAKS STLDIGALSL GLVVPCPERG KGPSGEADRL VLGEGLCDFR 370 380 390 400 410 420 LQAPQASVTA PSEQTTEFGI HKPHLGKSSS LDKQLPGPSG GEEEKPMGNG SPSPPPGTSL 430 440 450 460 470 480 DNPVPSPSPS EIFPVTHSFP SSAHSDTHHT STAESQKKAT AEGSAGRVEN FGKRKPLLQA 490 500 510 520 530 540 WVSPSETHPV SAQPGAGTGS AKHRLHPVKP MNAMATKVAN CSLGTATIIS ENLNNEVMMK 550 560 570 580 590 600 KYSPSDPAFA YAQLTHDELI QLVLKQKETI SKKEFQVREL EDYIDNLLVR VMEETPNILR 610 IPTQVGKKAG KM
	Isoform 4 (No Rab11-binding protein 2) [UniParc]. Checksum: 9A54EC6C78C3C3F3	FASTA	439	47,704
	10 20 30 40 50 60 MRNNMTASMF DLSMKDKSRN PFGKLKDKIK GKNKDSGSDT ASAIIPSTTP SVDSDDESVV 70 80 90 100 110 120 KDKKKKSKIK TLLSKSNLQK TPLSQSMSVL PTSKPEKVLL RPGDFQSQWD EDDNEDESSS 130 140 150 160 170 180 ASDVMSHKRT ASTDLKQLNQ VNFTLPKKEG LSFLGGLRSK NDVLSRSNVC INGNHVYLEQ 190 200 210 220 230 240 PEAKGEIKDS SPSSSPSPKG FRKKHLFSST ENLAAGSWKE PAEGGGLSSD RQLSESSTKD 250 260 270 280 290 300 SLKSMTLPSY RPAPLVSGDL RENMAPANSE ATKEAKESKK PESRRSSLLS LMTGKKDVAK 310 320 330 340 350 360 GSEGENPLTV PGREKEGMLM GVKPGEDASG PAEDLVRRSE KDTAAVVSRQ GSSLNLFEDV 370 380 390 400 410 420 QITEPEAEPE SKSEPRPPIS SPRAPQTRAV KPRLHPVKPM NAMATKVANC SLGTATIISE 430 NLNNEVMMKV CPLRSWCVR
	Isoform 5 [UniParc]. Checksum: 6C070166F8160FDF	FASTA	142	15,304
	10 20 30 40 50 60 MSLMVSAGRG LGAVWSPTHV QVTVLQARGL RAKGPGGTSD AYAVIQVGKE KYATSVSERS 70 80 90 100 110 120 LGAPVWREEA TFELPSLLSS GPAAAATLQL TVLHRALLGL DKFLGRAEVD LRDLHSSLGK 130 140 SFFKTLKKRA WAIFLRLCLK KN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein." Lindsay A.J., Hendrick A.G., Cantalupo G., Senic-Matuglia F., Goud B., Bucci C., McCaffrey M.W. J. Biol. Chem. 277:12190-12199(2002) [PubMed: 11786538] [Abstract] 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]	"A multiple-spliced family of human Rab11a-FIP1 proteins." Jin M., Hall J., Goldenring J.R. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), VARIANT 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 603-1283. Tissue: Small intestine.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lung and Spleen.
[5]	"Identification and characterization of a family of Rab11-interacting proteins." Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R., Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R. J. Biol. Chem. 276:39067-39075(2001) [PubMed: 11495908] [Abstract] Cited for: INTERACTION WITH RAB11A; RAB11B AND RAB25.
[6]	"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: 11944901] [Abstract] Cited for: SUBUNIT.
[7]	"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: 15280022] [Abstract] Cited for: INTERACTION WITH RAB4A AND RAB11A, MUTAGENESIS OF TYR-1254; ILE-1255 AND ASP-1256, SUBCELLULAR LOCATION.
[8]	"The RCP-Rab11 complex regulates endocytic protein sorting." Peden A.A., Schonteich E., Chun J., Junutula J.R., Scheller R.H., Prekeris R. Mol. Biol. Cell 15:3530-3541(2004) [PubMed: 15181150] [Abstract] Cited for: FUNCTION IN ENDOSOMAL RECYCLING PROCESS, INTERACTION WITH RAB11A, SUBCELLULAR LOCATION.
[9]	"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: 15355514] [Abstract] Cited for: FUNCTION IN PHAGOSOME TRAFFICKING AND PHAGOCYTOSIS, SUBCELLULAR LOCATION.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-435; SER-477; SER-500; SER-501; SER-545; THR-684; SER-685; SER-686; SER-692; SER-754; SER-758 AND SER-1135, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-338; SER-339; SER-341; SER-342; SER-343; SER-345; SER-435; SER-477 AND SER-545, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-202; SER-338; SER-343; SER-345 AND SER-545, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-357 AND SER-545, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF368294 mRNA. Translation: AAM09571.1. 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. BC077720 mRNA. Translation: AAH77720.1.
IPI	IPI00335140. IPI00419433. IPI00465151. IPI00472256. IPI00556406.
RefSeq	NP_001002814.2. NM_001002814.2. NP_079427.4. NM_025151.4.
UniGene	Hs.191179.
3D structure databases
ProteinModelPortal	Q6WKZ4.
SMR	Q6WKZ4. Positions 14-148, 1243-1275.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6WKZ4. 1 interaction.
STRING	Q6WKZ4.
PTM databases
PhosphoSite	Q6WKZ4.
Polymorphism databases
DMDM	67472130.
Proteomic databases
PRIDE	Q6WKZ4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000330843; ENSP00000331342; ENSG00000156675.
GeneID	80223.
KEGG	hsa:80223.
UCSC	uc003xkl.1. human. uc003xkm.1. human. uc003xkn.1. human. uc003xkp.1. human.
Organism-specific databases
CTD	80223.
GeneCards	GC08M037716.
H-InvDB	HIX0007422.
HGNC	HGNC:30265. RAB11FIP1.
HPA	CAB017037. HPA023904. HPA024010. HPA025960.
MIM	608737. gene.
neXtProt	NX_Q6WKZ4.
PharmGKB	PA134937501.
GenAtlas	Search...
Phylogenomic databases
InParanoid	Q6WKZ4.
OrthoDB	EOG42JNQP.
Gene expression databases
ArrayExpress	Q6WKZ4.
Bgee	Q6WKZ4.
CleanEx	HS_RAB11FIP1.
Genevestigator	Q6WKZ4.
GermOnline	ENSG00000156675. Homo sapiens.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR019018. Rab-bd_FIP-RBD. [Graphical view]
KO	K12484.
Pfam	PF00168. C2. 1 hit. PF09457. RBD-FIP. 1 hit. [Graphical view]
SMART	SM00239. C2. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit.
PROSITE	PS50004. C2. 1 hit. PS51511. FIP_RBD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	70641.
SOURCE	Search...

Entry information

Entry name

RFIP1_HUMAN

Accession

Primary (citable) accession number: Q6WKZ4
Secondary accession number(s): Q6AZK4 , Q6WKZ2, Q6WKZ6, Q86YV4, Q8TDL1, Q9H642

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	May 10, 2005
Last modified:	January 25, 2012
This is version 82 of the entry and version 2 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.