Q0JRZ9 (FCHO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FCH domain only protein 2

Gene names

Name:

FCHO2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	810 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor. Ref.9 Ref.11 Ref.13 Ref.15
Subunit structure	Homodimer; disulfide-linked. May form homotetramer. Interacts with AP2A1. Interacts with EPS15, EPS15R, ITSN1 and ITSN2; recruit those scaffolding proteins which in turn may interact with the adaptor protein complex AP-2 at the plasma membrane. Interacts with DAB2 (via DPF motifs); mediates LDL receptor/LDLR endocytosis. Ref.9 Ref.11 Ref.13 Ref.14 Ref.15
Subcellular location	Membrane › clathrin-coated pit; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2 By similarity. Ref.11 Ref.13
Post-translational modification	Ubiquitinated. Mainly undergoes monoubiquitination but also polyubiquitination By similarity.
Miscellaneous	Deforms liposomes into a range of tubule diameters from 20 to 130 nm in vitro.
Sequence similarities	Belongs to the FCHO family. Contains 1 FCH domain. Contains 1 MUHD (Muniscin C-terminal mu homology domain) domain.
Sequence caution	The sequence AAH14311.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Coated pit Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Disulfide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	clathrin coat assembly Inferred from mutant phenotype Ref.9. Source: UniProtKB clathrin-mediated endocytosis Inferred from mutant phenotype Ref.9Ref.11. Source: UniProtKB membrane invagination Inferred from sequence or structural similarity. Source: UniProtKB protein localization to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	clathrin-coated vesicle Inferred from direct assay Ref.11. Source: UniProtKB coated pit Inferred from direct assay Ref.11. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	phosphatidylinositol-4,5-bisphosphate binding Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylserine binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dab2	P98078	4	EBI-2609756,EBI-1391846	From a different organism.
EPS15	P42566	3	EBI-2609756,EBI-396684

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q0JRZ9-1)

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: Q0JRZ9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     306-373: ECPDADSLNI...PNNSHHTMAS → WSFTVVAQVG...PYWPGWSRTP
     374-810: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q0JRZ9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     200-232: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 810

810

FCH domain only protein 2

PRO_0000266005

Regions

Domain

4 – 85

82

FCH

Domain

542 – 808

267

MUHD

Region

3 – 274

272

Mediates dimerization and binding to membranes enriched in Pi(4,5)-P2 and induces their tubulation

Region

521 – 810

290

Mediates interaction with DAB2, EPS15, EPS15R and ITSN1

Coiled coil

87 – 156

70

Potential

Compositional bias

434 – 519

86

Ser-rich

Amino acid modifications

Modified residue

385

1

Phosphothreonine Ref.8

Modified residue

387

1

Phosphoserine Ref.6 Ref.8

Modified residue

394

1

Phosphoserine Ref.8

Modified residue

403

1

Phosphoserine Ref.6 Ref.8 Ref.12

Modified residue

488

1

Phosphoserine Ref.7 Ref.8

Modified residue

509

1

Phosphoserine By similarity

Modified residue

511

1

Phosphoserine Ref.7

Modified residue

533

1

Phosphoserine Ref.8

Disulfide bond

147

Interchain (with C-273) Ref.15

Disulfide bond

273

Interchain (with C-147) Ref.15

Natural variations

Alternative sequence

200 – 232

33

Missing in isoform 3.

VSP_044812

Alternative sequence

306 – 373

68

ECPDA…HTMAS → WSFTVVAQVGMQWRDLGLLH SPPPRFKRFSSYLSLPSSWN YGAHHHIWLIFCIFSRDRVS PYWPGWSRTP in isoform 2.

VSP_021910

Alternative sequence

374 – 810

437

Missing in isoform 2.

VSP_021911

Natural variant

371

1

M → V.
Corresponds to variant rs185435 [ dbSNP | Ensembl ].

VAR_029636

Experimental info

Mutagenesis

10

1

F → E: Binds preferentially to larger liposomes. Ref.15

Sequence conflict

6

1

F → L in AL831971. Ref.2

Sequence conflict

286

1

K → E in BAG58162. Ref.1

Sequence conflict

439

1

S → P in BAF84471. Ref.1

Sequence conflict

462

1

P → Q in AL831971. Ref.2

Sequence conflict

617

1

D → Y in BAG58162. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

810

Helix Strand Turn

Details...

Helix

5 – 9

5

Helix

17 – 61

45

Beta strand

67 – 69

3

Helix

70 – 72

3

Helix

73 – 118

46

Helix

120 – 156

37

Helix

160 – 244

85

Helix

247 – 258

12

Beta strand

261 – 263

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: 0FCFBC5D814B5242	FASTA	810	88,924
	10 20 30 40 50 60 MVMAYFVENF WGEKNSGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS RSMTKLAKSA 70 80 90 100 110 120 SNYSQLGTFA PVWDVFKTST EKLANCHLDL VRKLQELIKE VQKYGEEQVK SHKKTKEEVA 130 140 150 160 170 180 GTLEAVQTIQ SITQALQKSK ENYNAKCVEQ ERLKKEGATQ REIEKAAVKS KKATDTYKLY 190 200 210 220 230 240 VEKYALAKAD FEQKMTETAQ KFQDIEETHL IHIKEIIGSL SNAIKEIHLQ IGQVHEEFIN 250 260 270 280 290 300 NMANTTVESL IQKFAESKGT GKERPGLIEF EECDTASAVE GIKPRKRKTF ALPGIIKKEK 310 320 330 340 350 360 DAESVECPDA DSLNIPDVDE EGYSIKPETN QNDTKENHFY SSSDSDSEDE EPKKYRIEIK 370 380 390 400 410 420 PMHPNNSHHT MASLDELKVS IGNITLSPAI SRHSPVQMNR NLSNEELTKS KPSAPPNEKG 430 440 450 460 470 480 TSDLLAWDPL FGPSLDSSSS SSLTSSSSAR PTTPLSVGTI VPPPRPASRP KLTSGKLSGI 490 500 510 520 530 540 NEIPRPFSPP VTSNTSPPPA APLARAESSS SISSSASLSA ANTPTVGVSR GPSPVSLGNQ 550 560 570 580 590 600 DTLPVAVALT ESVNAYFKGA DPTKCIVKIT GDMTMSFPSG IIKVFTSNPT PAVLCFRVKN 610 620 630 640 650 660 ISRLEQILPN AQLVFSDPSQ CDSNTKDFWM NMQAVTVYLK KLSEQNPAAS YYNVDVLKYQ 670 680 690 700 710 720 VSSNGIQSTP LNLATYWKCS ASTTDLRVDY KYNPEAMVAP SVLSNIQVVV PVDGGVTNMQ 730 740 750 760 770 780 SLPPAIWNAE QMKAFWKLSS ISEKSENGGS GSLRAKFDLS EGPSKPTTLA VQFLSEGSTL 790 800 810 SGVDFELVGT GYRLSLIKKR FATGRYLADC
	Isoform 2 [UniParc]. Checksum: 070F5C2EE86C95CF	FASTA	375	43,036
	10 20 30 40 50 60 MVMAYFVENF WGEKNSGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS RSMTKLAKSA 70 80 90 100 110 120 SNYSQLGTFA PVWDVFKTST EKLANCHLDL VRKLQELIKE VQKYGEEQVK SHKKTKEEVA 130 140 150 160 170 180 GTLEAVQTIQ SITQALQKSK ENYNAKCVEQ ERLKKEGATQ REIEKAAVKS KKATDTYKLY 190 200 210 220 230 240 VEKYALAKAD FEQKMTETAQ KFQDIEETHL IHIKEIIGSL SNAIKEIHLQ IGQVHEEFIN 250 260 270 280 290 300 NMANTTVESL IQKFAESKGT GKERPGLIEF EECDTASAVE GIKPRKRKTF ALPGIIKKEK 310 320 330 340 350 360 DAESVWSFTV VAQVGMQWRD LGLLHSPPPR FKRFSSYLSL PSSWNYGAHH HIWLIFCIFS 370 RDRVSPYWPG WSRTP
	Isoform 3 [UniParc]. Checksum: D316D1D723C3698A	FASTA	777	85,146
	10 20 30 40 50 60 MVMAYFVENF WGEKNSGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS RSMTKLAKSA 70 80 90 100 110 120 SNYSQLGTFA PVWDVFKTST EKLANCHLDL VRKLQELIKE VQKYGEEQVK SHKKTKEEVA 130 140 150 160 170 180 GTLEAVQTIQ SITQALQKSK ENYNAKCVEQ ERLKKEGATQ REIEKAAVKS KKATDTYKLY 190 200 210 220 230 240 VEKYALAKAD FEQKMTETAQ VHEEFINNMA NTTVESLIQK FAESKGTGKE RPGLIEFEEC 250 260 270 280 290 300 DTASAVEGIK PRKRKTFALP GIIKKEKDAE SVECPDADSL NIPDVDEEGY SIKPETNQND 310 320 330 340 350 360 TKENHFYSSS DSDSEDEEPK KYRIEIKPMH PNNSHHTMAS LDELKVSIGN ITLSPAISRH 370 380 390 400 410 420 SPVQMNRNLS NEELTKSKPS APPNEKGTSD LLAWDPLFGP SLDSSSSSSL TSSSSARPTT 430 440 450 460 470 480 PLSVGTIVPP PRPASRPKLT SGKLSGINEI PRPFSPPVTS NTSPPPAAPL ARAESSSSIS 490 500 510 520 530 540 SSASLSAANT PTVGVSRGPS PVSLGNQDTL PVAVALTESV NAYFKGADPT KCIVKITGDM 550 560 570 580 590 600 TMSFPSGIIK VFTSNPTPAV LCFRVKNISR LEQILPNAQL VFSDPSQCDS NTKDFWMNMQ 610 620 630 640 650 660 AVTVYLKKLS EQNPAASYYN VDVLKYQVSS NGIQSTPLNL ATYWKCSAST TDLRVDYKYN 670 680 690 700 710 720 PEAMVAPSVL SNIQVVVPVD GGVTNMQSLP PAIWNAEQMK AFWKLSSISE KSENGGSGSL 730 740 750 760 770 RAKFDLSEGP SKPTTLAVQF LSEGSTLSGV DFELVGTGYR LSLIKKRFAT GRYLADC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 1 AND 3). Tissue: Brain and Placenta.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skeletal muscle.
[3]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Lung and Urinary bladder.
[5]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387 AND SER-403, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488 AND SER-511, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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 THR-385; SER-387; SER-394; SER-403; SER-488 AND SER-533, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"FCHo proteins are nucleators of clathrin-mediated endocytosis." Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R., McMahon H.T. Science 328:1281-1284(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CLATHRIN-COATED PITS NUCLEATION, INTERACTION WITH EPS15; EPS15R; ITSN1 AND ITSN2.
[10]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Characterization of the EFC/F-BAR domain protein, FCHO2." Uezu A., Umeda K., Tsujita K., Suetsugu S., Takenawa T., Nakanishi H. Genes Cells 16:868-878(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS, INTERACTION WITH EPS15 AND AP2A1, SUBCELLULAR LOCATION.
[12]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, MASS SPECTROMETRY.
[13]	"FCH domain only-2 organizes clathrin-coated structures and interacts with Disabled-2 for low-density lipoprotein receptor endocytosis." Mulkearns E.E., Cooper J.A. Mol. Biol. Cell 23:1330-1342(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DAB2-MEDIATED ENDOCYTOSIS, INTERACTION WITH DAB2, SUBCELLULAR LOCATION.
[14]	"Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning." Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M. Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract] Cited for: LIPID-BINDING, INTERACTION WITH DAB2; EPS15; EPS15R AND ITSN1.
[15]	"Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature." Henne W.M., Kent H.M., Ford M.G., Hegde B.G., Daumke O., Butler P.J., Mittal R., Langen R., Evans P.R., McMahon H.T. Structure 15:839-852(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-274, FUNCTION, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF PHE-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK291782 mRNA. Translation: BAF84471.1.
AK295141 mRNA. Translation: BAG58162.1.
AL831971 mRNA. No translation available.
AC008972 Genomic DNA. No translation available.
AC020893 Genomic DNA. No translation available.
AC020942 Genomic DNA. No translation available.
BC014311 mRNA. Translation: AAH14311.1. Different initiation.
BC137070 mRNA. Translation: AAI37071.1.

IPI

IPI00060416.
IPI00472794.
IPI00929732.

RefSeq

NP_001139504.1. NM_001146032.1.
NP_620137.2. NM_138782.2.

UniGene

Hs.741336.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V0O	X-ray	2.30	A/B/C	3-274	[»]

ProteinModelPortal

Q0JRZ9.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29488N.

IntAct

Q0JRZ9. 9 interactions.

STRING

9606.ENSP00000393776.

PTM databases

PhosphoSite

Q0JRZ9.

Polymorphism databases

DMDM

119369487.

Proteomic databases

PaxDb

Q0JRZ9.

PRIDE

Q0JRZ9.

Protocols and materials databases

DNASU

115548.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000430046; ENSP00000393776; ENSG00000157107.
ENST00000512348; ENSP00000427296; ENSG00000157107.

GeneID

115548.

KEGG

hsa:115548.

UCSC

uc003kcl.3. human.
uc011csk.1. human.
uc011csl.2. human.

Organism-specific databases

CTD

115548.

GeneCards

GC05P072287.

H-InvDB

HIX0004941.

HGNC

HGNC:25180. FCHO2.

HPA

HPA037686.

MIM

613438. gene.

neXtProt

NX_Q0JRZ9.

PharmGKB

PA134911830.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG324072.

HOGENOM

HOG000231544.

HOVERGEN

HBG081524.

InParanoid

Q0JRZ9.

OMA

FNCEGTT.

OrthoDB

EOG4C87S0.

Gene expression databases

ArrayExpress

Q0JRZ9.

Bgee

Q0JRZ9.

CleanEx

HS_FCHO2.

Genevestigator

Q0JRZ9.

Family and domain databases

InterPro

IPR001060. FCH_dom.
IPR018808. Muniscin_C-term_mu_dom.
[Graphical view]

Pfam

PF00611. FCH. 1 hit.
PF10291. muHD. 1 hit.
[Graphical view]

SMART

SM00055. FCH. 1 hit.
[Graphical view]

PROSITE

PS50133. FCH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

FCHO2. human.

EvolutionaryTrace

Q0JRZ9.

GenomeRNAi

115548.

NextBio

79607.

SOURCE

Search...

Entry information

Entry name

FCHO2_HUMAN

Accession

Primary (citable) accession number: Q0JRZ9
Secondary accession number(s): A8K6W7 , B2RNQ9, B4DHK0, E9PG79, Q0JTJ3, Q96CF5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	December 12, 2006
Last modified:	May 29, 2013
This is version 66 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.