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Q6UB35 (C1TM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Monofunctional C1-tetrahydrofolate synthase, mitochondrial

EC=6.3.4.3
Alternative name(s):
Formyltetrahydrofolate synthetase
Gene names
Name:MTHFD1L
Synonyms:FTHFSDC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length978 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism in embryonic an transformed cells complementing thus the enzymatic activities of MTHFD2 By similarity. Ref.5

Catalytic activity

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate. HAMAP-Rule MF_01543

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01543

Subunit structure

Homodimer. Ref.5

Subcellular location

Mitochondrion Ref.1.

Tissue specificity

Detected in most tissues, highest expression found in placenta, thymus and brain. Low expression is found in liver and skeletal muscle. Up-regulated in colon adenocarcinoma. Ref.1 Ref.2

Domain

This monofunctional enzyme consists of two major domains: an N-terminal inactive methylene-THF dehydrogenase and cyclohydrolase domain and an active larger formyl-THF synthetase C-terminal domain. HAMAP-Rule MF_01543

Miscellaneous

May participate in the progression of colorectal cancer by conferring growth advantage. Could be a new molecular target for cancer therapy.

Sequence similarities

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.

Caution

This enzyme lacks methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5) and ethenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) activities. An enzyme performing these two complementary activities has not been found in adult mitochondrial tissues; MTHFD2, which performs these two activities, was found in developing tissues only.

Was originally (Ref.1) thought to be a trifunctional enzyme but only a formyltetrahydrofolate synthetase activity was detected and not a dehydrogenase/cyclohydrogenase activity.

Biophysicochemical properties

Kinetic parameters:

KM=500 µM for THF monoglutamate Ref.5

KM=16 µM for THF triglutamate

KM=3.6 µM for THF pentaglutamate

Sequence caution

The sequence AAH08629.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB15009.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6UB35-1)

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: Q6UB35-2)

The sequence of this isoform differs from the canonical sequence as follows:
     261-275: LHEADIVVLGSPKPE → TESRSVTRLECRRVI
     276-978: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3131Mitochondrion Ref.5
Chain32 – 978947Monofunctional C1-tetrahydrofolate synthase, mitochondrial HAMAP-Rule MF_01543
PRO_0000343177

Regions

Nucleotide binding423 – 4308ATP By similarity
Region31 – 348318Methylenetetrahydrofolate dehydrogenase and cyclohydrolase HAMAP-Rule MF_01543
Region349 – 978630Formyltetrahydrofolate synthetase HAMAP-Rule MF_01543
Compositional bias34 – 429Poly-Gly HAMAP-Rule MF_01543

Amino acid modifications

Modified residue1891N6-acetyllysine; alternate Ref.10
Modified residue1891N6-succinyllysine; alternate By similarity
Modified residue5961N6-succinyllysine By similarity

Natural variations

Alternative sequence261 – 27515LHEAD…SPKPE → TESRSVTRLECRRVI in isoform 2.
VSP_034565
Alternative sequence276 – 978703Missing in isoform 2.
VSP_034566
Natural variant4441L → R in a colorectal cancer sample; somatic mutation. Ref.12
VAR_044346

Experimental info

Sequence conflict791I → V in AAI10320. Ref.7
Sequence conflict8701R → M in BAB15009. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 7D655CD8D2503378

FASTA978105,790
        10         20         30         40         50         60 
MGTRLPLVLR QLRRPPQPPG PPRRLRVPCR ASSGGGGGGG GGREGLLGQR RPQDGQARSS 

        70         80         90        100        110        120 
CSPGGRTPAA RDSIVREVIQ NSKEVLSLLQ EKNPAFKPVL AIIQAGDDNL MQEINQNLAE 

       130        140        150        160        170        180 
EAGLNITHIC LPPDSSEAEI IDEILKINED TRVHGLALQI SENLFSNKVL NALKPEKDVD 

       190        200        210        220        230        240 
GVTDINLGKL VRGDAHECFV SPVAKAVIEL LEKSGVNLDG KKILVVGAHG SLEAALQCLF 

       250        260        270        280        290        300 
QRKGSMTMSI QWKTRQLQSK LHEADIVVLG SPKPEEIPLT WIQPGTTVLN CSHDFLSGKV 

       310        320        330        340        350        360 
GCGSPRIHFG GLIEEDDVIL LAAALRIQNM VSSGRRWLRE QQHRRWRLHC LKLQPLSPVP 

       370        380        390        400        410        420 
SDIEISRGQT PKAVDVLAKE IGLLADEIEI YGKSKAKVRL SVLERLKDQA DGKYVLVAGI 

       430        440        450        460        470        480 
TPTPLGEGKS TVTIGLVQAL TAHLNVNSFA CLRQPSQGPT FGVKGGAAGG GYAQVIPMEE 

       490        500        510        520        530        540 
FNLHLTGDIH AITAANNLLA AAIDTRILHE NTQTDKALYN RLVPLVNGVR EFSEIQLARL 

       550        560        570        580        590        600 
KKLGINKTDP STLTEEEVSK FARLDIDPST ITWQRVLDTN DRFLRKITIG QGNTEKGHYR 

       610        620        630        640        650        660 
QAQFDIAVAS EIMAVLALTD SLADMKARLG RMVVASDKSG QPVTADDLGV TGALTVLMKD 

       670        680        690        700        710        720 
AIKPNLMQTL EGTPVFVHAG PFANIAHGNS SVLADKIALK LVGEEGFVVT EAGFGADIGM 

       730        740        750        760        770        780 
EKFFNIKCRA SGLVPNVVVL VATVRALKMH GGGPSVTAGV PLKKEYTEEN IQLVADGCCN 

       790        800        810        820        830        840 
LQKQIQITQL FGVPVVVALN VFKTDTRAEI DLVCELAKRA GAFDAVPCYH WSVGGKGSVD 

       850        860        870        880        890        900 
LARAVREAAS KRSRFQFLYD VQVPIVDKIR TIAQAVYGAK DIELSPEAQA KIDRYTQQGF 

       910        920        930        940        950        960 
GNLPICMAKT HLSLSHQPDK KGVPRDFILP ISDVRASIGA GFIYPLVGTM STMPGLPTRP 

       970 
CFYDIDLDTE TEQVKGLF 

« Hide

Isoform 2 [UniParc].

Checksum: AA044C3A5C698249
Show »

FASTA27529,804

References

« Hide 'large scale' references
[1]"Human mitochondrial C1-tetrahydrofolate synthase: gene structure, tissue distribution of the mRNA, and immunolocalization in Chinese hamster ovary calls."
Prasannan P., Pike S., Peng K., Shane B., Appling D.R.
J. Biol. Chem. 278:43178-43187(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"A novel mitochondrial C1-tetrahydrofolate synthetase is upregulated in human colon adenocarcinoma."
Sugiura T., Nagano Y., Inoue T., Hirotani K.
Biochem. Biophys. Res. Commun. 315:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Testis.
[3]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Enzymatic characterization of human mitochondrial C1-tetrahydrofolate synthase."
Walkup A.S., Appling D.R.
Arch. Biochem. Biophys. 442:196-205(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-66, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"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] OF 62-978 (ISOFORM 1).
Tissue: Uterus.
[7]"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] OF 79-978 (ISOFORM 1).
Tissue: Cervix, Eye and Muscle.
[8]Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 522-530; 564-575 AND 926-935, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Mammary carcinoma.
[9]"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. expand/collapse author list , 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] OF 591-978 (ISOFORM 1).
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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].
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-444.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY374130 mRNA. Translation: AAQ82696.1.
AY374131 mRNA. Translation: AAQ82697.1.
AB127387 mRNA. Translation: BAD93193.1.
CH471051 Genomic DNA. Translation: EAW47762.1.
AL035086, AL049694, AL133260 Genomic DNA. Translation: CAI42794.1.
AL133260, AL035086, AL049694 Genomic DNA. Translation: CAI95678.1.
AL049694, AL035086, AL133260 Genomic DNA. Translation: CAI95774.1.
AL117452 mRNA. Translation: CAB55934.1.
BC008629 mRNA. Translation: AAH08629.1. Different initiation.
BC017477 mRNA. Translation: AAH17477.2.
BC110319 mRNA. Translation: AAI10320.1.
AK024798 mRNA. Translation: BAB15009.1. Different initiation.
CCDSCCDS5228.1. [Q6UB35-1]
CCDS56457.1. [Q6UB35-2]
PIRT17244.
RefSeqNP_001229696.1. NM_001242767.1.
NP_001229697.1. NM_001242768.1.
NP_001229698.1. NM_001242769.1. [Q6UB35-2]
NP_056255.2. NM_015440.4. [Q6UB35-1]
UniGeneHs.591343.

3D structure databases

ProteinModelPortalQ6UB35.
SMRQ6UB35. Positions 83-295, 359-978.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117409. 12 interactions.
IntActQ6UB35. 2 interactions.
STRING9606.ENSP00000356290.

PTM databases

PhosphoSiteQ6UB35.

Polymorphism databases

DMDM74749360.

Proteomic databases

MaxQBQ6UB35.
PaxDbQ6UB35.
PRIDEQ6UB35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367307; ENSP00000356276; ENSG00000120254. [Q6UB35-2]
ENST00000367321; ENSP00000356290; ENSG00000120254. [Q6UB35-1]
GeneID25902.
KEGGhsa:25902.
UCSCuc003qoa.2. human. [Q6UB35-2]
uc003qob.3. human. [Q6UB35-1]

Organism-specific databases

CTD25902.
GeneCardsGC06P151186.
H-InvDBHIX0008064.
HIX0023219.
HIX0058616.
HGNCHGNC:21055. MTHFD1L.
HPAHPA015006.
MIM611427. gene.
neXtProtNX_Q6UB35.
PharmGKBPA134927803.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0190.
HOVERGENHBG004916.
InParanoidQ6UB35.
KOK13402.
OMAVNGVREF.
OrthoDBEOG76T9QN.
PhylomeDBQ6UB35.
TreeFamTF300623.

Enzyme and pathway databases

BRENDA6.3.4.3. 2681.
UniPathwayUPA00193.

Gene expression databases

ArrayExpressQ6UB35.
BgeeQ6UB35.
CleanExHS_MTHFD1L.
GenevestigatorQ6UB35.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
3.40.50.720. 2 hits.
HAMAPMF_01543. FTHFS.
InterProIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSPR00085. THFDHDRGNASE.
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMTHFD1L. human.
GeneWikiMTHFD1L.
GenomeRNAi25902.
NextBio47370.
PROQ6UB35.
SOURCESearch...

Entry information

Entry nameC1TM_HUMAN
AccessionPrimary (citable) accession number: Q6UB35
Secondary accession number(s): Q2TBF3 expand/collapse secondary AC list , Q8WVW0, Q96HG8, Q9H789, Q9UFU8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM