O15344 (TRI18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Midline-1
EC=6.3.2.-

Alternative name(s):
Midin
Midline 1 RING finger protein
Putative transcription factor XPRF
RING finger protein 59
Tripartite motif-containing protein 18

Gene names

Name:	MID1
Synonyms:	FXY, RNF59, TRIM18, XPRF

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	667 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. Ref.9 Ref.11
Subunit structure	Homodimer or heterodimer with MID2. Interacts with IGBP1. Ref.12
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › spindle. Note: Microtubule-associated. It is associated with microtubules throughout the cell cycle, co-localizing with cytoplasmic fibers in interphase and with the mitotic spindle and midbodies during mitosis and cytokinesis. Ref.10
Tissue specificity	In the fetus, highest expression found in kidney, followed by brain and lung. Expressed at low levels in fetal liver. In the adult, most abundant in heart, placenta and brain.
Induction	A retroviral element acts as an alternative tissue-specific promoter for this gene. The LTR of an HERV-E element enhances the expression in placenta and embryonic kidney.
Post-translational modification	Phosphorylated on serine and threonine residues. Ref.12 Ref.13 Ref.14
Involvement in disease	Defects in MID1 are the cause of Opitz syndrome type I (OS-I) [MIM:300000]. OS-I is an X-linked recessive disorder characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules. Ref.1 Ref.4 Ref.16 Ref.18
Sequence similarities	Belongs to the TRIM/RBCC family. Contains 2 B box-type zinc fingers. Contains 1 B30.2/SPRY domain. Contains 1 COS domain. Contains 1 fibronectin type-III domain. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	microtubule cytoskeleton organization Traceable author statement. Source: ProtInc pattern specification process Traceable author statement. Source: ProtInc positive regulation of stress-activated MAPK cascade Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Traceable author statement. Source: ProtInc spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin protein ligase binding Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O15344-1)

Also known as: Alpha;

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: O15344-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     553-667: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 667

667

Midline-1

PRO_0000056227

Regions

Domain

320 – 379

60

COS

Domain

380 – 481

102

Fibronectin type-III

Domain

482 – 659

178

B30.2/SPRY

Zinc finger

10 – 60

51

RING-type

Zinc finger

116 – 165

50

B box-type 1

Zinc finger

172 – 212

41

B box-type 2

Coiled coil

205 – 264

60

Potential

Sites

Metal binding

119

1

Zinc 1

Metal binding

122

1

Zinc 1

Metal binding

134

1

Zinc 2

Metal binding

137

1

Zinc 2

Metal binding

142

1

Zinc 1

Metal binding

145

1

Zinc 1

Metal binding

150

1

Zinc 2

Metal binding

159

1

Zinc 2

Amino acid modifications

Modified residue

90

1

Phosphoserine Ref.14

Modified residue

92

1

Phosphoserine Ref.13 Ref.14

Modified residue

96

1

Phosphoserine Ref.14

Modified residue

98

1

Phosphoserine Ref.13 Ref.14

Natural variations

Alternative sequence

553 – 667

115

Missing in isoform 2.

VSP_005735

Natural variant

266

1

C → R in OS-I. Ref.16

VAR_013758

Natural variant

295

1

L → P in OS-I. Ref.18

VAR_025495

Natural variant

391 – 392

2

LC → R in OS-I.

VAR_025496

Natural variant

438

1

Missing in OS-I.

VAR_013759

Natural variant

534

1

V → VFIDSGRHL in OS-I.

VAR_013760

Natural variant

536

1

I → T in OS-I. Ref.16

VAR_013761

Natural variant

626

1

L → P in OS-I. Ref.4
Corresponds to variant rs28934611 [ dbSNP | Ensembl ].

VAR_013762

Experimental info

Sequence conflict

228

1

T → P in AAC32999. Ref.3

Sequence conflict

484

1

Q → P in AAC32998. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

667

Helix Strand Turn

Details...

Beta strand

112 – 114

3

Beta strand

124 – 126

3

Beta strand

132 – 134

3

Turn

135 – 138

4

Beta strand

139 – 141

3

Helix

143 – 149

7

Beta strand

154 – 156

3

Beta strand

185 – 187

3

Turn

188 – 191

4

Beta strand

192 – 194

3

Helix

196 – 200

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 673C5120018BA619	FASTA	667	75,251
	10 20 30 40 50 60 METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCATNESVES ITAFQCPTCR 70 80 90 100 110 120 HVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET RRERAFDANT MTSAEKVLCQ 130 140 150 160 170 180 FCDQDPAQDA VKTCVTCEVS YCDECLKATH PNKKPFTGHR LIEPIPDSHI RGLMCLEHED 190 200 210 220 230 240 EKVNMYCVTD DQLICALCKL VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL 250 260 270 280 290 300 LAKLIQTCQH VEVNASRQEA KLTEECDLLI EIIQQRRQII GTKIKEGKVM RLRKLAQQIA 310 320 330 340 350 360 NCKQCIERSA SLISQAEHSL KENDHARFLQ TAKNITERVS MATASSQVLI PEINLNDTFD 370 380 390 400 410 420 TFALDFSREK KLLECLDYLT APNPPTIREE LCTASYDTIT VHWTSDDEFS VVSYELQYTI 430 440 450 460 470 480 FTGQANVVSL CNSADSWMIV PNIKQNHYTV HGLQSGTKYI FMVKAINQAG SRSSEPGKLK 490 500 510 520 530 540 TNSQPFKLDP KSAHRKLKVS HDNLTVERDE SSSKKSHTPE RFTSQGSYGV AGNVFIDSGR 550 560 570 580 590 600 HYWEVVISGS TWYAIGLAYK SAPKHEWIGK NSASWALCRC NNNWVVRHNS KEIPIEPAPH 610 620 630 640 650 660 LRRVGILLDY DNGSIAFYDA LNSIHLYTFD VAFAQPVCPT FTVWNKCLTI ITGLPIPDHL DCTEQLP
	Isoform 2 (Beta) [UniParc]. Checksum: FD4D4C0EA5915DB2	FASTA	552	62,288
	10 20 30 40 50 60 METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCATNESVES ITAFQCPTCR 70 80 90 100 110 120 HVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET RRERAFDANT MTSAEKVLCQ 130 140 150 160 170 180 FCDQDPAQDA VKTCVTCEVS YCDECLKATH PNKKPFTGHR LIEPIPDSHI RGLMCLEHED 190 200 210 220 230 240 EKVNMYCVTD DQLICALCKL VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL 250 260 270 280 290 300 LAKLIQTCQH VEVNASRQEA KLTEECDLLI EIIQQRRQII GTKIKEGKVM RLRKLAQQIA 310 320 330 340 350 360 NCKQCIERSA SLISQAEHSL KENDHARFLQ TAKNITERVS MATASSQVLI PEINLNDTFD 370 380 390 400 410 420 TFALDFSREK KLLECLDYLT APNPPTIREE LCTASYDTIT VHWTSDDEFS VVSYELQYTI 430 440 450 460 470 480 FTGQANVVSL CNSADSWMIV PNIKQNHYTV HGLQSGTKYI FMVKAINQAG SRSSEPGKLK 490 500 510 520 530 540 TNSQPFKLDP KSAHRKLKVS HDNLTVERDE SSSKKSHTPE RFTSQGSYGV AGNVFIDSGR 550 HYWEVVISGS TW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22." Quaderi N.A., Schweiger S., Gaudenz K., Franco B., Rugarli E.I., Berger W., Feldman G.J., Volta M., Andolfi G., Gilgenkrantz S., Marion R.W., Hennekam R.C.M., Opitz J.M., Muenke M., Ropers H.-H., Ballabio A. Nat. Genet. 17:285-291(1997) [PubMed: 9354791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS OS-I MET-438 DEL AND PHE-ILE-ASP-SER-GLY-ARG-HIS-LEU-534 INS. Tissue: Neuron.
[2]	"The human FXY gene is located within Xp22.3: implications for evolution of the mammalian X chromosome." Perry J., Feather S., Smith A., Palmer S., Ashworth A. Hum. Mol. Genet. 7:299-305(1998) [PubMed: 9425238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[3]	"Characterization and physical mapping in human and mouse of a novel RING finger gene in Xp22." Van den Veyver I.B., Cormier T.A., Jurecic V., Baldini A., Zoghbi H.Y. Genomics 51:251-261(1998) [PubMed: 9722948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal kidney.
[4]	"New mutations in MID1 provide support for loss of function as the cause of X-linked Opitz syndrome." Cox T.C., Allen L.R., Cox L.L., Hopwood B., Goodwin B., Haan E., Suthers G.K. Hum. Mol. Genet. 9:2553-2562(2000) [PubMed: 11030761] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT OS-I PRO-626. Tissue: Brain.
[5]	"The tripartite motif family identifies cell compartments." Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A. EMBO J. 20:2140-2151(2001) [PubMed: 11331580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[6]	"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 2). Tissue: Placenta.
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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 1). Tissue: Skin.
[9]	"Functional characterization of the Opitz syndrome gene product (midin): evidence for homodimerization and association with microtubules throughout the cell cycle." Cainarca S., Messali S., Ballabio A., Meroni G. Hum. Mol. Genet. 8:1387-1396(1999) [PubMed: 10400985] [Abstract] Cited for: FUNCTION.
[10]	"The Opitz syndrome gene product, MID1, associates with microtubules." Schweiger S., Foerster J., Lehmann T., Suckow V., Muller Y.A., Walter G., Davies T., Porter H., van Bokhoven H., Lunt P.W., Traub P., Ropers H.H. Proc. Natl. Acad. Sci. U.S.A. 96:2794-2799(1999) [PubMed: 10077590] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation." Trockenbacher A., Suckow V., Foerster J., Winter J., Krauss S., Ropers H.H., Schneider R., Schweiger S. Nat. Genet. 29:287-294(2001) [PubMed: 11685209] [Abstract] Cited for: FUNCTION.
[12]	"MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, Alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders." Short K.M., Hopwood B., Yi Z., Cox T.C. BMC Cell Biol. 3:1-1(2002) [PubMed: 11806752] [Abstract] Cited for: INTERACTION WITH IGBP1, PHOSPHORYLATION.
[13]	"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-92 AND SER-98, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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-90; SER-92; SER-96 AND SER-98, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-box with a RING." Massiah M.A., Simmons B.N., Short K.M., Cox T.C. J. Mol. Biol. 358:532-545(2006) [PubMed: 16529770] [Abstract] Cited for: STRUCTURE BY NMR OF 87-164.
[16]	"Opitz G/BBB syndrome in Xp22: mutations in the MID1 gene cluster in the carboxy-terminal domain." Gaudenz K., Roessler E., Quaderi N.A., Franco B., Feldman G.J., Gasser D.L., Wittwer B., Horst J., Montini E., Opitz J.M., Ballabio A., Muenke M. Am. J. Hum. Genet. 63:703-710(1998) [PubMed: 9718340] [Abstract] Cited for: VARIANTS OS-I ARG-266 AND THR-536.
[17]	Erratum Gaudenz K., Roessler E., Quaderi N.A., Franco B., Feldman G.J., Gasser D.L., Wittwer B., Horst J., Montini E., Opitz J.M., Ballabio A., Muenke M. Am. J. Hum. Genet. 63:1571-1571(1998)
[18]	"Mild phenotypes in a series of patients with Opitz GBBB syndrome with MID1 mutations." So J., Suckow V., Kijas Z., Kalscheuer V., Moser B., Winter J., Baars M., Firth H., Lunt P., Hamel B.C.J., Meinecke P., Moraine C., Odent S., Schinzel A., van der Smagt J.J., Devriendt K., Albrecht B., Gillessen-Kaesbach G. , van der Burgt I., Petrij F., Faivre L., McGaughran J., McKenzie F., Opitz J.M., Cox T., Schweiger S. Am. J. Med. Genet. A 132:1-7(2005) [PubMed: 15558842] [Abstract] Cited for: VARIANTS OS-I PRO-295 AND 391-LEU-CYS-392 DELINS ARG.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y13667 mRNA. Translation: CAA74018.1.
AF035360 mRNA. Translation: AAB99951.1.
AF041206 mRNA. Translation: AAC32998.1.
AF041207 mRNA. Translation: AAC32999.1.
AF041208 mRNA. Translation: AAC33000.1.
AF041209 mRNA. Translation: AAC33001.1.
AF041210 mRNA. Translation: AAC33002.1.
AF230976 mRNA. Translation: AAG50191.1.
AF230977 mRNA. Translation: AAG50192.1.
AF269101 mRNA. Translation: AAG33130.1.
AK315095 mRNA. Translation: BAG37559.1.
CH471074 Genomic DNA. Translation: EAW98780.1.
BC053626 mRNA. Translation: AAH53626.1.

IPI

IPI00029324.
IPI00219026.

PIR

T09482.

RefSeq

NP_000372.1. NM_000381.3.
NP_001092094.1. NM_001098624.2.
NP_001180206.1. NM_001193277.1.
NP_001180207.1. NM_001193278.1.
NP_001180208.1. NM_001193279.1.
NP_001180209.1. NM_001193280.1.
NP_001180210.1. NM_001193281.1.
NP_150632.1. NM_033290.3.

UniGene

Hs.27695.
Hs.689953.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DQ5	NMR	-	A	168-214	[»]
2FFW	NMR	-	A	87-164	[»]
2JUN	NMR	-	A	114-214	[»]

ProteinModelPortal

O15344.

SMR

O15344. Positions 1-84, 87-214, 376-644.

ModBase

Search...

Protein-protein interaction databases

IntAct

O15344. 12 interactions.

STRING

O15344.

PTM databases

PhosphoSite

O15344.

Proteomic databases

PRIDE

O15344.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000317552; ENSP00000312678; ENSG00000101871.
ENST00000380779; ENSP00000370156; ENSG00000101871.
ENST00000380780; ENSP00000370157; ENSG00000101871.
ENST00000380785; ENSP00000370162; ENSG00000101871.
ENST00000380787; ENSP00000370164; ENSG00000101871.
ENST00000437096; ENSP00000391726; ENSG00000101871.
ENST00000453318; ENSP00000414521; ENSG00000101871.

GeneID

4281.

KEGG

hsa:4281.

UCSC

uc004cte.2. human.
uc004ctm.1. human.

Organism-specific databases

CTD

4281.

GeneCards

GC0XM010373.

H-InvDB

HIX0016649.

HGNC

HGNC:7095. MID1.

HPA

HPA003715.

MIM

300000. phenotype.
300552. gene.

neXtProt

NX_O15344.

Orphanet

2745. Opitz BBB/G syndrome.

PharmGKB

PA30816.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10794.

GeneTree

ENSGT00580000081333.

HOGENOM

HBG447175.

HOVERGEN

HBG056432.

InParanoid

O15344.

OMA

VLCRCNN.

OrthoDB

EOG49S65S.

PhylomeDB

O15344.

Gene expression databases

ArrayExpress

O15344.

Bgee

O15344.

CleanEx

HS_MID1.

Genevestigator

O15344.

GermOnline

ENSG00000101871. Homo sapiens.

Family and domain databases

InterPro

IPR001870. B30.2/SPRY.
IPR003649. Bbox_C.
IPR003879. Butyrophylin.
IPR008985. ConA-like_lec_gl.
IPR017903. COS_domain.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR006574. PRY.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
IPR000315. Znf_B-box.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.

KO

K08285.

Pfam

PF00041. fn3. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]

PRINTS

PR01407. BUTYPHLNCDUF.

SMART

SM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00060. FN3. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.
SSF49265. FN_III-like. 1 hit.

PROSITE

PS50188. B302_SPRY. 1 hit.
PS51262. COS. 1 hit.
PS50853. FN3. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

16837.

SOURCE

Search...

Entry information

Entry name

TRI18_HUMAN

Accession

Primary (citable) accession number: O15344
Secondary accession number(s): B2RCG2, O75361, Q9BZX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 131 of the entry and version 1 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.